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env

Gene
env
Protein
Envelope glycoprotein
Organism
Walleye dermal sarcoma virus
Length
1160 amino acids
Function
Transmembrane protein: (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
130.922 kDa
Sequence
MDTPGSLQVIAIISLLLVGGASQPATFLEKALPTDGPSLETIEHKTEMVNTTRSEEQSPVRPSKTRQQLIDETPEICANAWVIRLITEFPTELGNMSQKQKTIAIQVHNTTMTMEETVFSLVSHVNKKNYEIHNVSGICTKYQLVPGNFTCSTRKCISQTKEKRIISTTVKDTYEVYLPFAWSQKPTGGDKYPEPQIGYNTGTGRLNQWNKDEFVIKQCRKKRGKRQITVPNSTLSPTGTTDFTKFTPNPISPNSTALNELEQKTTPIGTEQPFNNEKWQNLIFGNIVTKMDPQCEAELFQQFNISDKTVQVEFKVTSLPGQNISCQAIYNTEHGINIENKNCVISLIKENRKIKAHAYITRTGSYEWYAQQVTSKGIIQEVRNLVTIVECECPIVKPLPQGGIIPLTMPMRVLTNPSPILIHSALKFDLSKFGLSPCSFSPMEWQTYITKPLKRAMHGFEVHQRKKRDLGIGLHSTLNSWWNGANSLGLTVESADRQKYDQKILKVLQNLAVQQRTDVKNQQTLGKALETPIYTITLQLADSLTAAILKHEQQQNVGITCKDIAILTVTQIATYLRDIQHEHLPVWFIEQITNQILLPVGQVIMPEITAPPILNPLIGWNQSVLVIGLTHQLTITTVQQPLYKAANMGNFQDWTPFPPFILANKTHGFSIDCPIMRNSFLCHTLPTPVKLSEWERSTSTIYQTSPQVWITPEGKACLNHRNITVQDRTCLINKPGCFIPKHPWSAGKQTIVPTQYIQQNFVPDTIDTEDNQTRVLQKEMIEAISKAKRDYGVLKQGQIALIRHHEAITTILGQEATYSIKETQALISSIEQEAWYNNLFSWYDGSVWSQLQLIIVVITCTIPLLWVLNTCLFFKLRRAIRRERDNNIVVEYQAQTRGRRTHMTEPITKKQRAKLLRHAKTNRRLPRSLRATPAVSAFEMVTFDPQEETVEINRIDPSHENNDHGGPMNMAPIISADSYALPTPYITIMLDRELLNQGMRKVITLLNDPAREVFNKAYNLVTTNHFTLAYGCDESAGWVNQHAEYMGKPVIVTLAGLVITPVGLAWIPLPQQEPLEKLFMVPNSMPHVTVAMADYHETKEMGKIVKDINNEELLLVKPQLFKWGPEGFFVACPLVIRGVVTGHSLLHIACPATAVQAEGT

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Maedi visna virus (strain 1514 / clone LV1-1KS2)
Length
991 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
115.016 kDa
Sequence
MTSKESKPSRTTWRGMEPPLRETWNQVLQELVKRQQQEEEEQQGLVSGKKKSWVSIDLLGTEGKDIKKVNIWEPCEKWFAQVVWGVLWVLQIVLWGCLMWEMRKGNQCQAEEVIALVSDPGGFQRVQHVETVPVTCVTKNFTQWGCQPEGAYPDPELEYRNISREILEEVYKQDWPWNTYHWPLWQMENMRQWMKENEKEYKERTNKTKEDIDDLVAGRIRGRFCVPYPYALLRCEEWCWYPESINQETGHAEKIKINCTKAKAVSCTEKMPLAAVQRVYWEKEDEESMKFLNIKACNISLRCQDEEKSPGGCVQGYPIPKGAEIIPEAMKYLRGKKSRYGGIKDKNGELKLPLSVRVWVRMANLSGWVNGTPPYWNARINGSTGINGTRWYGVGTLHHLGYNISSNPERGICDFTGELWIGGDKFPYYYKPSWNCSQNWTGHPVWQVFRYLDMTEHMTSRCIQRPERHNITVGNGTITGNCSVTNWDGCNCTRSGNHLYNSTSGGLLVIICRQNSTITGIMGTNTNWTTMWNIYQNCSKCNNSSLDRTGKGTLGTVNDLKCSLPHRNESNKWTCAARTGRKGSQRDSLYIAGRDFWGRVKAKYSCESNLGGLDSMMHQQMLLQRYQVIRVRAYTYGVVEMPQSYMEAQGKNRRSRRNLQRKKRGIGLVIVLAIMAIIAAAGAGLGVANAVQQSYTRTAVQSLANATAAQQEVLEASYAMVQHIAKGIRILEARVARVEALVDRMMVYHELDCWHYQHYCVTSTRSEVANYVNWTRFKDNCTWQQWEEEIEQHEGNLSLLLREAALQVHIAQRDARRIPDAWKAIQEAFNWSSWFSWLKYVPWIIMGIVGLICFRILMCVISMCLQAYKQVKQIRYTQVTVVIEAPVELEEKQKRNGDGTNGCASLEHERRTSHRSFIQIWRATWWAWKTSPWRHNWRTMPYITLLPILVIWQWMEENGWNGENQHKKKKERVDCQDREQMPTLENDYVEL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Ovine maedi visna related virus (strain South Africa)
Length
990 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
114.498 kDa
Sequence
MASSKNMPSRITQKSMEPPLRETWQQVVQEMVMRKQRDEEEKQNLVTGKEKSWVSIDLLGTKQEGKRQKVNIWGPWEKWGIKIVWVMLWVIQLMLWGCLIWEMGKKHSCNAEEVIALVDDPGGFQKVKYVESVPVTCMTKNFTQWGCQPEGAYPDPDLEYRNISQDILEQVYKQEWPWNTYHWPLWQMENMRQWMKENEKEYTSRNNKTKEDIDALLAGKIRGRFCVPYPFALLKCEEWCWYPANINQETGHAQQIKINCTKAKAVSCTEQMPLAAVQRVYWEKEDEEGMKFMNIQACNESQLRCKTSPGGCVQGYPIPVGAEIIPESMKYLRGKKSPYGGIKDKNGELKLPLSVRVWVRMANLSGWVNGTPPYWSARIKGSTGINGTRWYGIGTLHHLGYNISSNPEKGLCNFTKELWIGGDRFQYQYKPSWNCSQNWTGYPVWHVFRYLDMTEHMTSRCVQRPLRHNITVGNGTITGNCSVTDWEGCNCTRSGNYLYNSTTGGLLVIICRQNSTITGIMGTNTNWTTMWGIYKNCSECKNSTLDRTDNGTLGTVNNINCSLPHYNESNKWTCAARNSKKKRDSLYIAGRDFWGRVKALYSCESNLGGLDGMMHQQMVLQKYQVIKVRAYTYGVVDMPKAYREKNMRNKRSTEISRPRKKRGIGLVIVLAIMAIIAAAGAGLGVANAVQQSYTRTAVQSLANATAAQQNVLEATYAMVQHVAKGVRILEARVARVEAIVDRMMLYHELDCWHYQHYCVTSTRTEVAQYVNWTRYKDNCTWQQWEEEIEQHEANLSLLLKEAALQVQIAQRDAQRIPDVWKALQEAFDWSGWFSWLKYIPWIVVCIVGVICFRLLMCVITMCLQAYRQVREIRYTRVTVVIEAPVDLEEKQREERDGSSGSENLEHEKRTSPRSFIQIWRATVQAWKTSPWGKGWKKILYMTLLPLLTLQIWMEETGWNGDKRCKKKKERVDCQDRESMPAIENEYVELS

Gene
env
Protein
Envelope glycoprotein gp130
Organism
Human spumaretrovirus
Length
989 amino acids
Function
The leader peptide is a component of released, infectious virions and is required for particle budding.
Mass
113.891 kDa
Sequence
MAPPMTLQQWIIWKKMNKAHEALQNTTTVTEQQKEQIILDIQNEEVQPTRRDKFRYLLYTCCATSSRVLAWMFLVCILLIIVLVSCFVTISRIQWNKDIQVLGPVIDWNVTQRAVYQPLQTRRIARSLRMQHPVPKYVEVNMTSIPQGVYYEPHPEPIVVKERVLGLSQILMINSENIANNANLTQEVKKLLTEMVNEEMQSLSDVMIDFEIPLGDPRDQEQYIHRKCYQEFANCYLVKYKEPKPWPKEGLIADQCPLPGYHAGLTYNRQSIWDYYIKVESIRPANWTTKSKYGQARLGSFYIPSSLRQINVSHVLFCSDQLYSKWYNIENTIEQNERFLLNKLNNLTSGTSVLKKRALPKDWSSQGKNALFREINVLDICSKPESVILLNTSYYSFSLWEGDCNFTKDMISQLVPECDGFYNNSKWMHMHPYACRFWRSKKNEKEETKCRDGETKRCLYYPLWDSPESTYDFGYLAYQKNFPSPICIEQQKIRDQDYEVYSLYQERKIASKAYGIDTVLFSLKNFLNYTGTPVNEMPNARAFVGLIDPKFPPSYPNVTREHYTSCNNRKRRSVDNNYAKLRSMGYALTGAVQTLSQISDINDENLQQGIYLLRDHVITLMEATLHDISVMEGMFAVQHLHTHLNHLKTMLLERRIDWTYMSSTWLQQQLQKSDDEMKVIKRIARSLVYYVKQTHSSPTATAWEIGLYYELVIPKHIYLNNWNVVNIGHLVKSAGQLTHVTIAHPYEIINKECVETIYLHLEDCTRQDYVICDVVKIVQPCGNSSDTSDCPVWAEAVKEPFVQVNPLKNGSYLVLASSTDCQIPPYVPSIVTVNETTSCFGLDFKRPLVAEERLSFEPRLPNLQLRLPHLVGIIAKIKGIKIEVTSSGESIKEQIERAKAELLRLDIHEGDTPAWIQQLAAATKDVWPAAASALQGIGNFLSGTAQGIFGTAFSLLGYLKPILIGVGVILLVILIFKIVSWIPTKKKNQ

Gene
env
Protein
Envelope glycoprotein gp130
Organism
Human spumaretrovirus
Length
989 amino acids
Function
The leader peptide is a component of released, infectious virions and is required for particle budding.
Mass
113.891 kDa
Sequence
MAPPMTLQQWIIWKKMNKAHEALQNTTTVTEQQKEQIILDIQNEEVQPTRRDKFRYLLYTCCATSSRVLAWMFLVCILLIIVLVSCFVTISRIQWNKDIQVLGPVIDWNVTQRAVYQPLQTRRIARSLRMQHPVPKYVEVNMTSIPQGVYYEPHPEPIVVKERVLGLSQILMINSENIANNANLTQEVKKLLTEMVNEEMQSLSDVMIDFEIPLGDPRDQEQYIHRKCYQEFANCYLVKYKEPKPWPKEGLIADQCPLPGYHAGLTYNRQSIWDYYIKVESIRPANWTTKSKYGQARLGSFYIPSSLRQINVSHVLFCSDQLYSKWYNIENTIEQNERFLLNKLNNLTSGTSVLKKRALPKDWSSQGKNALFREINVLDICSKPESVILLNTSYYSFSLWEGDCNFTKDMISQLVPECDGFYNNSKWMHMHPYACRFWRSKKNEKEETKCRDGETKRCLYYPLWDSPESTYDFGYLAYQKNFPSPICIEQQKIRDQDYEVYSLYQERKIASKAYGIDTVLFSLKNFLNYTGTPVNEMPNARAFVGLIDPKFPPSYPNVTREHYTSCNNRKRRSVDNNYAKLRSMGYALTGAVQTLSQISDINDENLQQGIYLLRDHVITLMEATLHDISVMEGMFAVQHLHTHLNHLKTMLLERRIDWTYMSSTWLQQQLQKSDDEMKVIKRIARSLVYYVKQTHSSPTATAWEIGLYYELVIPKHIYLNNWNVVNIGHLVKSAGQLTHVTIAHPYEIINKECVETIYLHLEDCTRQDYVICDVVKIVQPCGNSSDTSDCPVWAEAVKEPFVQVNPLKNGSYLVLASSTDCQIPPYVPSIVTVNETTSCFGLDFKRPLVAEERLSFEPRLPNLQLRLPHLVGIIAKIKGIKIEVTSSGESIKEQIERAKAELLRLDIHEGDTPAWIQQLAAATKDVWPAAASALQGIGNFLSGTAQGIFGTAFSLLGYLKPILIGVGVILLVILIFKIVSWIPTKKKNQ

Gene
env
Protein
Envelope glycoprotein gp130
Organism
Simian foamy virus type 1
Length
989 amino acids
Function
The leader peptide is a component of released, infectious virions and is required for particle budding.
Mass
113.705 kDa
Sequence
MAPPMTLEQWLLWKKMSQAHQALENVTTLTEEQKQQVIIDIQHEDVVPTRMDKLKYLAYSCCATSTRVLCWIVLVCVLLLVVFISCFVTMSRIQWNKDIAVFGPVIDWNVSQQAVIQQIRAKRLARSIRVEHATETYVEVNMTSIPQGVLYVPHPEPIILKERILGLSQVMMINSENIANTANLTQETKVLLADMINEEMNDLANQMIDFEIPLGDPRDQKQYQHQKCFQEFAHCYLVKYKTTKGWPSSTVIADQCPLPGNHPTVQYAHQNIWDYYVPFEQIRPEGWNSKSYYEDARIGGFYIPKWLRNNSYTHVLFCSDQIYGKWYNIDLTAQERENLLVRKLINLAKGNSSQLKDRAMPAEWDKQGKADLFRQINTLDVCNRPEMVFLLNSSYYEFSLWEGDCGFTRQNVTQANSLCKDFYNNSKWQKLHPYSCRFWRYKQEKEETKCSNGEKKKCLYYPQWDTPEALYDFGFLAYLNSFPSPICIKNQTIREPEYKISSLYLECMNASDRHGIDSALLALKTFLNFTGQSVNEMPLARAFVGLTDPKFPPTYPNITRESSGCNNNKRKRRSVNNYERLRSMGYALTGAVQTLSQISDINDERLQHGVYLLRDHVVTLMEAALHDVSIMEGMLAIQHVHTHLNHLKTMLLMRKIDWTFIRSDWIQQQLQKTDDEMKLIRRTARSLVYYVTQTSSSPTATSWEIGIYYEIVIPKHIYLNNWQVINVGHLLESAGHLTHVKVKHPYEIINKECSDTQYLHLEECIREDYVICDIVQIVQPCGNATELSDCPVTALKVKTPYIQVSPLKNGSYLVLSSTKDCSIPAYVPSVVTVNETVKCFGVEFHKPLYAETKTSYEPQVPHLKLRLPHLTGIIASLQSLEIEVTSTQENIKDQIERAKAQLLRLDIHEGDFPDWLKQVASATRDVWPAAASFIQGVGNFLSNTAQGIFGSAVSLLFYAKPILIGIGVILLIALLFKIISWLPGKPKKN

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Maedi visna virus (strain 1514 / clone LV1-1KS1)
Length
989 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
114.798 kDa
Sequence
MTSKESKPSRTTWRGMEPPLRETWNQVLQELVKRQQQEEEEQQGLVSGKKKSWVSIDLLGTEGKDIKKVNIWEPCEKWFAQVIWGVLWVLQIVLWGCLMWEMRKGNQCQAEEVIALVSDPGGFQRVQHVETVPVTCVTKNFTQWGCQPEGAYPDPELEYRNISREILEEVYKQDWPWNTYHWPLWQMENMRQWMKENEKEYKERTNKTKEDIDDLVAGRIRGRFCVPYPYALLRCEEWCWYPESINQETGHAEKIKINCTKAKAVSCTEKMPLAAVQRVYWEKEDEESMKFLNIKACNISLRCQDEGKSPGGCVQGYPIPKGAEIIPEAMKYLRGKKSRYGGIKDKNGELKLPLSVRVWVRMANLSGWVNGTPPYWSARVNGSTGINGTRWYGVGTLHHLGYNISSNPERGICDFTGELWIGGDKFPYYYKPSWNCSQNWTGHPVWQVFRYLDMTEHMTSRCIQRPERHNITVGNGTITGNCSVTNWDGCNCTRSGNHLYNSTSGGLLVIICRQNSTITGIMGTNTNWTTMWNIYQNCSKCNNSSLDRTGNGTLGTVNDLKCSLPHRNESNKWTCAARRKGSRRDSLYIAGRDFWGRVKAKYSCESNLGGLDSMMHQQMLLQRYQVIRVRAYTYGVVEMPQSYMEAQGENRRSRRNLQRKKRGIGLVIVLAIMAIIAAAGAGLGVANAVQQSYTRTAVQSLANATAAQQEVLEASYAMVQHIAKGIRILEARVARVEALVDRMMVYHELDCWHYQHYCVTSTRSEVANYVNWTRFKDNCTWQQWEEEIEQHEGNLSLLLREAALQVHIAQRDARRIPDAWKAIQEAFNWSSWFSWLKYIPWIIMGIVGLICFRILMCVISMCLQAYKQVKQIRYTQVTVVIEAPVELEEKQKRNGDGTNGCASLERERRTSHRSFIQIWRATWWAWKTSPWRHSWRTMPYITLLPMLVIWQWMEENGWNGENQHKKKKERVDCQDREQMPTLENDYVEL

Gene
env
Protein
Envelope glycoprotein gp130
Organism
Simian foamy virus (isolate chimpanzee)
Length
988 amino acids
Function
The leader peptide is a component of released, infectious virions and is required for particle budding.
Mass
113.353 kDa
Sequence
MAPPMTLQQWIIWNKMNKAHEALQNSTTVTDQQKEQIILEIQNEEVRPTRKDKIRYLLYTCCATSSRVLAWMLLVCVLLIVVLVSCFLTISRIQWNRDIQVLGPVIDWNVTQRAVYQPLQTRRIARSLRMQHPVPKYIEVNMTSIPQGVYYEPHPEPIVVTERVLGLSQVLMINSENIANNANLTQEVKKLLAEVVNEEMQSLSDVMIDFEIPLGDPRDQEQYIHRKCYQEFAHCYLVKYKTPKSWPTEGLIADQCPLPGYHAGLSYKPQSIWDYYIKVEITRPANWSSQAVYGQARLGSFYVPKGIRQNNYSHVLFCSDQLYSKWYNIENSIEQNEKFLLNKLDNLTTGSSLLKKRALPKEWSSQGKNALFKEINVLDVCSKPELVILLNTSYYSFSLWEGDCNFTKNMISQLVPECEGFYNNSKWMHMHPYACRFWRSKNEKEETKCRPGEKEKCLYYPYQDSLESTYDFGFLAYQKNFPAPICIEQQEIRDKDYEVYSLYQECKLASKVHGIDTVLFSLKNFLNHTGRPVNEMPNARAFVGLVDPKFPPSYPNVTREHYTSCNNRKRRSTDNNYAKLKSMGYALTGAVQTLSQISDINDENLQQGIYLLRDHVITLMEATLHDISVMEGMFAVQHLHTHLNHLKTMLLERRIDWTYMSSAWLQQQLQKSDDEMKVIKRIAKSLVYYVKQTYNSPTATAWEIGLYYELTIPKHVYLNNWNVVNIGHLVQSAGQLTHVTIAHPYEIINKECTETKYLHLKDCRRQDYVICDVVEIVQPCGNSTDTSDCPVWAEAVKEPFVQVNPLKNGSYLVLASSTDCQIPPYVPSIVTVNETTSCYGLNFKKPLVAEERLGFEPRLPNLQLRLPHLVGIIAKIKGLKIEVTSSGESIKDQIERAKAELLRLDIHEGDTPAWIQQLAAATKDVWPAAASALQGIGNFLSGAAHGIFGTAFSLLGYLKPILIGVGVILLIILIFKIVSWIPTKKKSQ

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Maedi visna virus (strain KV1772)
Length
983 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
113.939 kDa
Sequence
MASKESKPSRTTRRGMEPPLRETWNQVLQELVKRQQQEEEEQQGLVSGKKKSWVSIDLLGTEGKDIKKVNIWEPCEKWFAQVVWGVLWVLQIVLWGCLMWEVRKGNQCQAEEVIALVSDPGGFQRVQHVETVPVTCVTKNFTQWGCQPEGAYPDPELEYRNISREILEEVYKQDWPWNTYHWPLWQMENMRQWMKENEKEYKERTNKTKEDIDDLVAGRIRGRFCVPYPYALLRCEEWCWYPESINQETGHAEKIKINCTKAKAVSCTEKMSLAAVQRVYWEKEDEESMKFLNIKACNISLRCQDEGKSPGGCVQGYPIPKGAEIIPEAMKYLRGKKSRYGGIKDKNGELKLPLSVRVWVRMANLSGWVNGTPPYWSARINGSTGINGTRWYGIGTLHHLGCNISSNPERGICNFTGELWIGGDKFPYYYTPSWNCSQNWTGHPVWHVFRYLDMTEHMTSRCIQRPKRHNITVGNGTITGNCSVTNWDGCNCTRSGNHLYNSTSGGLLVIICRQNSTITGIMGTNTNWTTMWNIYQNCSRCNNSSLDRTGSGTLGTVNNLKCSLPHRNESNKWTCKSQRDSYIAGRDFWGKVKAKYSCESNLGGLDSMMHQQMLLQRYQVIRVRAYTYGVVEMPQSYMEAQGENKRSRRNLQRKKRGIGLVIVLAIMAIIAAAGAGLGVANAVQQSYTRTAVQSLANATAAQQEVLEASYAMVQHIAKGIRILEARVARVEALVDRMMVYQELDCWHYQHYCVTSTRSEVANYVNWTRFKDNCTWQQWEEEIEQHEGNLSLLLREAALQVHIAQRDARRIPDAWKAIQEAFNWSSWFSWLKYIPWIIMGIVGLMCFRILMCVISMCLQAYKQVKQIRYTQVTVVIEAPVELEEKQKRNGDGTNGCASLERERRTSHRSFIQIWRATWWAWKTSPWRHNWRTMPYITLLPILVIWQWMEENGWNGENQHKKKKERVDCQDREQMPTLENDYVEL

Gene
env
Protein
Envelope glycoprotein gp130
Organism
Simian foamy virus type 3 (strain LK3)
Length
982 amino acids
Function
The leader peptide is a component of released, infectious virions and is required for particle budding.
Mass
113.314 kDa
Sequence
MAPPMNLQQWLLWKKMNETHLALENISSLTEEQKQQVIIEIQQEEVIPTRMDRVKYLAYACCATSTRVMCWLFLICVLLIIVFVSCFVTVARIQWNRDINVFGPVIDWNVTHQATYQQLKAARLTRSLKVEHPHISYISINMSSIPQGVMYTPHPEPIILKERVLGISQVLMINSENIANVANLSQETKVLLTDMINEELQDLSNQMIDFELPLGDPRDQDQYIHHKCYQEFAHCYLVKYKKPSPWISEGIIVDQCPLPRIHDPNYYKYQPIWDYYLKIQNIRPQGWTSKSYYGTARMGSFYIPTFLRNNTVSHVLFCSDQLYGKWYNIENNIQENEQLLKTKLYNLTTYSKLKARALPKEWNNQGNARLFRSFNPLDVCNRPEAVLLLNTTYFTYSLWEGDCNYTTALIQNLTECRQPDRLKLKHPYACRFWRYKEGQEEVKCLGNEKKKCLYYSEYSSPEAQFDFGFLSYLNAFPGLKYIENQTVREPEYEVYSLYMECMNSAEKYGIDSVLFALKTFLNFTGTPVNEMSTARAFVGLTDPKFPPTYPNITKEQKRCNNLKRRKRSTNIEKLRSMGYSLTGAVQTLSQISDINDERLQQGVSLLRDHVVTLMEAALHDITIMEGMLAIQHVHTHLNHLKTILLMRKIDWTFIKSNWIKEQLQKTEDEMKIIRRTAKSLVYYVTQTSSSTTATSWEIGIYYEITIPKHIYLNNWQVINIGHLVESAGHLTLIRVKHPYEVINKECTYEQYLHLEDCISQDYVICDTVQIVSPCGNSTTTSDCPVTAEKVKEPYVQVSALKNGSYLVLTSRTDCSIPAYVPSIVTVNETVKCFGVEFHKPLYSESKVSFEPQVPHLKLRLPHLVGIIANLQNLEIEVTSTQESIKDQIERAKSQLLRLDIHEGDFPAWIQQLASATRDVWPAAARALQGIGNVLSNTAQGIFGTTVSILSYAKPILIGIGVILLIAFLFKIVSWLPGKKKRN

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Maedi visna virus (strain 1514)
Length
982 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
113.978 kDa
Sequence
MASKESKPSRTTWRDMEPPLRETWNQVLQELVKRQQQEEEEQQGLVSGKKKSWVSIDLLGTEGKDIKKVNIWEPCEKWFAQVVWGVLWVLQIVLWGCLMWEVRKGNQCQAEEVIALVSDPGGFQRVQHVETVPVTCVTKNFTQWGCQPEGAYPDPELEYRNISREILEEVYKQDWPWNTYHWPLWQMENMRQWMKENEKEYKERTNKTKEDIDDLVAGRIRGRFCVPYPYALLRCEEWCWYPESINQETGHAEKIKINCTKAKAVSCTEKMPLAAVQRVYWEKEDEESMKFLNIKACNISLRCQDEGKSPGGCVQGYPIPKGAEIIPEAMKYLRGKKSRYGGIKDKNGELKLPLSVRVWVRMANLSGWVNGTPPYWSARINGSTGINGTRWYGVGTLHHLGYNISSNPEGGICNFTGELWIGGDRFPYYYKPSWNCSQNWTGHPVWHVFRYLDMTEHMTSRCIQRPKRHNITVGNGTITGNCSVTNWDGCNCTRSGNHLYNSTSGGLLVIICRQNSTITGIMGTNTNWTTMWNIYQNCSRCNNSSLDRTGSGTLGTVNNLKCSLPHRNESNKWTCKSQRDSYIAGRDFWGKVKAKYSCESNLGGLDSMMHQQMLLQRYQVIRVRAYTYGVVEMPQSYMEERGENRRSRRNLQRKKRGIGLVIVLAIMAIIAAAGAGLGVANAVQQSYTRTAVQSLANATAAQQEVLEASYAMVQHIAKGIRILEARVARVEALVDMMVYQELDCWHYQHYCVTSTRSEVANYVNWTRFKDNCTWQQWEEEIEQHEGNLSLLLREAALQVHIAQRDARRIPDAWKAIQEAFNWSSWFSWLKYIPWIIMGIVGLMCFRILMCVISMCLQAYKQVKQIRYTQVTVVIEAPVELEEKQKRNGDGTNGCASLEHERRTSHRSFIQIWRATWWAWKTSPWRHNWRTMPYITLLPILVIWQWMEENGWNGENQHKKKKERVDCQDREQMPTLENDYVEL

Gene
env
Protein
Envelope glycoprotein
Organism
Caprine arthritis encephalitis virus (strain Cork)
Length
966 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
110.291 kDa
Sequence
MDAGARYMRLTGKENWVEVTMDGEKERKREGFTAGQQGKYNPQVSKNIGNRNTNDCFAYKGIFLWRISLTMWILLGINMCVSAEDYITLISDPYGFSPIKNVSGVPVTCVTKEFAKWGCQPLGAYPDPEIEYRNVSQEVVKEVYQENWPWNTYHWPLWQMENVRYWLKENMQENQQRKNNTKEGIEELLAGTIRGRFCVPYPFALLKCTKWCWYTAAINNESGKAGKIKINCTEARAVSCTEDMPLASIQRAYWDEKDRESMAFMNIKACDSNLRCQKRPGGCMEGYPIPVGAEIIPESMKYLRGAKSQYGGIKDKNGELKLPLTLRVWVKLANVSEWVNGTPPDWQDRINGSKGINGTLWGELNSMHHLGFALSQNGKWCNYTGEIKLGQETFQYHYKPNWNCTGNWTQYPVWQVIRNLDMVEHMTGECVQRPQRHNITVGNGTITGNCSTTNWDGCNCSRSGNYLYNSSEGGLLLILCRQNSTLTRILGTNTNWTTMWGIYKNCSGCENATLDNTGEGTLGGVANKNCSLPHKNESNKWTCAPRQRDGKTDSLYIAGGKKFWTRIKAQFSCESNIGQLDGMLHQQILLQKYQVIKVRAYTYGVIEMPENYAKTRIINRKKRELSHKRKKRGVGLVIMLVIMAIVAAAGASLGVANAIQQSYTKAAVQTLANATAAQQDVLEATYAMVQHVAKGVRILEARVARVEAITDRIMLYQELDCWHYHQYCITSTKTEVAKYINWTRFKDNCTWQQWERGLQGYDTNLTILLKESAAMTQLAEEQARRIPEVWESLKDVFDWSGWFSWLKYIPIIVVGLLGCILIRAVICVCQPLVEIYRTLSTPTYQRVTVIMETRADVAGENQDFGDGLEESDNSETSERVTVQKAWSRAWELWQNSPWKEPWKRGLLRLLVLPLTMGIWINGWLGEHHKNKKRKGGLETWHKKGTDIGLGQIPVDHLWCYKKSKSL

Gene
env
Protein
Envelope glycoprotein
Organism
Caprine arthritis encephalitis virus (strain 63)
Length
942 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
108.437 kDa
Sequence
MDAGASYMRLTGEENWVEVTMDEEKERKGKDVQQGKYRPQVSKPIINRDTNTSFAYKGIFLWGIQITMWILLWTNMCVRAEDYITLISDPYGFSPIKNVSGVPVTCVTKEFARWGCQPLGAYPDPEIEYRNVSQEIVKEVYQENWPWNTYHWPLWQMENVRYWLKENIAENKKRKNSTKKGIEELLAGTIRGRFCVPYPFALLKCTKWCWYPAEIDQETGRARKIKINCTEARAVSCTEEMPLASIHRAYWDEKDRESMAFMNIRACDSNLRCQKRPGGCVEGYPIPVGANIIPENMKYLRGQKSQYGGIKDKNGELKLPLTVRVWVKLANVSTWVNGTPPYWQNRINGSKGINGTLWGQLSGMHHLGFNLSQTGKWCNYTGKIKIGQETFSYHYKPNWNCTGNWTQHPVWQVMRDLDMVEHMTGECVQRPQRHNITVDRNQTITGNCSVTNWDGCNCSRSGNYLYNSTTGGLLVIICRNNNTITGIMGTNTNWTTMWRIYRNCSGCENATLDRKETGTLGGVANKNCSLPHKNESNKWTCAPRQREGKTDSLYIAGGKKFWTREKAQYSCENNIGELDGMLHQQILLQKYQVIKVRAYTYGVIEMPENYAKTRIINRRKRELSHTRKKRGVGLVIMLVIMAIVAAAGASLGVANAIQQSYTKAAVQTLANATAAQQDALEATYAMVQHVAKGVRILEARVARVEAITDRIMLYQELDCWHYHQYCVTSTRADVAKYINWTRFKDNCTWQQWERELQGYDGNLTMLLRESARQTQLAEEQVRRIPDVWESLKEVFDWSGWFSWLKYIPIIVVGLVGCILIRAVICVCQPLVQIYRTLSTPTYQRVTVIMEKRADVAGENQDFGDGLEESDDSKTDQKVTVQKAWSRAWELWQNSPWKEPWKRSLLKLLILPLTMGIWINGRLGEHLKNKKERVDCETWGKGD

Gene
env
Protein
Envelope glycoprotein
Organism
Bovine immunodeficiency virus (strain R29)
Length
904 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
102.27 kDa
Sequence
MDQDLDGAERGERGGGSEELLQEEINEGRLTAREALQTWINNGEIHPWVLAGMLSMGVGMLLGVYCQLPDTLIWILMFQLCLYWGLGETSRELDKDSWQWVRSVFIIAILGTLTMAGTALADDDQSTLIPNITKIPTKDTEPGCTYPWILILLILAFILGILGIILVLRRSNSEDILAARDTIDWWLSANQEIPPKFAFPIILISSPLAGIIGYYVMERHLEIFKKGCQICGSLSSMWGMLLEEIGRWLARREWNVSRVMVILLISFSWGMYVNRVNASGSHVAMVTSPPGYRIVNDTSQAPWYCFSSAPIPTCSSSQWGDKYFEEKINETLVKQVYEQAAKHSRATWIEPDLLEEAVYELALLSANDSRQVVVENGTDVCSSQNSSTNKGHPMTLLKLRGQVSETWIGNSSLQFCVQWPYVLVGLNNSDSNISFNSGDWIATNCMHPITLNKSAQDLGKNFPRLTFLDGQLSQLKNTLCGHNTNCLKFGNKSFSTNSLILCQDNPIGNDTFYSLSHSFSKQASARWILVKVPSYGFVVVNDTDTPPSLRIRKPRAVGLAIFLLVLAIMAITSSLVAATTLVNQHTTAKVVERVVQNVSYIAQTQDQFTHLFRNINNRLNVLHHRVSYLEYVEEIRQKQVFFGCKPHGRYCHFDFGPEEVGWNNSWNSKTWNDLQDEYDKIEEKILKIRVDWLNSSLSDTQDTFGLETSIFDHLVQLFDWTSWKDWIKIIIVIIVLWLLIKILLGMLRSCAKVSQNYQHLPAEEEDGDTEPESSPARGDPASGSLYENWLNKIGESKNDAYRVWTEEYNSLRILFATCRWDLLTPQLLQLPFFLLTLLLKLLWDIFRHAPILNLKGWTVGQGGTSGQQQPPDFPYVNWTGSREQNNPEGGLDSGAWYEGLRGSQ

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate PBj14/BCL-3)
Length
889 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
102.054 kDa
Sequence
MGCLGNQLLIALLLLSASGIYCVQYVTVFYGIPAWRNATVPLFCATKNRDTWGTTQCLPDNGDYSELAINVTEAFDAWDNTVTEQAIEDVWNLFETSIKPCVKLTPLCITMRCNKSETDRWGLTGTPAPTTTQTTTTQASTTPTSPITAKVVNDSDPCIKINNCTGLEQEPMVSCKFNMTGLKRDKKREYNETWYSRDLVCEQNSNETDSKCYMNHCNTSVIQESCDKHYWDAIRFRYCAPPGYALLRCNDSNYSGFAPNCTKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRSNRTIISLNKYYNLTMRCRRPGNKTVLPVTIMSGLVFHSQPINERPKQAWCWFGGEWKKAIQEVKETLVKHPRYTGTNKTEQIKLTAPGGGDPEVTFMWTNCRGEFLYCKMNWFLNWVENIQNGSRWTSQNQKERQRRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIAEIDWINGNETNITMSAEVAELYRLELGDYKLVEITPIAFAPTSVKRYTTTGASRNKRGVFVLGFLGFLATAGSAMSAASVTLSAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGAKNLQTRVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPRPNDTLTPNWNNMTWQEWEKQVNFLEANITQSLEEAQIQQEKNTYELQKLNSWDIFGNWFDLTSWIKYIQYGVLIVLGVIGLRIVIYVVQMLARLRQGYRPVFSSPPAYVQQIPIQTGQELPTKEGEEGDGGGRGGNRSWPWQIEYIHFLIRQLIRLLTWLFSSCRDWLLRNCQTLQPVLQSLSRTLQRAREVIRVQIAYLQYGWRYLQEAAQAWWKFVRETLASAWRDLWETLGRVGRGILAIPRRIRQGLELTLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate F236/smH4)
Length
885 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
101.864 kDa
Sequence
MGCLGNQLLIALLLVSVLEICCVQYVTVFYGVPAWKNATIPLFCATKNRDTWGTTQCLPDNDDYSELAINVTEAFDAWDNTVTEQAIEDVWNLFETSIKPCVKLTPLCIAMRCNKTETDRWGLTGNAGTTTTAITTTATPSVAENVINESNPCIKNNSCAGLEQEPMIGCKFNMTGLNRDKKKEYNETWYSRDLICEQSANESESKCYMHHCNTSVIQESCDKHYWDAIRFRYCAPPGYALLRCNDSNYLGFAPNCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGKSNRTIISLNKYYNLTMRCRRPENKTVLPVTIMSGLVFHSQPINERPKQAWCWFEGSWKKAIQEVKETLVKHPRYTGTNDTRKINLTAPAGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRDQKGGRWKQQNRKEQQKKNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIAEIDWINSNETNITMSAEVAELYRLELGDYKLIEITPIGLAPTSVRRYTTTGASRNKRGVFVLGFLGFLATAGSAMGAASVTLSAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTRVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWPNETLVPNWNNMTWQEWERQVDFLEANITQLLEEAQIQQEKNMYELQKLNSWDIFGNWFDLTSWIRYIQYGVLIVLGVIGLRIVIYVVQMLARLRQGYRPVFSSPPAYVQQIPIHKGQEPPTKEGEEGDGGDRGGSRSWPWQIEYIHFLIRQLIRLLTWLFSSCRDWLLRSYQILQPVLQSLSTTLQRVREVIRIEIAYLQYGWRYFQEAVQAWWKLARETLASAWGDIWETLGRVGRGILAIPRRIRQGLELTLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate Mm142-83)
Length
882 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
101.198 kDa
Sequence
MGCLGNQLLIAILLLSVYGIYCIQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNDDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDKWGLTKSSTTTASTTTTTTAKSVETRDIVNETSPCVVHDNCTGLEQEPMISCKFNMTGLKRDKKKEYNETWYSADLVCEQGNSTGNESRCYMNHCNTSVIQECCDKDYWDAIRCRYCAPPGYALLRCNDTNYSGFMPNCSKVVVSSCTRMMETQTSTWFRFNGTRAENRTYIYWHGRDNRTIISLNKHYNLTMKCRRPGNKTVLPVTIMSALVFHSQPVNERPKQAWCRFGGNWKEAIKEVKQTIVKHPRYTGTNNTDKINLTAPRGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRSLTTQKPKERHKRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANINWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTNVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASLTVTAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTRVSAIEKYLKDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNETWQEWERKVDFLEANITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLTSWIKYIQYGIYIIVGVILLRIVIYIVQMLARLRQGYRPVFSSPPSYFQXTHTQQDPALPTKEGKKGDGGGSGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPIFQRLSATLRRIREVLRLELTYLQYGWSYFQEAVQAAQRSATETLAGAWGELWEALQRGGRWILAIPRRIRQGLELTLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate Mm251)
Length
881 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
101.252 kDa
Sequence
MGCLGNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKIDMVNETSSCIAQNNCTGLEQEQMISCKFTMTGLKRDKTKEYNETWYSTDLVCEQGNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKTVLPVTIMSGLVFHSQPINDRPKQAWCWFGGKWKDAIKEVKQTIVKHPRYTGTNNTDKINLTAPGGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRDVTTQRPKERHRRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANIDWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTDVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASLTLTAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTRVTAIEKYLKDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNDTWQEWERKVDFLEENITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLASWIKYIQYGIYVVVGVILLRIVIYIVQMLAKLRQGYRPVFSSPPSYFQXTHTQQDPALPTREGKEGDGGEGGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPILQRLSATLRRVREVLRTELTYLQYGWSYFHEAVQAGWRSATETLAGAWRDLWETLRRGGRWILAIPRRIRQGLELTLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate K6W)
Length
881 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
101.186 kDa
Sequence
MGCLGNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKIDMVNETSSCIAQNNCTGLEQEQMISCKFTMTGLKRDKTKEYNETWYSTDLVCEQGNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKTVLPVTIMSGLVFHSQPLTDRPKQAWCWFGGKWKDAIKEVKQTIVKHPRYTGTNNTDKINLTAPGGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDRDVTTQRPKERHRRNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANIDWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTDVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAMGAASFRLTAQSRTLLAGIVQQQQQLLGVVKRQQELLRLTVWGTKNLQTRVTAIEKYLEDQAQLNAWGCAFRQVCHTTVPWPNASLTPDWNNDTWQEWERKVDFLEENITALLEEAQIQQEKNMYELQKLNSWDVFGNWFDLASWIKYIQYGIYVVVGVILLRIVIYIVQMLAKLRQGYRPVFSSPPSYFQXTHTQQDPALPTREGKEGDGGEGGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPILQRLSATLRRIREVLRTELTYLQYGWSYFHEAVQAGWRSATETLAGAWGDLWETLRRGGRWILAIPRRIRQGLELTLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate K78)
Length
881 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
101.357 kDa
Sequence
MGCLKNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKLDMVNETSSCIAQNNCTGLEQEQMISCKFNMTGLKRDKTKEYNETWYSTDLVCEQRNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKTVLPVTIMSELVFHSQPINDRPKQAWCWFGGKWKDAIKEVKQTIVKHPRYTGTNNTDKINLTAPGGGDPEVTFMWTNCRGEFLYCKMNWFLNWVEDKDVTTQRPKERHRKNYVPCHIRQIINTWHKVGKNVYLPPREGDLTCNSTVTSLIANIDWTDGNQTSITMSAEVAELYRLELGDYKLVEITPIGLAPTDVKRYTTGGTSRNKRGVFVLGFLGFLATAGSAIGAVVVDVTAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTKVTAIEKYLKDQAQLNAWGCAFRQVCHITVPWPNASLTPDWNNDTWQEWERKVDFLEENITALLEEAQIQQEKNMYKLQKLNSWDVFGNWFDLASWIKYIQYGIYVVVGVILLRIVIYIVQMLAKLRQGYRPVFSSPPSYFQXTHTQQDPALPTREGKEGDGGEGGGNSSWPWQIEYIHFLIRQLIRLLTWLFSNCRTLLSRAYQILQPILQRLSATLRRIREVLRTELTYLQYGWSYFHEAVQAGWRSATETLAGAWGDLWETLRRGGRWILAIPRRIRQGLELTLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate MB66)
Length
880 amino acids
Function
Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.
Similarity
Belongs to the HIV-1 env protein family.
Mass
99.656 kDa
Sequence
MKAMETQRNCRTLSLKEIILCTLVLGIIGIIKCEDNMWVTVYYGVPVWREADTTLFCASDAKAQNPEVHNVWASQACVSTNPNPEEIELTNVTEYFNAWENNMVEQMHEDIVNLWDQSVKPCVKLIPLCVTLNCSLFKCIKENGNTTNCTVQISTGNDSTANNITVGTIDMYNCSFNATTELRDRKKQVYSLFYRQDLEPLEGNKPPEGDKNALYRLYNCNTTAMTQACSKVSLEPIPIHYCAPAGFALLKCNDKNFTGIGQCKNVSTVHCTHGIRPVVSTQFLLNGTLEEKVTVLDRNVSNDMDTIIVKLNETVRLNCTRTGNNTIKGIPIGPSQIFYGIETVIGDTRQAFCQLNKTVWTNTFKKVRHALNETYKGYLGNETITFGPSTGGDLEVTNLHLICGGEFFYCNTSILFNTSIIFNETKDDNITIPCRIRQIVRLWQRVGRGIFLPPIRGTINCISNITGILFAQQKTDRMNKSAMFTPVGGEMRNNWRSELYKYKVVRIEPLGVAPTKAKRRTVHREKRAAVGLGALFLGFLGAAGSTMGAASLTLTVQARQLLSGIVQQQSNLLRAIEAQQHLLQLSVWGIKQLQARVLAVERYLKDQQLLGLWGCSGKLICTTSVPWNTTWTNKSYDDIWYNMTWMQWDKEVSNYTDVIYNLLEKAQTQQENNEKELLELDKWASLWNWFDITSWLWYIKIFIIIVGGLIGLRIVFALLSIVNRVRQGYSPLSFQTLIPARRDRDRPEEIEEGGGEPDNVRSIRLVSGFLALAWNDLRDLCLFLYHRLRDLLLIVLRTLELVGQTLLKGLRRGREALIHLRGILQYWGQELKTSAISLLDTTAIAVAEGTDRIIEIAQRFGRGILNIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus agm.vervet (isolate AGM3)
Length
877 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
99.521 kDa
Sequence
MKLTLLIGILLIGIGVVLNTRQQWVTVFYGVPVWKNSSVQAFCMTPTTRLWATTNSIPDDHDYTEVPLNITEPFEAWADRNPLVAQAGSNIHLLFEQTLKPCVKLSPLCIKMSCVELNSSEPTTTPKSTTASTTNITASTTTLPCVQNKTSTVLESCNETIIEKELNEEPASNCTFAMAGYVRDQKKKYSVVWNDAEIMCKKGNNSNRECYMIHCNDSVIKEACDKTYWDELRLRYCAPAGFALLKCNDYDYAGFKTNCSNVSVVHCTNLINTTVTTGLLLNGSYSENRTQIWQKHRVSNDSVLVLFNKHYNLTVTCKRPGNKTVLPVTIMAGLVFHSQRYNTRLRQAWCHFQGNWRGAWKEVKNEIVKLPKDRYQGTNDTEEIYLQRLFGDPEAANLWFNCQGEFFYCKMDWFLNYLNNRTVDPDHNPCNGTKGKGKAPGPCAQRTYVACHIRSVINDWYTLSRKTYAPPREGHLQCTSTVTGMSVELNYNSKNRTNVTLSPQIETIWAAELGRYKLVEITPIGFAPTEVRRYTGGHDRTKRVPFVLGFLGFLGAAGTAMGAAATALTVQSQHLLAGILQQQKNLLAAVEAQQQMLKLTIWGVKNLNARVTALEKYLEDQARLNAWGCAWKQVCHTTVPWQWNNRTPDWNNMTWLEWERQISYLEGNITTQLEEARAQEEKNLDAYQKLSSWSDFWSWFDFSKWLNILKIGFLDVLGIIGLRLLYTVYSCIARVRQGYSPLSPQIHIHPWKGQPDNAEGPGEGGDKRKNSSEPWQKESGTAEWKSNWCKRLTNWCSISSIWLYNSCLTLLVHLRSAFQYIQYGLGELKAAAQEAVVALARLAQNAGYQIWLACRSAYRAIINSPRRVRQGLEGILN

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group O (isolate MVP5180)
Length
876 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
99.246 kDa
Sequence
MTVTMKVMKKNNRKSWSLYIAMALLIPCLSYSKQLYATVYSGVPVWEEAAPVLFCASDANLTSTEQHNIWASQACVPTDPNPHEFPLGNVTDNFDIWKNYMVDQMHEDIISLWEQSLKPCEKMTFLCVQMNCVDLQTNKTGLLNETINEMRNCSFNVTTVLTDKKEQKQALFYVSDLSKVNDSNAVNGTTYMLTNCNSTIIKQACPKVSFEPIPIHYCAPTGYAIFKCNDTDFNGTGLCHNISVVTCTHGIKPTVSTQLILNGTLSREKIRIMGKNITESAKNIIVTLNTPINMTCIREGIAEVQDIYTGPMRWRSMTLKRSNNTSPRSRVAYCTYNKTVWENALQQTAIRYLNLVNQTENVTIIFSRTSGGDAEVSHLHFNCHGEFFYCNTSGMFNYTFINCTKSGCQEIKGSNETNKNGTIPCKLRQLVRSWMKGESRIYAPPIPGNLTCHSNITGMILQLDQPWNSTGENTLRPVGGDMKDIWRTKLYNYKVVQIKPFSVAPTKMSRPIINIHTPHREKRAVGLGMLFLGVLSAAGSTMGAAATALTVRTHSVLKGIVQQQDNLLRAIQAQQHLLRLSVWGIRQLRARLQALETLIQNQQRLNLWGCKGKLICYTSVKWNTSWSGRYNDDSIWDNLTWQQWDQHINNVSSIIYDEIQAAQDQQEKNVKALLELDEWASLWNWFDITKWLWYIKIAIIIVGALIGIRVIMIILNLVKNIRQGYQPLSLQIPVPHRQEAETPGRTGEEGGEGDRPKWTALPPGFLQQLYTDLRTIILWTYHLLSNLISGIRRLIDYLGLGLWILGQKTIEACRLCGAVMQYWLQELKNSATNLLDTIAVSVANWTDGIILGLQRIGQGFLHIPRRIRQGAERILV

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate CDC-451)
Length
868 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
98.699 kDa
Sequence
MAMRAKGIRKNCQHLWRWGTMLLGMLMICSAAANLWVTVYYGVPVWKEATTTLFCASDAKAYDTEAHNVWATHACVPTNPNPQEVVLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLNTNNTTNTTELSIIVVWEQRGKGEMRNCSFNITTSIRDKVQREYALFYKLDVEPIDDNKNTTNNTKYRLINCNTSVITQACPKVSFEPIPIHYCTPTGFALLKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTNNAKTIIVQLNVSVEINCTRPNNHTRKRVTLGPGRVWYTTGEILGNIRQAHCNISRAQWNNTLQQIATTLREQFGNKTIAFNQSSGGDPEIVMHSFNCGGEFFYCNSTQLFNSAWNVTSNGTWSVTRKQKDTGDIITLPCRIKQIINRWQVVGKAMYALPIKGLIRCSSNITGLLLTRDGGGENQTTEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGMLGAMFLGFLGAAGSTMGATSMALTVQARQLLSGIVQQQNNLLRAIKAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGFWGCSGKLICTTAVPWNASWSNKTLDQIWNNMTWMEWDREIDNYTHLIYTLIEESQNQQEKNQQELLQLDKWASLWTWSDITKWLWYIKIFIMIVGGLIGLRIVFAVLSIVNRVRQGYSPLSFQTLLPNPRGPDRPEGTEEGGGERGRDGSTRLVHGFLALVWDDLRSLCLFSYHRLRDLLLIVARIVELLGRRGWEVLKYWWNLLQYWSQELKNSAVSLVNVTAIAVAEGTDRVIEVVQRIYRAFLHIPRRIRQGFERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate JH32)
Length
867 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
98.399 kDa
Sequence
MRVKGIRKNYQHLWRWGTMLLGILMICSAAEQLWVTVYYGVPVWKEAATTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLENVTEKFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDWGNDTSPNATNTTSSGGEKMEKGEMKNCSFNITTSIRDKVQKEHALFYKHDVVPINNSTKDNIKNDNSTRYRLISCNTSVITQACPKISFEPIPIHYCAPAGFAIIKCNDKKFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVVIRSENFTDNAKTIIVQLKEPVVINCTRPSKTTRRRIHIGPGRAFYTTKQIAGDLRQAHCNINRARWNATLKQIVGKLRKQFVNKTIVFNRSSGGDPEIVMHSFNCGGEFFYCNSTQLFNSTWLSNSTWNDTEGSNNTGGNDTITLPCRIKQIINMWQEVGKAMYAPPIEGQIRCSSNITGLLLTRDGGDNQNETETFRPGGGNMRDNWRSELYKYKVVKIELLGVAPTKAKRRVVQREKRAVGIGAVFLGFLGAAGSTMGASMTLTVQARLLLSGIVQQQNNLLRAIEGQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEEIWDNMTWMEWEREIDNYTSLIYTLIEESQNQQEKNEQELLGLDKWASLWNWFTITNWLWYIRIFIMIVGGLVGLRIVFTVLSIVNRVRQGYSPLSFQTRLPAPRGPDRPEGIEEEGGDRDRDRSGQLVDGLLAIIWVDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLFNAIAIAVAEGTDRVLKILQRAFRAILHIPTRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3)
Length
865 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.809 kDa
Sequence
MRVMEMRKNCQHLWKWGTMLLGMLMICSAAEDLWVTVYYGVPVWKEATTTLFCASEAKAYKTEVHNVWAKHACVPTDPNPQEVLLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDANLNGTNVTSSSGGTMMENGEIKNCSFQVTTSRRDKTQKKYALFYKLDVVPIEKGNISPKNNTSNNTSYGNYTLIHCNSSVITQACPKVSFEPIPIHYCTPAGFAILKCNDKKFNGTGPCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTDNVKTIIVQLNASVQINCTRPNNNTRKSITKGPGRVIYATGQIIGDIRKAHCNLSRAQWNNTLKQVVTKLREQFDNKTIVFTSSSGGDPEIVLHSFNCGGEFFYCNTTQLFNSTWNSTEGSNNTGGNDTITLPCRIKQIVNMWQEVGKAMYAPPISGQIKCISNITGLLLTRDGGEDTTNTTEIFRLGGGNMRDNWRSELYKYKVVRIEPLGVAPTRAKRRVVQREKRAVGTIGAMFLGFLGAAGSTMGAGSITLTVQARHLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNASWSNKSLNMIWNNMTWMQWEREIDNYTGIIYNLLEESQNQQEKNEQELLELDKWANLWNWFDITQWLWYIRIFIMIVGGLVGLKIVFAVLSIVNRVRQGYSPLSFQTHLPAPRGPDRPEGIEGEGGERDRDRSGGAVNGFLTLIWDDLWTLCSFSYHRLRDLLLIVVRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNTTAIAVAEGTDRIIEVAQRILRAFLHIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1)
Length
865 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
99.026 kDa
Sequence
MRYTIITLGIIVIGIGIVLSKQWITVFYGIPVWKNSSVQAFCMTPTTSLWATTNCIPDDHDYTEVPLNITEPFEAWGDRNPLIAQAASNIHLLFEQTMKPCVKLSPLCIKMNCVELNSTRERATTPTTTPKSTGLPCVGPTSGENLQSCNASIIEREMEDEPASNCTFAMAGYVRDQKKNYYSVVWNDAEIYCKNKTNSTSKECYMIHCNDSVIKEACDKTYWDQLRLRYCAPAGYALLKCNDEDYNGYKQNCSNVSVVHCTGLMNTTVTTGLLLNGSYHENRTQIWQKHRVNNNTVLILFNKHYNLSVTCRRPGNKTVLPVTIMAGLVFHSQKYNMKLRQAWCHFEGNWRGAWREVKQKIVELPKDRYKGTNNTEHIYLQRQWGDPEASNLWFNCQGEFFYCKMDWFLNYLNNKTWDAYHNFCSSKKKGHAPGPCVQRTYVAYHIRSVINDSYTLSKKTYAPPREGHLQCRSTVTGMTVELNYNSKNRTNVTLSPQIESIWAAELGRYKLVEITPIGFAPTEVRRYTGGHERQKRVPFVLGFLGFLGAAGTAMGAAASSLTVQSRHLLAGILQQQKNLLAAVEAQQQMLKLTIWGVKNLNARVTALEKYLEDQARLNSWGCAWKQVCHTTVEWPWTNRTPDWQNMTWLEWERQIADLESNITGQLVKAREQEEKNLDAYQKLTSWSDFWSWFDFSKWLNILKMGFLVIVGIIGLRLLYTVYGCIVRVRQGYVPLSPQIHIHQVGKGRPDNADEPGEGGDNSRIKLESWXKDSKSRCMQLTAWLTRLNTWLYNSCLTLLIQLRKAFQYLQYGLAELKTGAQEILQTLAGVAQNACHQIWLACRSAYRNIVNSPRRVRQGLEEILN

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group O (isolate ANT70)
Length
863 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.104 kDa
Sequence
MIVTMKAMEKRNKKLWTLYLAMALITPCLSLRQLYATVYAGVPVWEDATPVLFCASDANLTSTEKHNIWASQACVPTDPTPYEYPLHNVTDDFNIWKNYMVEQMQEDIISLWDQSLKPCVQMTFLCVQMECTNIAGTTNENLMKKCEFNVTTVIKDKKEKKQALFYVSDLMELNETSSTNKTNSKMYTLTNCNSTTITQACPKVSFEPIPIHYCAPAGYAIFKCNSTEFNGTGTCRNITVVTCTHGIRPTVSTQLILNGTLSKGKIRMMAKDILEGGKNIIVTLNSTLNMTCERPQIDIQEMRIGPMAWYSMGIGGTAGNSSRAAYCKYNATDWGKILKQTAERYLELVNNTGSINMTFNHSSGGDLEVTHLHFNCHGEFFYCNTAKMFNYTFSCNGTTCSVSNVSQGNNGTLPCKLRQVVRSWIRGQSGLYAPPIKGNLTCMSNITGMILQMDNTWNSSNNNVTFRPIGGDMKDIWRTELFNYKVVRVKPFSVAPTRIARPVISTRTHREKRAVGLGMLFLGVLSAAGSTMGAAATTLAVQTHTLLKGIVQQQDNLLRAIQAQQQLLRLSXWGIRQLRARLLALETLLQNQQLLSLWGCKGKLVCYTSVKWNRTWIGNESIWDTLTWQEWDRQISNISSTIYEEIQKAQVQQEQNEKKLLELDEWASIWNWLDITKWLWYIKIAIIIVGALVGVRVIMIVLNIVKNIRQGYQPLSLQIPNHHQEEAGTPGRTGGGGGEEGRPRWIPSPQGFLPLLYTDLRTIILWTYHLLSNLASGIQKVISYLRLGLWILGQKIINVCRICAAVTQYWLQELQNSATSLLDTLAVAVANWTDGIIAGIQRIGTGIRNIPRRIRQGLERSLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype D (isolate Z84)
Length
863 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.743 kDa
Sequence
MRVMGIRMNYQHLWKWGIMLLGILMTCSVAEDLWVTVYYGVPVWKEATTTLFCASDAKSYEPEAHNIWATHACVPTDPNPREIEMENVTENFNMWKNNMVEQMHEDIISLWDQNLKPCVKLTPLCVTLNCTNAGGNKTTNGNNTTNQEEQMMEKGEMKNCSFNITTVISDKKKQVHALFYRLDVVPIDDDNSANTSNTNYTNYRLINCNTSAITQACPKVTFEPIPIHYCAPAGFAILKCKDKKFNGTGPCKKVSTVQCTHGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNVKTIIVHLNESVEINCTRPDNKITRQSTPIGLGQALYTTRIKGDIRQAYCNISAAAWNKTLQQVAKKLGDLLNQTTIIFKPPAGGDPEITTHSFNCGGEFFYCNTSRLFNSTWNSSTWNNDTLNSEGTIKLPCRIKQIINMWQGVGKAMYAPPIEGLIKCTSNITGLLLTRDGGVNNSTNETFRPGGGDMKDNWRNELYKYKVVRIEPLGIAPTRAKRRVVEREKRAIGLGAVFLGFLGAAGSTMGAVSVALTGQARQLLSGIVQQQNNLLRAIEAQQHMLQLTVWGIKQLQARVLAVESYLKDQQLLGIWGCSGKHICTTTVPWNSSWSNKSLEEIWNNMTWIEWEREIDNYTGVIYSLIENSQIQQEKNEQDLLQLDKWASLWNWFSITKWLWYIKIFIMIVGGLIGLRIVFTVLSLVNRVRQGYSPLSFQTLLPAPRGPDRPEGIEEEGGEQGRDRSIRLVNGFSALFWDDLRNLCLFSYHRLRDLILIATRIVELLGRRGWEAIKYLWSLLQYWTQELKNSFISLLNATAIAVAEGTDRIIELIRRAFRAVLHIPRRVRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate KB-1/ETR)
Length
861 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
98.116 kDa
Sequence
MRVKEIRKNYQHLWRWGIMLRWGTMLLGMLMICSAAEQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEAHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNNMVEQMHENIISLWDQSLKPCVKLTPLCVTLHCTDLRNTTNNNSSIEEKMKGEIKNCSFNVTTNIRDKVQKEYALFYKLDVVPIDNDNNSTNTCYRLISCDTSVITQACPKVSFEPIPIHYCTPAGFALLKCNNKTFNGTGPCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEGVVIRSENFTDNVKTIIVQLNETVKINCIRPNNKTRKRVTMGPGRVYYTTGEIIGDIRQAHCNISRAEWNKTLEQIANKLRKQFENKTIVFNQSSGGDPEIVMHNFNCGGEFFYCDSSQLFNSTHLSNGTWWNGTGPENITLPCRIKQIVNMWQEVGKAMYAPPIRGQIRCSSNITGLLLTRDGGNTQNNNTNSSIEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTRAKRRVVQREKRAVGIGAVFLGFLGAAGSTMGAAAVTLTVQARQLLPGIVQQQNNLLRAIDAQQHLLQLTVWGIKQLQARVLAVERYLKDQQLMGIWGCSGKFICTTAVPWNTSWSNKSFNEIWDNMTWMEWEREINNYTNLIYNLIEESQNQQEKNEQDLLALDKWDSLWNWFSITKWLWYIKIFIMIVGGLVGLRIVFTVLSIVNRVRQGYSPLSFQTRLPARGPDRPEGIEEEGGERDRDRSGPLVDGLLALIWVDLRSLCLFSYHRLRDLLLIVTRTVELLGRKGWEVLKYLWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEILQRTYRAILHIPVKIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI)
Length
861 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.488 kDa
Sequence
MRVKEKYQHLWRWGWKWGTMLLGILMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLGNATNTNSSNTNSSSGEMMMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSANFTDNAKTIIVQLNQSVEINCTRPNNNTRKSIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNATLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQFINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNNNNGSEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGARSMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNNMTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate BEN)
Length
860 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
98.931 kDa
Sequence
MEPGRNQLFVVILLTSACLVYCSQYVTVFYGIPAWKNASIPLFCATKNRDTWGTIQCLPDNDDYQEIILNVTEAFDAWNNTVTEQAVEDVWHLFETSIKPCVKLTPLCVAMNCSRVQGNTTTPNPRTSSSTTSRPPTSAASIINETSNCIENNTCAGLGYEEMMQCEFNMKGLEQDKKRRYKDTWYLEDVVCDNTTAGTCYMRHCNTSIIKESCDKHYWDAMRFRYCAPPGFALLRCNDTNYSGFEPKCTKVVAASCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMRCKRPGNKTVLPITLMSGLVFHSQPINTRPRQAWCRFGGRWREAMQEVKQTLVQHPRYKGINDTGKINFTKPGAGSDPEVAFMWTNCRGEFLYCNMTWFLNWVEDKNQTRRNYCHIKQIINTWHKVGKNVYLPPREGELACESTVTSIIANIDIDKNRTHTNITFSAEVAELYRLELGDYKLIEITPIGFAPTDQRRYSSTPVRNKRGVFVLGFLGFLATAGSAMGARSLTLSAQSRTLLAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLKHQAQLNSWGCAFRQVCHTTVPWVNDSLSPDWKNMTWQEWEKQVRYLEANISQSLEEAQIQQEKNMYELQKLNSWDILGNWFDLTSWVKYIQYGVHIVVGIIALRIAIYVVQLLSRFRKGYRPVFSSPPGYLQQIHIHKDRGQPANEGTEEDVGGDSGYDLWPWPINYVQFLIHLLTRLLIGLYNICRDLLSKNSPTRRLISQSLTAIRDWLRLKAAQLQYGCEWIQEAFQAFARTTRETLAGAWGWLWEAARRIGRGILAVPRRIRQGAELALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype A (isolate MAL)
Length
859 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.109 kDa
Sequence
MRVREIQRNYQNWWRWGMMLLGMLMTCSIAEDLWVTVYYGVPVWKEATTTLFCASDAKSYETEVHNIWATHACVPTDPNPQEIELENVTEGFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTNVNGTAVNGTNAGSNRTNAELKMEIGEVKNCSFNITPVGSDKRQEYATFYNLDLVQIDDSDNSSYRLINCNTSVITQACPKVTFDPIPIHYCAPAGFAILKCNDKKFNGTEICKNVSTVQCTHGIKPVVSTQLLLNGSLAEEEIMIRSENLTDNTKNIIVQLNETVTINCTRPGNNTRRGIHFGPGQALYTTGIVGDIRRAYCTINETEWDKTLQQVAVKLGSLLNKTKIIFNSSSGGDPEITTHSFNCRGEFFYCNTSKLFNSTWQNNGARLSNSTESTGSITLPCRIKQIINMWQKTGKAMYAPPIAGVINCLSNITGLILTRDGGNSSDNSDNETLRPGGGDMRDNWISELYKYKVVRIEPLGVAPTKAKRRVVEREKRAIGLGAMFLGFLGAAGSTMGAASLTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLQDQRLLGMWGCSGKHICTTFVPWNSSWSNRSLDDIWNNMTWMQWEKEISNYTGIIYNLIEESQIQQEKNEKELLELDKWASLWNWFSISKWLWYIRIFIIVVGGLIGLRIIFAVLSLVNRVRQGYSPLSLQTLLPTPRGPPDRPEGIEEEGGEQGRGRSIRLVNGFSALIWDDLRNLCLFSYHRLRDLLLIATRIVELLGRRGWEALKYLWNLLQYWGQELKNSAISLLNTTAIAVAECTDRVIEIGQRFGRAILHIPRRIRQGFERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype H (isolate VI991)
Length
859 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.577 kDa
Sequence
METQRNYPSLWRWGTLILGMLLICSVVGNLWVTVYYGVPVWKEAKTTLFCASDAKAYDTERHNVWATHACVPTDPNPQEMVLENVTETFNMWVNDMVEQMHTDIISLWDQSLKPCVKLTPLCVTLDCSSVNATNVTKSNNSTDINIGEIQEQRNCSFNVTTAIRDKNQKVHALFYRADIVQIDEGERNKSDNHYRLINCNTSVIKQACPKVSFEPIPIHYCAPAGFAILKCNGKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEVEEVIIRSKNITDNTKNIIVQLNEPVQINCTRTGNNTRKSIRIGPGQAFYATGDIIGDIRRAYCNISGKQWNETLHKVITKLGSYFDNKTIILQPPAGGDIEIITHSFNCGGEFFYCNTTKLFNSTWTNSSYTNDTYNSNSTEDITGNITLQCKIKQIVNMWQRVGQAMYAPPIRGNITCISNITGLILTFDRNNTNNVTFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTEARRRVVEREKRAVGMGAFFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIQAQQHMLQLTVWGIKQLQARVLAVERYLKDQQLLGIWGCSGKLICTTNVPWNSSWSNKSLDEIWDNMTWMEWDKQINNYTDEIYRLLEVSQNQQEKNEQDLLALDKWANLWNWFSITNWLWYIRIFIMIVGGIIGLRIVFAVLSIVNRVRQGYSPLSLQTLIPNQRGPDRPREIEEEGGEQDRDRSIRLVNGFLPLVWEDLRNLCLFSYRRLRDLLSIVARTVELLGRRGWEALKLLGNLLLYWGQELKNSAISLLNTTAIAVAEGTDRIIELVQRAWRAILHIPRRIRQGFERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate CAM2)
Length
859 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
99.018 kDa
Sequence
MERGRNQLLIAILLASACLIYCRQQYVTVFYGVPAWKNASIPLFCATKNRDTWGTIQCLPDNDDYQEIPLNVTEAFDAWDNTITEQAIEDVWNLFETSIKPCVKLTPLCVAMKCNISTSDTTMIRTTTPSTAKEAPISDNSPCIRTNNCSGLEEEKIVKCHFNMTGLERDKKKQYNETWYSSDVVCDNSTDQTTNETTCYMNHCNTSVITESCDKHYWDAMRFRYCAPPGFAILRCNDTKYSGFAPNCSKVVASTCTRMMETQTSTWFGFNGTRAENRTYIYWHGKDNRTIISLNKHYNLSMYCRRPGNKTVVPITLMSGQRFHSRPIINKRPRQAWCWFKGNWTEAMQEVKQTLAEHPRYKGTKNITDITFKAPERGSDPEVTYMWSNCRGEFFYCNMTWFLNWVENKPNTTKRNYAPCHIRQIINTWHKVGKNVYLPPREGELTCNSTVTSIIANIDERDNQTTNITFSADVAELYRLELGDYKLVEITPIGFAPTSQKRYSPAHGRPKRGAFVLGFLGFLTTAGVAMGTASLTLSAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKILQARVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWANESLTPDWNNMTWQEWEQKVRYLEANISQSLEEAQLQQEKNMYELQKLNNWDVFTNWFDLTSWISYIQYGVYIVVGIIVLRIVIYVVQMLSRLRKGYRPVFSSSPGYIQQIHIHKDPEQPASEETEEDVGGNGGDRSWPWQIEYIHFLIRQLIRLLTGLYNICRNLLSRIFQTLQPILQNLRDWLRPKVAFLQYGCEWIQEAFQAAARAARETLAGACRDVWGMLQRIGRGILAVPRRIRQGAELALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype B (isolate D205)
Length
859 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
98.607 kDa
Sequence
MAYFSSRLPIALLLIGISGFVCKQYVTVFYGIPAWRNATVPLICATTNRDTWGTVQCLPDNGDYTEIRLNITEAFDAWDNTVTQQAVDDVWRLFETSIKPCVKLTPLCVAMNCSKTETNPGNASSTTTTKPTTTSRGLKTINETDPCIKNDSCTGLGEEEIMQCNFSMTGLRRDELKQYKDTWYSEDLECNNTRKYTSRCYIRTCNTTIIQESCDKHYWDSLRFRYCAPPGFFLLRCNDTNYSGFMPNCSKVVASSCTRMMETQSSTWFGFNGTRAENRTYIYWHEKDNRTIISLNTYYNLSIHCKRPGNKTVVPIRTVSGLLFHSQPINKRPRQAWCWFKGNWTEAIKEVKRTIIKHPRYKGGAKNITSVKLVSEHGKGSDPETTYMWTNCRGEFLYCNMTWFLNWVENKTNTTRRNYAPCHIRQIINTWHKVGKNIYLPPREGELSCNSTVTSLIANINSDNSTTNISVSAEVSELYRLELGDYKLVEITPIGFAPTDVRRYSSVKPRNKRGVMVLGFLGFLAMAGSAMGATSLTLSAQSRTLLAGIVQQQQQPVDVVKRQQELLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWPNETLTPNWNNMTWQQWEKQVHFLDANITALLEEAQIQQEKNMYELQKINSWDVFGNWFDLTSWIKYIHLGLYIVAGLVVLRIVVYIVQMLARLRKGYRPVFSSPPSYTQQIPIRKDRGQPANEETEEGGGNDGDYRSWPWQIEYIHFLLRQLRNLLIWLYNGCRTLLLKTFQILHQISTNLQPLRLPVAYLQYGISWFQEALRAAARATGETLASAGETLWEALRRAARAIIAIPRRIRQGLELTLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate ST)
Length
859 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
99.07 kDa
Sequence
MCGRNQLFVASLLASACLIYCVQYVTVFYGVPVWRNASIPLFCATKNRDTWGTIQCLPDNDDYQEIALNVTEAFDAWNNTVTEQAVEDVWSLFETSIKPCVKLTPLCVAMRCNSTTAKNTTSTPTTTTTANTTIGENSSCIRTDNCTGLGEEEMVDCQFNMTGLERDKKKLYNETWYSKDVVCESNDTKKEKTCYMNHCNTSVITESCDKHYWDTMRFRYCAPPGFALLRCNDTNYSGFEPNCSKVVAATCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKFYNLTVHCKRPGNKTVVPITLMSGLVFHSQPINRRPRQAWCWFKGEWKEAMKEVKLTLAKHPRYKGTNDTEKIRFIAPGERSDPEVAYMWTNCRGEFLYCNMTWFLNWVENRTNQTQHNYVPCHIKQIINTWHKVGKNVYLPPREGQLTCNSTVTSIIANIDGGENQTNITFSAEVAELYRLELGDYKLIEVTPIGFAPTPVKRYSSAPVRNKRGVFVLGFLGFLTTAGAAMGAASLTLSAQSRTLLAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWVNDTLTPDWNNMTWQEWEQRIRNLEANISESLEQAQIQQEKNMYELQKLNSWDVFGNWFDLTSWIKYIQYGVYIVVGIIVLRIVIYVVQMLSRLRKGYRPVFSSPPAYFQQIHIHKDREQPAREETEEDVGNSVGDNWWPWPIRYIHFLIRQLIRLLNRLYNICRDLLSRSFQTLQLISQSLRRALTAVRDWLRFNTAYLQYGGEWIQEAFRAFARATGETLTNAWRGFWGTLGQIGRGILAVPRRIRQGAEIALL

Gene
env
Protein
Envelope glycoprotein
Organism
Equine infectious anemia virus (isolate P3.2-1)
Length
859 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
97.14 kDa
Sequence
MVSIAFYGGIPGGISTPITQQSEKSKCEENTMFQPYCYNNDSKNSMAESKEARDQEMNLKEESKEEKRRNDWWKIGMFLLCLAGTTGGILWWYEGLPQQHYIGLVAIGGRLNGSGQSNAIECWGSFPGCRPFQNYFSYETNRSIHMNNNTATLLEAYHREITFIYKSSCTDSDHCQEYQCKKVNLNSSDSSNSVRVEDVTNTAEYWGFKWLECNQTENFKTILVPENEMVNINDTDTWIPKGCNETWARVKRCPIDILYGIHPIRLCVQPPFFLVQEKGIADTSRIGNCGPTIFLGVLEDNKGVVRGDYTACNVRRLNINRKDYTGMYQVPIFYTCTFTNITSCNSEPIISVIMYETNQVQYLLCNNNNSNNYNCVVQSFGVIGQAHLELPRPNKRIRNQSFNQYNCSINNKTELETWKLVNTSGITPLPISSEANTGLIRHKRDFGISAIVAAIVAATAIARSATMSYVALTEVNKIMEVQNHTFEVENSTLNGMDLIERQIKILYAMILQTHADVQLLKERQQVEETFNLIGCIERTHVFCHTGHPWNMSWGHLNESTQWDDWVSKMEDLNQEILTTLHGARNNLAQSMITFNTPDSIAQFGKDLWSHIGNWIPGLGASIIKYIVMFLLIYLLLTSSPKILRALWKVTSGAGSSGGRYLKKKFHHKHASREDTWDQAQHNIHLAGVTGGSGDKYYKQKYSRNDWNGESEEYNRRPKSWVKSIEAFGESYISEKTKGEISQPGAAINEHKNGSGGNNPHQGSLDLEIRSEGGNIYDCCIKAQEGTLAIPCCGFPLWLFWGLVIIVGRIAGYGLRGLAVIIRICIRGLNLIFEIIRKMLDYIGRALNPGTSHVSMPQYV

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate ROD)
Length
858 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
98.824 kDa
Sequence
MMNQLLIAILLASACLVYCTQYVTVFYGVPTWKNATIPLFCATRNRDTWGTIQCLPDNDDYQEITLNVTEAFDAWNNTVTEQAIEDVWHLFETSIKPCVKLTPLCVAMKCSSTESSTGNNTTSKSTSTTTTTPTDQEQEISEDTPCARADNCSGLGEEETINCQFNMTGLERDKKKQYNETWYSKDVVCETNNSTNQTQCYMNHCNTSVITESCDKHYWDAIRFRYCAPPGYALLRCNDTNYSGFAPNCSKVVASTCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLSLHCKRPGNKTVKQIMLMSGHVFHSHYQPINKRPRQAWCWFKGKWKDAMQEVKETLAKHPRYRGTNDTRNISFAAPGKGSDPEVAYMWTNCRGEFLYCNMTWFLNWIENKTHRNYAPCHIKQIINTWHKVGRNVYLPPREGELSCNSTVTSIIANIDWQNNNQTNITFSAEVAELYRLELGDYKLVEITPIGFAPTKEKRYSSAHGRHTRGVFVLGFLGFLATAGSAMGAASLTVSAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQARVTAIEKYLQDQARLNSWGCAFRQVCHTTVPWVNDSLAPDWDNMTWQEWEKQVRYLEANISKSLEQAQIQQEKNMYELQKLNSWDIFGNWFDLTSWVKYIQYGVLIIVAVIALRIVIYVVQMLSRLRKGYRPVFSSPPGYIQQIHIHKDRGQPANEETEEDGGSNGGDRYWPWPIAYIHFLIRQLIRLLTRLYSICRDLLSRSFLTLQLIYQNLRDWLRLRTAFLQYGCEWIQEAFQAAARATRETLAGACRGLWRVLERIGRGILAVPRRIRQGAEIALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate KR)
Length
857 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
98.689 kDa
Sequence
MDSRNQLIVAILLTSACLIYCAQYVTVFYGIPAWKNASIPLFCATRNRDTWGTIQCLPDNDDYQEIPLNVTEAFDAWNNTVTEQAVEDVWNLFETSVKPCVKLTPLCVQMECNSTSTESSNSTSEGSTVPEILNETTSCITNNSCSDLGSEEVVDCRFNMTGLQLDKPQQYSETWYSKDVVCDTTNGTSRKCYMNHCNTSVITESCDKHYWDAMRFRYCAPPGLCLLRCNDTNYSGFEPKCPKVVAATCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNTHYNLTMHCKRPGNKSVLPITLRSGRVFHSRPIINERPKQAWCWFGGDWKKAMQEVKQTLVKHPRYRGTNDTQKINFTQPGKGSDAEVVYMWTNCRGEFLYCNMTRFLNWIENRAHPQRNYAPCHIRQIINTWHRVGQNIYLPPREGELVCNSTVTSIIANIDMFDNQTSITFSAEVAELYRLELGDYKLVEITPIGFAPTSEKRYSSAPQRNKRGVFVLGVLGFLATAGSAMGAASLTLSAHPGLYWAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQTRVTAIEKYLRDQARLNSWGCAFRQVCYTTVLWENNSIVPDWNNMTWQEWEQQTRDLEANISRSLEQAQIQQEKNMYELQKLNSWDVFGNWFDLTSWIKYIQYGVYVIIGIIALRIVIYVVQLLSRLRKGYRPVFSSPPGYIQQIHIHKDWEQPDREETDEDAGNSIGDSSWPWPIAYIHFLIRQLIRLLTGLYSVCKDLLSRSFPTLQLIFQSLQRALTTIRDWLRLTIAYLQYGCEWIQEVLQVLARTTRETLASAWRDLWGAMGRIGRGILAVPRRIRQGAELALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype B (isolate UC1)
Length
857 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
98.643 kDa
Sequence
MAHTSNHLFILLLLISVYGFLGHKKNYVTVFYGIPAWRNATVPLFCATTNRDTWGTVQCLPDNGDYTEISVNITEAFDAWNNTVTEQAVDDVWSLFETSIKPCVKLTPLCVAMRCNNTGTNTTTKPITTPITTTKPSENLLNDTSPCIKNDTCPGIGLENTVDCYFNMTGLRRDEKKQYKDTWYEKDLECNGNSTSTICYMRTCNTSVIQESCDKHYWDSLRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRTENRTYMYWHSKDNRTIISLNKYYNLTMHCRRPGNKTVIPITIMSGLNFHSQPLNTRPRQAWCWFKGNWIEAIREVKETIIKHPRYKGTNNTERIRLVGPSAGSDPEVRHMWTNCRGEFFYCNMTWFLNWVENRTGTTQKNYVTCHIKQIVNTWHKVGKYVYLPPREGTLSCNSSVTSLIANIDVYYDGNDTKTNITMSAEVGELYRLELGDYKLVEITPIGFAPTEIKRYSSTTPRNKRGVMVLGFLGLLAMAGSAMGATSLTLSAQSRTLLAGIVQQQQQLLDVVKRQQELLRLTVWGTKNLQTRVTAIEKYLKDQALLNSWGCAFRQVCHTTVPWPNETLTPDWENMTWQQWEKRVNFLDANITALLEEAQIQQERNMYELQKLNSWDVFGNWFDFTSWMAYIRLGLYVVAGLIVLRIVIYIMQMLARLRKGYRPVFSSPPSYTQQIPIRKHRGQPANEETEDEGGNEGAYRSWPWQIEYAHFLIRQLRNLLIWLYNGCRNLLLKTSQILQPALQPLRLSLAYLQYGISWFQEAIQAATRAARETLANTGRALWKALRRTAEAIIAIPRRIRQGLELALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate LW123)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.938 kDa
Sequence
MRVKEKYQHLRRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGGMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKHDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVVIRSANLTDNVKTIIVQLNQSVEINCTRPNNNTRKRIRIQRGPGRTFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQYGNNKTIIFKQSSGGDLEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNNNNGSEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGHSPLSFQTHLPTPGGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate MN)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.14 kDa
Sequence
MRVKGIRRNYQHWWGWGTMLLGLLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATQACVPTDPNPQEVELVNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLRNTTNTNNSTANNNSNSEGTIKGGEMKNCSFNITTSIRDKMQKEYALLYKLDIVSIDNDSTSYRLISCNTSVITQACPKISFEPIPIHYCAPAGFAILKCNDKKFSGKGSCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTDNAKTIIVHLNESVQINCTRPNYNKRKRIHIGPGRAFYTTKNIIGTIRQAHCNISRAKWNDTLRQIVSKLKEQFKNKTIVFNQSSGGDPEIVMHSFNCGGEFFYCNTSPLFNSTWNGNNTWNNTTGSNNNITLQCKIKQIINMWQEVGKAMYAPPIEGQIRCSSNITGLLLTRDGGKDTDTNDTEIFRPGGGDMRDNWRSELYKYKVVTIEPLGVAPTKAKRRVVQREKRAAIGALFLGFLGAAGSTMGAASVTLTVQARLLLSGIVQQQNNLLRAIEAQQHMLQLTVWGIKQLQARVLAVERYLKDQQLLGFWGCSGKLICTTTVPWNASWSNKSLDDIWNNMTWMQWEREIDNYTSLIYSLLEKSQTQQEKNEQELLELDKWASLWNWFDITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSLQTRPPVPRGPDRPEGIEEEGGERDRDTSGRLVHGFLAIIWVDLRSLFLFSYHHRDLLLIAARIVELLGRRGWEVLKYWWNLLQYWSQELKSSAVSLLNATAIAVAEGTDRVIEVLQRAGRAILHIPTRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate SC)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.056 kDa
Sequence
MRVKGSGRNYQHLWRWGTMLLGILMICSAAEQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNIWATHACVPTDPNPQEVVLGNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTNLRNDTSTNATNTTSSNRGKMEGGEMTNCSFNITTSIRSKVQKEYALFYKLDVVPIDNTSYTLINCNTSVITQACPKVSFEPIPIHYCARWFAILNCNNKKFNGTGPCTNVSTVQCTHGIRPVVSTHLLLNGSLAEEEVVLRSENFTDNAKTIIVQLKEAVEINCTRPNNNTTRSIHIGPGRAFYATGDIIGDIRQAHCNISRAKWNNTLKQIVIKLRDQFENKTIIFNRSSGGDPEIVMHSFNCGGEFFYCNSTQLFSSTWNGTEGSNNTGGNDTITLPCRIKEIINMWQEVGKAMYAPPIKGQVKCSSNITGLLLTRDGGNSKNGSKNENTEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGTIGAMFLGFLGAAGSTMGATSMTLTVQARLLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNTSWSNKSLDKIWGNMTWMEWEREIDNYTSLIYTLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFTVLSIVNRVRQGYSPLSFQTRLPSQRGPDRPEGIEEEGGERDRDRSGRLVDGFLAIIWVDXRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELRNSAVSFVNATAIAVAEGTDRVIELLQRAFRAILHIPTRIRQGLERALQ

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.23 kDa
Sequence
MRVEGIQRNWKQWWIWGILGFWMVMIYNVRGNLWVTVYYGVPVWKEAKTTLFCASDAKAYDAEVHNVWATHACVPTDPNPQEMVLENVTENFNMWENDMVEQMHQDIISLWDQSLKPCVKLTPLCVTLHCSNRTIDYNNRTDNMGGEIKNCSFNMTTEVRDKREKVHALFYRLDIVPLKNESSNTSGDYRLINCNTSAITQACPKVSFDPIPIHYCAPAGYAILKCNNKTFNGTGPCNNVSTIQCTHGTKPVVSTQLLLNGSLAEEEIIIRSKNLTDNVKTIIVHLNESVEINCTRPNNNTRKSIRIGPGQAFYATGEIIGDIRQAHCNISRTAWNKTLQEVGKKLAEHFPNKAIKFAKHSGGDLEITTHSFNCRGEFFYCNTSSLFNSTYTPNSTENITGTENSIITIPCRIKQIINMWQGVGRAMYAPPIEGILTCRSNITGLLLTRDGGTGMHDTEIFRPEGGDMRDNWRSELYKYKVVEIKPLGIAPTKAKRRVVEREKRAVGIGAVFLGFLGAAGSTMGAASITLTVQVRQLLSGIVQQQSNLLRAIEAQQHMLQLTVWGIKQLQTRVLAIERYLRDQQLLGIWGCSGKLICTTAVPWNSSWSNRSQEDIWNNMTWMQWDREISNYTNTIYRLLEDSQNQQEKNEQDLLALDKWQNLWTWFGITNWLWYIKIFIKIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLTPNPRGPDRLGGIEEEGGEQDRDRSIRLVSGFLALAWDDLRSLCLFSYHRLRDLILIAARAVELLGRSSLRGIQRGWEILKYLGGLVQYWSLELKKSAISLFDTIAIAVAEGTDRIIEVIQGIWRAICNIPRRIRQGFEAALQ

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.225 kDa
Sequence
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSANFTDNAKTIIVQLNQSVEINCTRPNNNTRKSIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIDSKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTKGSNNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNNMTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSVVNRVRQGYSPLSFQTHLPIPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGAYRAIRHIPRRIRQGLERILL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.213 kDa
Sequence
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB3)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.189 kDa
Sequence
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHAGVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKKIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNATLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQFINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNNNNGSEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLLCTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSVVNRVRQGYSPLSFQTHLPIPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQEAYRAIRHIPRRIRQGLERILL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate WMJ1)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.526 kDa
Sequence
MRVKGIRRNCQHLWIWGTMLFGMWMICSAVEQLWVTVYYGVPVWKEATTTLFCASDAKAYSTEAHKVWATHACVPTNPNPQEVVLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDKNITDWENKTIIGGGEVKNCSFNITTSIRDKVHKEYALFYKLDVVPIKSNNDSSTYTRYRLIHCNTSVITQACSKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVIRSENFTDNAKTIIVHLNESVEINCTRPNNNVRRRHIHIGPGRAFYTGEIRGNIRQAHCNISRAKWNNTLKQIVEKLREQFKNKTIVFNHSSGGDPEIVTHSFNCGGEFFYCDSTQLFNSTWNVTGISTEGNNNTEENGDTITLPCRIKQIINMWQGVGKAMYAPPIGGQIRCSSNITGLLLTRDGGNSSSREEIFRPGGGNMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGAIGAMFLGFLGAAGSTMGAASLTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNASWSNKSMDQIWNNMTWMEWEREIDNYTSLIYNLIEESQNQQEKNEQELLELDKWASLWNWFSITNWLWYIKIFIMIVGGLVGLRIVFSVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGTEEEGGERDRDRSVRLVHGFLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSKELKNSAVGLLNAIAIAVAEGTDRVIEVVQRICRAIIHIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype A (isolate Z321)
Length
856 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.909 kDa
Sequence
MKVKGIQGNWQNWWKWGTLILGLVIICSAAENLWVTVYYGVPVWKDAETTLFCASDAKAYDTEKHNVWATHACVPTDPNPQELSLGNVTEKFDMWKNNMVEQMHEDVISLWDQSLKPCVKLTPLCVTLSCHNITIKDNNTNVDTEMKEEIKNCSYNMTTELRDKQRKIYSLFYRLDIVPIGGNSSNGDSSKYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDEEFEGKGPCRNVSTVQCTHGIRPVVSTQLLLNGSLAEGEVRIRSENFTDNAKIIIVQLVKPVNITCMRPNNNTRKSISIGPGRAFFATGDIIGDIRQAHCNVSRTEWNDTLSKVAAQLRKHFVNTSTDIIFANSSGGDVEITTHSFNCGGEFFYCNTSGLFNGTWLNGTSNNTWKIDTVNDTIILPCRIKQIVNMWQRVGQAMYAPPIKGVIKCVSNITGILLTRDGVGNNTSNETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVAREKRAIGMGAFFLGFLGAAGSTMGAASITLTVQARRLLSGIVQQQNNLLRAIEAQQHLLKLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKIICPTNVPWNSSWSNKSQSDIWDKMTWLEWDKEVSNYTQVIYNLIEESQTQQEINERDLLALDKWANLWNWFDISNWLWYIKIFIMIVGGLIGLRIVFAVLSIINRVRQGYSPLSFQTLTHHQREPDRPERIEEGGGEQDRDRSIRLVSGFLPLAWDDLRSLCLFCYHRLRDCALIAARIVETLIRRGWETLKYLGNLVIYWGQELKNSAINLLDTVAIAVADWTDRVIEVVQRAGRAFLNIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate NIH-Z)
Length
856 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
98.666 kDa
Sequence
MKGSKNQLLIAIVLASAYLIHCKQFVTVFYGIPAWRNASIPLFCATKNRDTWGTIQCLPDNDDYQEITLNVTEAFDAWNNTVTEQAVEDVWNLFETSIKPCVKLTPLCVAMNCTRNMTTWTGRTDTQNITIINDTSHARADNCTGLKEEEMIDCQFSMTGLERDKRKQYTEAWYSKDVVCDNNTSSQSKCYMNHCNTSVITESCDKHYWDAMRFRYCAPPGFALLRCNDTNYSGFAPNCSKVVAATCTRMMETQTSTWFGFNGTRAENRTYIYWHGKDNRTIISLNNFYNLTMHCKRPGNKTVLPITFMSGFKFHSQPVINKKPRQAWCWFEGQWKEAMQEVKETLAKHPRYKGNRSRTENIKFKAPGRGSDPEVTYMWTNCRGESLYCNMTWFLNWVENRTGQKQRNYAPCRIRQIINTWHRVGKNLYLPPREGELTCNSTVTSIIANIDAGDQTNITFSAEAAELYRLELGDYKLVEITPIGFAPTSVKRYSSAHQRHTRGVFVLGFLGFLATAGSAMGAASLTLSAQSRTLLAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTSVPWVNDTLTPDWNNMTWQEWEQKVRYLEANISQSLEQAQIQQEKNMYELQKLNSWDVFTNWLDFTSWVRYIQYGVYVVVGIVALRIVIYIVQMLSRLRKGYRPVFSSPPGYIQQIHIHKDQEQPAREETEEDVGSNGGDRSWPWPIAYIHFLIRLLIRLLTGLYNICRDLLSRISPILQPIFQSLQRALTAIRDWLRLKAAYLQYGCEWIQEAFQALARTTRETLAGAGRDLWRALQRIGRGILAVPRRIRQGAELALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate OYI)
Length
855 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.476 kDa
Sequence
MTARGTRKNYQRLWRWGTMLLGMLMICSAAENLWVTVYYGVPVWKEATTTLFCASDARAYATEVHNVWATHACVPTDPNPQEVVLGNVTENFDMWKNNMVEQMQEDIISLWDQSLKPCVKLTPLCVTLDCTDVNTTSSSLRNATNTTSSSWETMEKGELKNCSFNTTTSIRDKMQEQYALFYKLDVLPIDKNDTKFRLIHCNTSTITQACPKISFEPIPMHYCTPAGFAILKCNDKKFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVIIRSSNFTNNAKIIIVQLNKSVEINCTRPNNNTRNRISIGPGRAFHTTKQIIGDIRQAHCNLSRATWEKTLEQIATKLRKQFRNKTIAFDRSSGGDPEIVMHSFNCGGEFFYCNTSQLFNSTWNDTTRANSTEVTITLPCRIKQIVNMWQEVGKAMYAPPISGQIRCSSKITGLLLTRDGGKNTTNGIEIFRPAGGDMRDNWRSELYKYKVVKIEPLGVAPTKARRRVVQREKRAVGMLGAMFLGFLGAAGSTMGARSMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLKDQQLLGIWGCSGKLICTTTVPWNASWSNKSLNEIWDNMTWMQWEREIDNYTHLIYTLIEESQNQQEKNEQELLELDKWAGLWSWFSITNWLWYIRIFIIIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTRLPTQRGPDRPEGIEEEGGERDRDRSGRLVDGFLALIWDDLRSLCLFSYHRLRDLILIVARIVELLGRRGWEVLKYWWNLLQYWSQELKNSVISLLNATAIAVAEGTDRVIEIVQRAYRAFLNIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
Length
855 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.438 kDa
Sequence
MKVKGTRRNYQHLWRWGTLLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDARAYDTEVHNVWATHACVPTDPNPQEVVLGNVTENFNMWKNNMVEQMQEDIISLWDQSLKPCVKLTPLCVTLNCTDLGKATNTNSSNWKEEIKGEIKNCSFNITTSIRDKIQKENALFRNLDVVPIDNASTTTNYTNYRLIHCNRSVITQACPKVSFEPIPIHYCTPAGFAILKCNNKTFNGKGPCTNVSTVQCTHGIRPIVSTQLLLNGSLAEEEVVIRSDNFTNNAKTIIVQLNESVAINCTRPNNNTRKSIYIGPGRAFHTTGRIIGDIRKAHCNISRAQWNNTLEQIVKKLREQFGNNKTIVFNQSSGGDPEIVMHSFNCRGEFFYCNTTQLFNNTWRLNHTEGTKGNDTIILPCRIKQIINMWQEVGKAMYAPPIGGQISCSSNITGLLLTRDGGTNVTNDTEVFRPGGGDMRDNWRSELYKYKVIKIEPLGIAPTKAKRRVVQREKRAVGIVGAMFLGFLGAAGSTMGAVSLTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEDIWDNMTWMQWEREIDNYTNTIYTLLEESQNQQEKNEQELLELDKWASLWNWFSITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTRLPVPRGPDRPDGIEEEGGERDRDRSVRLVDGFLALIWEDLRSLCLFSYRRLRDLLLIAARTVEILGHRGWEALKYWWSLLQYWIQELKNSAVSWLNATAIAVTEGTDRVIEVAQRAYRAILHIHRRIRQGLERLLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype D (isolate Z6)
Length
855 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.971 kDa
Sequence
MRAREIERNCPNLWKWGIMLLGILMICSAADNLWVTVYYGVPVWKEATTTLFCASDAKSYKTEAHNIWATHACVPTDPNPQEIELENVTENFNMWRNNMVEQIHEDIISLWDQSLKPCVKLTPLCVTLNCTDESDEWMGNVTGKNVTEDIRMKNCSFNITTVVRDKTKQVHALFYRLDIVPIDNDNSTNSTNYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDKRFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNAKIIIVQLNESVAINCTRPYKNTRQSTPIGLGQALYTTRGRTKIIGQAHCNISKEDWNKTLQRVAIKLGNLLNKTTIIFKPSSGGDAEITTHSFNCGGEFFYCNTSGLFNSTWNINNSEGANSTESDNKLITLQCRIKQIINMWQGVGKAMYAPPIEGQINCSSNITGLLLTRDGGTNNSSNETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVEREKRAIGLGAMFLGFLGAAGSTMGAASVTLTVQARQLMSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTTVPWNSSWSNRSLNDIWQNMTWMEWEREIDNYTGLIYRLIEESQTQQEKNEQELLELDKWASLWNWFNITQWLWYIKIFIMIVGGLIGLRIVFAVLSLVNRVRQGYSPLSFQTLLPAPREPDRPEGIEEEGGERGRDRSIRLVNGFSALIWDDLRNLCLFSYHRLRDLILIAARIVELLGRRGWEALKYLWNLLQYWSRELRNSASSLLDTIAIAVAEGTDRVIEIVRRTYRAVLNVPTRIRQGLERLLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate CPZ GAB1)
Length
854 amino acids
Function
Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.803 kDa
Sequence
MKVMEKKKRDWNSLSIITIITIILLTPCLTSELWVTVYYGVPVWHDADPVLFCASDAKAHSTEAHNIWATQACVPTDPSPQEVFLPNVIESFNMWKNNMVDQMHEDIISLWDQSLKPCVKLTPLCVTLQCSKANFSQAKNLTNQTSSPPLEMKNCSFNVTTELRDKKKQVYSLFYVEDVVNLGNENNTYRIINCNTTAITQACPKTSFEPIPIHYCAPAGFAILKCNDKDFSGKGKCTNVSTVHCTHGIKPVVTTQLLINGSLAEGNITVRVENKSKNTDVWIVQLVEAVSLNCHRPGNNTRGEVQIGPGMTFYNIENVVGDTRSAYCKINGTTWNRTVEEVKKALATSSNRTAANITLNRASGGDPEVTHHMFNCGGEFFYCNTSQIFTDNITNGIIILPCRIRQIVSSWMRVGRGIYAPPIRGNITCNSNITGLLLTSDTPVTNNSGNLTFRPTGGNMKDIWRSELYKYKVVRIEPLSVAPTKARRHTVARQKDRQKRAAFGLGALFLGFLGAAGSTMGAAAVTLTVQARQLLSGIVQQQNNLLKAIEAQQHLLQLSIWGVKQLQARLLAVERYLQDQQILGLWGCSGKAVCYTTVPWNNSWPGSNSTDDIWGNLTWQQWDKLVSNYTGKIFGLLEEAQSQQEKNERDLLELDQWASLWNWFDITKWLWYIKIFLMAVGGIIGLRIIMTVFSVVRRVRQGYSPLSLQTLIPVQREQGRLGEIDEGGGEQDRSRSVRLVEGCLPLIWDDLRNLGIWSYQSLTSLACNVWRQLKTLGHLILHSLRLLRERLCLLGGIIQYWGKELKISAISLLDATAIAVAEGTDRIIEAFQVTLRIIRNIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus agm.grivet (isolate AGM gr-1)
Length
854 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
96.856 kDa
Sequence
MGRLLIKILIIAIGISIGIGNLYVTVFYGIPVWKNSTVQAFCMTPNTNMWATTNCIPDDHDNTEVPLNITEAFEAWDNPLVKQAESNIHLLFEQTMRPCVKLSPICIKMSCVELNGTATTKATTTATTTMTTPCQNCSTEQIEGEMAEEPASNCTFAIAGYQRDVKKNYSMTWYDQELVCNNKTGSEKGSKDCYMIHCNDSVIKEACDKTYWDTLRVRYCAPAGYALLKCNDKDYRGFAPKCKNVSVVHCTRLINTTITTGIGLNGSRSENRTEIWQKGGNDNDTVIIKLNKFYNLTVRCRRPGNKTVLPVTIMAGLVFHSQKYNTRLKQAWCHFQGDWKGAWKEVREEVKKVKNLTEVSIENIHLRRIWGDPESANFWFNCQGEFFYCKMDWFINYLNNRTEDAEGTNRTCDKGKPGPGPCVQRTYVACHIRQVVNDWYTVSKKVYAPPREGHLECNSSVTALYVAIDYNNKSGPINVTLSPQVRSIWAYELGDYKLVEITPIGFAPTDVRRYTGPTREKRVPFVLGFLGFLGAAGTAMGAAATTLTVQSRHLLAGILQQQKNLLAAVEQQQQLLKLTIWGVKNLNARVTALEKYLEDQARLNSWGCAWKQVCHTTVPWKYNNTPKWDNMTWLEWERQINALEGNITQLLEEAQNQESKNLDLYQKLDDWSGFWSWFSLSTWLGYVKIGFLVIVIILGLRFAWVLWGCIRNIRQGYNPLPQIHIHSSAERPDNGGGQDRGGESSSSKLIRLQEESSTPSRINNWWLNFKSCSLRIRTWCYNICLTLLIFIRTAVGYLQYGLQQLQEAATGLAQALARAAREAWGRLGAIVRSAYRAVINSPRRVRQGLEKVLG

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate MFA)
Length
853 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.912 kDa
Sequence
MRVKEKYQHLWRWGWKWGIMLLGILMICSATENLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVCATHACVPTDPNPQEVILVNVTENFDMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVNLKCTDLKNDTNTNSSNGRMIMEKGEIKNCSFNISTSIRNKVQKEYAFFYKLDIRPIDNTTYRLISCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNDKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEGVIRSANFTDNAKTIIVQLNTSVEINCTRPNNNTRKSIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWMSTLKQIASKLREQFGNNKTVIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQFINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGKNTNESEVFRPGGGDMRDNWRSELYKYKVVKIETLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQFWNNMTWMEWDREINNYTSLIHSLIDESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPNRGGPDRPEGIEEEGGERDRDRSVRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGAYRAIRHIPRRIRQGLERIL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (strain 89.6)
Length
853 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.944 kDa
Sequence
MRVKEIRKNWQHLRGGILLLGMLMICSAAKEKTWVTIYYGVPVWREATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLGNVTENFNMWKNNMVDQMHEDIISLWDESLKPCVKLTPLCVTLNCTNLNITKNTTNPTSSSWGMMEKGEIKNCSFYITTSIRNKVKKEYALFNRLDVVPIENTNNTKYRLISCNTSVITQACPKVSFQPIPIHYCVPAGFAMLKCNNKTFNGSGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEDIVIRSENFTDNAKTIIVQLNESVVINCTRPNNNTRRRLSIGPGRAFYARRNIIGDIRQAHCNISRAKWNNTLQQIVIKLREKFRNKTIAFNQSSGGDPEIVMHSFNCGGEFFYCNTAQLFNSTWNVTGGTNGTEGNDIITLQCRIKQIINMWQKVGKAMYAPPITGQIRCSSNITGLLLTRDGGNSTETETEIFRPGGGDMRDNWRSELYKYKVVRIEPIGVAPTRAKRRTVQREKRAVGIGAVFLGFLGAAGSTMGAASVTLTVQARLLLSGIVQQQNNLLRAIEAQQHMLQLTVWGIKQLQARVLALERYLRDQQLMGIWGCSGKLICTTSVPWNVSWSNKSVDDIWNNMTWMEWEREIDNYTDYIYDLLEKSQTQQEKNEKELLELDKWASLWNWFDITNWLWYIRLFIMIVGGLIGLRIVFAVLSIVNRVRQGYSPLSFQTLLPASRGPDRPEGTEEEGGERDRDRSGPLVNGFLALFWVDLRNLCLFLYHLLRNLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIKIVQRACRAIRNIPTRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype D (isolate ELI)
Length
853 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.721 kDa
Sequence
MRARGIERNCQNWWKWGIMLLGILMTCSAADNLWVTVYYGVPVWKEATTTLFCASDAKSYETEAHNIWATHACVPTDPNPQEIALENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCSDELRNNGTMGNNVTTEEKGMKNCSFNVTTVLKDKKQQVYALFYRLDIVPIDNDSSTNSTNYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVIIRSENLTNNAKNIIAHLNESVKITCARPYQNTRQRTPIGLGQSLYTTRSRSIIGQAHCNISRAQWSKTLQQVARKLGTLLNKTIIKFKPSSGGDPEITTHSFNCGGEFFYCNTSGLFNSTWNISAWNNITESNNSTNTNITLQCRIKQIIKMVAGRKAIYAPPIERNILCSSNITGLLLTRDGGINNSTNETFRPGGGDMRDNWRSELYKYKVVQIEPLGVAPTRAKRRVVEREKRAIGLGAMFLGFLGAAGSTMGARSVTLTVQARQLMSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKHICTTNVPWNSSWSNRSLNEIWQNMTWMEWEREIDNYTGLIYSLIEESQTQQEKNEKELLELDKWASLWNWFSITQWLWYIKIFIMIIGGLIGLRIVFAVLSLVNRVRQGYSPLSFQTLLPAPRGPDRPEGTEEEGGERGRDRSVRLLNGFSALIWDDLRSLCLFSYHRLRDLILIAVRIVELLGRRGWDILKYLWNLLQYWSQELRNSASSLFDAIAIAVAEGTDRVIEIIQRACRAVLNIPRRIRQGLERSLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34)
Length
853 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.044 kDa
Sequence
MRVRGIERNCQNLWKWGIMLLGILMTCSNADNLWVTVYYGVPVWKEATTTLFCASDAKSYKTEAHNIWATHACVPTDPNPQEIELENVTENFNMWRNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDEVMENVTMKNNNVTEEIRMKNCSFNITTVVRDKTKQVHALFYRLDIVPIDNDNSTNSTNYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDKRFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNAKIIIVQLNESVAINCTRPYRNIRQRTSIGLGQALYTTKTRSIIGQAYCNISKNEWNKTLQQVAIKLGNLLNKTTIIFKPSSGGDPEITTHSFNCGGEFFYCNTSGLFNSTWDISKSEWANSTESDDKPITLQCRIKQIINMWQGVGKAMYAPPIEGQINCSSNITGLLLTRDGGTNNSSNETFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTRAKRRVVEREKRAIGLGAMFLGFLGAAGSTMGARSLTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTTVPWNSSWSNRSLNDIWQNMTWMEWEREIDNYTGLIYRLIEESQTQQEKNEQELLELDKWASLWNWFNITQWLWYIKIFIMIVGGLIGLRIVFAVLSLVNRVRQGYSPLSFQTLLPAPRGPDRPEGIEEEGGERGRDRSIRLVNGFSALIWDDLRNLCLFSYHRLRDLILIAARIVELLGRRGWEALKYLWNLLQYWSRELKNSASSLLDTIAIAVAEGTDRVIEIVRRACRAVLHIPTRIRQGLERLLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate SF33)
Length
852 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.663 kDa
Sequence
MRARETRKNYQCLWRWGTMLLGMLMICSAAENLWVTVYYGVPVWKDATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLGNVTENFNMWKNNMVDQMHEDIVSLWDQSLKPCVKLTPLCVTLNCTDYLGNATNTNNSSGGTVEKEEIKNCSFNITTGIRDKVQKAYAYFYKLDVVPIDDDNTNTSYRLIHCNSSVITQTCPKVSFEPIPIHYCAPAGFAILKCNNKKFSGKGQCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVVIRSDNFTNNAKTILVQLNVSVEINCTRPNNNRRRRITSGPGKVLYTTGEIIGDIRKAYCNISRAKWNKTLEQVATKLREQFGNKTIVFKQSSGGDPEIVMHSFNCRGEFFYCNTTKLFNSTWNENSTWNATGNDTITLPCRIKQIINMWQEVGKAMYAPPIEGQIRCSSNITGLLLTRDGGGDKNSTTEIFRPAGGNMKDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGVIGAMFLGFLGAAGSTMGAASITLTVQARKLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNTSWSNKSLDKIWNNMTWMEWEREIDNYTSLIYTLLEESQNQQEKNEQELLELDKWASLWNWFSITNWLWYIRIFIMIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLIPAQRGPDRPEGIEEGGGERDRDRSTRLVNGFLALFWDDLRSLCLFSYHRLTDLLLIVARIVELLGRRGWEVLKYWWNLLLYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQRVGRAILHIPTRIRQGFERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BRVA)
Length
852 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
97.203 kDa
Sequence
MRVKGIKKNYQHLWRWGGMMLLGILMICSATDKLWVTVYYGVPVWKEANTTLFCASDAKAYDTEIHNVWATHACVPTDPNPQELVMGNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCHDFNATNATSNSGKMMEGGEMKNCSFNITTSIRDKMQKEYALFYKLDIVPIDNDKTNTRYRLISCNTSVITQACPKVTFEPIPIHYCAPAGFAILKCNNKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTNNVKTIIVQLNESVEINCTRPNNNTRKRITMGPGRVYYTTGQIIGDIRRAHCNLSRSKWENTLKQIVTKLRVQFKNKTIVFNRSSGGDPEIVMHSFNCGGEFFFCNTTQLFNSTWYRNTTGNITEGNSPITLPCRIKQIINMWQEVGKAMYAPPIRGQIKCSSNITGLLLTRDGGNNNETTDTEIFRPGGGNMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGLGALFLGFLGAAGSTMGAASLTLTVQARLLLSGIVQQQNNLLMAIEAQQHMLELTVWGIKQLQARVLAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLSDIWDNMTWMEWEREIDNYTNLIYSLIEDSQIQQEKNEKELLELDKWASLWNWFNITNWLWYIKIFIMIVGGLIGLRIVFAVLSIVNRVRQGYSPLSFQTRLPGRRGPDRPEGIEEEGGERDRDRSSPLVDGFLALFWVDLRSLFLFSYHRLRDLLLIVTRIVELLGRRGWEVLKYWWNLLQYWSQELKNSAVSLLNATAIAVGERTDRAIEVVQRAFRAILHIPRRIRQGLERALQ

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype B (isolate EHO)
Length
852 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
98.061 kDa
Sequence
MAHVNNYLLVTLLLISIYGYMGKNFVTVFYGIPAWKNASIPLFCATRNRDTWGTVQCLPDNDDYTEIQLNITEAFDAWDNTVTDQATKDVWSLFETSIKPCVKLTPLCVTMKCNKTWSSASKETTTSSASLRSSTQTLLNEDSKCIQNDSCAGIGLEEMIDCQFKMTGLKRDESKQYKDTWYKQDLVCEKGTRSNESKCYIKTCNTSIIQESCDKHYWDSLRFRYCAPPGFALLRCNDTKYSGFMPNCSKVVVSLYRMMETQTSTWFGFNGTRAENRTYIYWHGKDNRTIISLNSYYNLTMHCKRPGNKMVVPIRTVSGILFHSQPINKRPKQAWCWFKGNWTEAIQEVKETIKNHPRYSGTTNISQIRLAEHARSSDPEVRYMWTNCRGEFLYCNMTFFLNWVENRTGLKRNYASCHIRQIVNTWHKIGRNVYLPPREGELSCNSTVTSLIANIDWIDKNLTNITVSAEVSELYKLELGDYKLVEITPIGFAPTSIKRYSSVTPRNKRGVLVLGFLGFLATAGSAMGAASLTLSAQSRTLLAGIVQQQQQLVDVVKRQQELLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWVNESLKPDWNNMTWQQWERQVRFLDANITKLLEEAQIQQEKNMYELQKLNQWDIFSNWFDFTSWMAYIRLGLYIVIGIVVLRIAIYIIQMLARLRKGYRPVFSSPPSYTQQIPIRKDRGQPANEETEEGGGNNEGYRSWPWQIEYIHFPIRQLRDLLIWLYSGCRTLLSKTFQTLQPVLQPLRLPPAYLRYGISWFQEAIQAAARAAGETLASAARTSWGVLRRAAGEIIAIPRRIRQGAELALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype K (isolate 97ZR-EQTB11)
Length
851 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.273 kDa
Sequence
MRAREIQRNWQHLGKRGILFLGILIICSAANNLWVTVYYGVPVWKEATTTLFCASDAKAYETEVHNVWATHACVPTDPNPQEVVLENVTENFNMWKNNMVEQMHTDIISLWDESLKPCVKLTPLCVTLTCTNVTNNRTNANKNDTNINATVTSTDEIKNCSFNITTELKDKKKRVSALFYKLDIVQIKQSEINQSESEDRLINCNTSTVTQACPKVSFEPIPIHYCAPAGFAILKCNNNTCNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSEDITKNTKNIIVQLNEAVEINCTRPSNNTRKSIHIGPGRAFYATGDIIGDIRQAHCNISGGQWNKTVNQVKKELGKHFNKTIIFQPSSGGDPQVTRHIFNCRGEFSYCDTTDTVDDTEEEEDTTITIPCRIKQIINMWQKVGQAIYAPPTAGNITCRSNITGMILTRDGGNDNNTRTEETFRPGGGDMRDNWRSELYKYKVVQIEPLGIAPTRARRRVVQREKRAVGIGALFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQNNLLRAIEAQQQMLQLTVWGIKQLRARVLAVERYLRDQQLLGIWGCSGKLICTTNVPWNSSWSNKSQSEIWENMTWMQWEKEISNHTSTIYRLIEESQIQQEKNEQDLLALDKWASLWNWFDISNWLWYIKIFIMIVGGLIGLRIVFTVLSVVNRVRQGYSPLSFQTLTPSPRGPDRPEGIEEGGGEQDKDRSVRLVSGFLALAWDDLRNLCLFSYRHLRDLVLIATRILDRGLKGSWEALKYLWNLILYWGQEIKNSAINLLNTTAIAVAEGTDRIIEIVYRAFRALLHIPRRIRQGFERLLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate BH8)
Length
851 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.644 kDa
Sequence
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYFGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSKRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLDTSVEINCTRPNNNTRKKIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNATLKQIDSKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWSTKGSNNTEGSDTITLPCRIKQIINMWQEVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEGQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNNMTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPNPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVNLLNATAIAVAEGTDRVIELVQAAYRAIRHIPRRIRQGLERILL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype C (isolate ETH2220)
Length
851 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.621 kDa
Sequence
MKVMGIQRNCQQWWIWGILGFWMLMICNGMGNLWVTVYYGVPVWKDASPTLFCASDAKAYDTEVHNVWGTFACVPTDPSPQELGLENVTENFNMWKNDMVEQMHQDIISLWDQGLKPCVKLTPLCVTLNCNAIKNNTKVTNNSINSANDEMKNCSFNITTELRDKKRKAYALFYKLDIVPLNNGSTDYRLINCNTSTITQACPKVSLDPIPIHYCAPAGYAILKCRDKTFTGTGPCHNVSTVQCTHGIKPVVSTQLLLNGSIAEGETIIRFENLTNNAKIIIVQLNESVEITCTRPSNNTRESIRIGPGQTFYATGDIIGDIRQAHCNISEEKWNKTLQKVKEKLQKHFPNKTIEFKPSSGGDLEITTHSFNCGGEFFYCNTSNLFNSTKLELFNSSTNLNITLQCRIKQIINMWQGVGRAMYAPPIEGIIMCRSNITGLLLTRDGAKEPHSTKEIFRPEGGDMRDNWRSELYKYKVVEIKPLGVAPTKPKRRVVEREKRAALGALFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLKAIEAQQHMLQLTVWGIKQLQTRVLAIERHLRDQQLLGIWGCSGKLICTTAVPWNSSWSNKSQEEIWDNMTWMQWDREISNYTDIIYNLLEVSQNQQDKNEKDLLALDKWENLWNWFNITNWLWYIKIFIMIVGGVIGLRIIFAVLSIVNRVRQGYSPLSFQTLIPHPRGPDRLGGIEEEGGEQGRDRSIRLVNGFLAIFWDDLRSLCLFSYHRLRDLILIAARTVELLGRSSLKGLQRGWETLKYLGSLVQYWGLELKKSAINLLNTTAIVVGEGTDRFIELIQRIWRAFCNIPRRIRQGLEAALQ

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate D194)
Length
851 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
97.179 kDa
Sequence
MEPGRNQLLVAILLTSACLIYCKQYVTVFYGIPAWRNASIPLFCATKNRDTWGTIQCLPDNDDYQEITLNVTEAFDAWDNTVTEQAIEDVWRLFETSIKPCVKLTPLCVAMNCNITSGTTATPSPPNITIIDENSTCIGDNNCTGLGKEEVVECEFNMTGLEQDKKRKYNDAWYSRDVVCDKTNGTGTCYMRHCNTSVIKESCDKHYWDAMKFRYCAPPGFALLRCNDTNYSGFEPKCSKVVAASCTRMMETQTSTWFGFNGTRAENRTYIYWHGKDNRTIISLNKYYNLTMHCKRPGNKTVVPITLMSGRRFHSRPVYNKKPGQAWCWFQGNWIEAMREVKQTLAKHPRYGGTNDTGKINFTKPGIGSDPEVTYMWTNCRGEFLYCNMTWFLNWVENKTNQTHGNYAPCHIRQIINTWHKVGTNVYLPPREGELTCNSTVTSIIANIDSDGNQTNITFSAEVAELYRLELGDYKLIEVTPIPFAPTKEKRYSSAPVRNKRGVFVLGFLGFLATAGSAMGGASLTLSAQSRTLLAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWVNDSLTPDWNNMTWQEWEKRVHYLEANISQSLEQAQIQQEKNMYELQKLNSWDVFGNWFDLTSWIKYIQYGVYIVVGIIGLRIAIYIVQLLSRLRKGYRPVFSSPPGYLQQIHIHTDRGQPANEETEEDAGDDSGFGLWPWPLNYIQFLIHLLTRLLTGLYNSCRGLLSKNSPTRRLISQSLTAIRDWLRLKAAYLQYGCEWIQEAFRAFARTARETIAGAWRGLCEAAQRIGRGILAVPRRIRQGAEIALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate Ghana-1)
Length
851 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
97.491 kDa
Sequence
MCGKSLLCVASLLASAYLVYCTQYVTVFYGVPVWRNASIPLFCATKNRDTWGTIQCKPDNDDYQEITLNVTEAFDAWDNTVTEQAVEDVWSLFETSIKPCVKLTPLCVAMSCNSTTNNTTTTGSTTGMSEINETSPSYSDNCTGLGKEEIVNCQFYMTGLERDKKKQYNETWYSKDVVCESNNTKDGKNRCYMNHCNTSVITESCDKHYWDAIKFRYCAPPGYALLRCNDTNYSGFEPKCSKVVASTCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLSIHCKRPGNKTVVPITLMSGLVFHSQPINTRPRQAWCWFKGKWREAMQEVKQTLIKHPRYKGTNDTKNINFTKPGRGSDPEVAYMWTNCRGEFLYCNMTWFLNWVENRPNQTQHNYAPCHIRQIINTWHKVGKNVYLPPREGQLTCNSTVTSIIANIDVNSNQTNITFSAEVAELYRLELGDYKLIEVTPIGFAPTREKRYSSAPVRNKRGVFVLGFLGFLATAGSAMGAASLTLSAQSRTLLAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWVNDSLSPDWNNMTWQEWEKQVRYLEANISQSLEQAQIQQEKNMYELQKLNSWDVFGNWFDLTSWIKYIQYGVYIVVGVIVLRIAIYIVQLLSRLRKGYRPVFSSPPGYLQQIHIHTDRGQPANEGTEEDDRDDDGYDLPWPINYIHFLIHLLTRLLTGLYKICRDLLSTNSPTHRLISQNLTAIRDWLRLKAAYLQYGGEWIQEAFQAFAKTTRETLASAWGGLCAAVQRVGRGILAVPRRIRQGAEIALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype F2 (isolate MP257)
Length
850 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.359 kDa
Sequence
MRVREMQRNWQHLGRWGLLFLGILIICSAADKLWVTVYYGVPVWKEATTTLFCASDAKAYEREVHNVWATYACVPTDPSPQELVLGNVSEKFNMWKNNMVDQMHEDIISLWDESLKPCVKLTPLCVTLNCTKAIINVTSSNNTTLAPNVTISEEMKNCSFNITTEIRDKQKKEYALFYKLDVVQINNSNTSYRLINCNTSTLTQACPKVSFDPIPIHYCAPAGFAILKCNNKTFNGTGLCRNVSTVQCTHGIKPVVSTQLLLNGSLAEEKMIIRSENISDNTKTIIVQFKNPVKINCTRPNNNTRRSIHIGPGRAFYATGEIIGDTRKAHCNISEKQWYDTLIKIATEFKDQYNKTVGFQPSAGGDLEITTHSFNCRGEFFYCNTTILFNHTRVNDILSNNHTRENDTITLPCRIKQIVNMWQRVGQAMYAPPIAGKIQCNSNITGLLLTIDGGEGNESETLRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRQVVQREKRAVGMGAMFLGFLGAAGSTMGAASITLTVQARNLLSGIVQQQSNLLKAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICPTTVPWNLSWSNKSQDEIWGNMTWMEWEKEIGNYTDTIYRLIESAQNQQEKNEQDLLALDKWDNLWNWFSITRWLWYIEIFIMIIGSLIGLRIVFTVLSIINRVRQGYSPLSLQTLIPNSRGPERPGGIEEEGGEQDKDRSIRLVSGFLALAWDDFRSLCVFSYHCLRNFILIAARTVDKGLKRGWEVLKYLWNLAQYWGQELKNSAISLLDRTAIAVAEGTDRIIEILQRAGRAVLNIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype J (isolate SE9173)
Length
850 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.858 kDa
Sequence
METQTSWLSLWRWGLMIFGMLMICSARENLWVTVYYGVPVWRDAKTTLFCASDAKAYSTEKHNVWATHACVPTDPNPQEMSLPNVTENFNMWKNDMVDQMQEDIISVWDESLKPCVKITPLCVTLNCSDVNSNNSTDSNSSASNNSPEIMKNCSFNVTTEIRNKRKQEYALFYRQDVVPINSDNKSYILINCNTSVIKQACPKVSFQPIPIHYCAPAGFAILKCNNKTFNGTGPCKNVSTVQCTHGIKPVVSTQLLLNGSVAEGDIIIRSENISDNAKNIIVQLNDTVEIVCTRPNNNTRKGIHMGPGQVLYATGEIIGDIRKAYCNISRKDWNNTLRRVAKKLREHFNKTIDFTSPSGGDIEITTHSFNCGGEFFYCNTSTLFNSSWDENNIKDTNSTNDNTTITIPCKIKQIVRMWQRTGQAIYAPPIAGNITCKSNITGLLLTRDGGNRNGSENGTETFRPTGGNMKDNWRSELYKYKVVELEPLGVAPTKAKRRVVEREKRAVGIGAVFLGFLGTAGSTMGAASITLTVQVRQLLSGIVQQQSNLLKAIXAQQHLLKLTVWGIKQLQARVLAVERYLKDQQLLGIWGCSGKLICTTNVPWNASWSNKSYEDIWENMTWIQWEREINNYTGIIYSLIEEAQNQQETNEKDLLALDKWTNLWNWFNISNWLWYIKIFIMIIGGLIGLRIIFAVLAIVNRVRQGYSPLSFQTLIPNPTEADRPGGIEEGGGEQGRTRSIRLVNGFLALAWDDLRSLCLFSYHRLRDFVLIAARTVGTLGLRGWEILKYLVNLVWYWGQELKNSAISLLNTTAIAVAEGTDRIIEIAQRAFRAILHIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype G (isolate 92NG083)
Length
849 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.397 kDa
Sequence
MRVKGIQRNWQHLWKWGTLILGLVIICSASDNLWVTVYYGVPVWEDADTPLFCASDAKSYSSEKHNVWATHACVPTDPNPQEIAIENVTENFNMWKNNMVEQMQEDIISLWEESLKPCVKLTPLCITLNCTNVNSANHTEANNTVENKEEIKNCSFKITTERGGKKKEEYALFYKLDVVPISNGNKTSYRLIHCNVSTIKQACPKVNFDPIPIHYCAPAGFAILKCRDKEYNGTGPCKNVSTVQCTHGIKPVVSTQLLLNGSLAEEDIRIRSENFTDNTKVIIVQLNNSIEINCIRPNNNTRKSIPIGPGQAFYATGDIIGDIRQAHCNVSRIKWREMLKNVTAQLRKIYNNKNITFNSSAGGDLEITTHSFNCRGEFFYCNTSGLFNNNISNINNETITLPCKIKQIVRMWQKVGQAMYALPIAGNLVCKSNITGLILTRDGGNNNDSTEETFRPGGGDMRDNWRSELYKYKTVKIKSLGVAPTRARRRVVEREKRAVGLGAVFLGFLGAAGSTMGAASITLTAQVRQLLSGIVQQQSNLLRAIEAQQHLLQLTVWGIKQLQSRVLAIERYLKDQQLLGIWGCSGKLICTTNVPWNTSWSNKSYNEIWDNMTWLEWEREIHNYTQHIYSLIEESQNQQEKNEQDLLALDKWASLWNWFDISNWLWYIRIFIMIVGGLIGLRIVFAVLSIVNRVRQGYSPLSFQTLTHHQREPDRLGKTEEGGGEQDRDRSTRLVSGFLALAWDDLRSLCLFSYHRLRDLVLIAARTVELLGRSSLKGLRLGWEGLKYLWNLLLYWGRELKNSAINLLDTIAIATANGTDRVIEVAQRAYRAILNVPTRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate JRCSF)
Length
848 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.475 kDa
Sequence
MRVKGIRKNYQHLWKGGILLLGTLMICSAVEKLWVTVYYGVPVWKETTTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLENVTEDFNMWKNNMVEQMQEDVINLWDQSLKPCVKLTPLCVTLNCKDVNATNTTSSSEGMMERGEIKNCSFNITKSIRDKVQKEYALFYKLDVVPIDNKNNTKYRLISCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGKGQCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEKVVIRSDNFTDNAKTIIVQLNESVKINCTRPSNNTRKSIHIGPGRAFYTTGEIIGDIRQAHCNISRAQWNNTLKQIVEKLREQFNNKTIVFTHSSGGDPEIVMHSFNCGGEFFYCNSTQLFNSTWNDTEKSSGTEGNDTIILPCRIKQIINMWQEVGKAMYAPPIKGQIRCSSNITGLLLTRDGGKNESEIEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGARSMTLTVQARQLLSGIVQQQNNLLRAIEAQQHMLQLTVWGIKQLQARVLAVERYLKDQQLMGIWGCSGKLICTTAVPWNTSWSNKSLDSIWNNMTWMEWEKEIENYTNTIYTLIEESQIQQEKNEQELLELDKWASLWNWFGITKWLWYIKIFIMIVGGLIGLRIVFSVLSIVNRVRQGYSPLSFQTLLPATRGPDRPEGIEEEGGERDRDRSGQLVNGFLALIWVDLRSLFLFSYHRLRDLLLTVTRIVELLGRRGWEILKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRIIEVVQRVYRAILHIPTRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype J (isolate SE9280)
Length
848 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.488 kDa
Sequence
METQKNWQTLWRGGLMIFGMLMICKAKEDLWVTVYYGVPVWKDAKTTLFCASDAKAYSTEKHNVWATHACVPTDPSPQEMNLPNVTENFNMWKNDMVDQMQEDIISVWDESLKPCVKITPLCVTLNCSNITSNSNTTSNSSVSSPDIMTNCSFNITTEIRNKRKQEYALFYRQDVVPIDSNNKNYILINCNTSVIKQACPKVSFQPIPIHYCAPAGFAILKCNDKNFNGTGSCKNVSTVQCTHGIKPVVSTQLLLNGSIAEGDIIIRSENISDNAKNIIVQLNKTVEIVCYRPNNNTRKGIHMGPGQVLYATGEIIGNIRETHCNISERDWSNTLRRVATKLREHFNKTINFTSPSGGDIEIVTHSFNCGGEFLYCNTSKLFNSSWDKNSIEATNDTSXATITIPCKIKQIVRMWQRTGQAIYAPPIAGNITCTSNITGLLLTRDGGNRGNGSENGTETFRPTGGNMKDNWRSELYKYKVVEIEPLGVAPTKAKRRVVEREKRAVGIGAVFLGFLGTAGSTMGAASITLTVQVRQLLSGIVQQQSNLLKAIEAQQHLLKLTVWGIKQLQARVLAVERYLKDQQLLGIWGCSGKLICTTNVPWNASWSNKSYEDIWENMTWIQWEREINNYTGIIYSLIEEAQNQQENNEKDLLALDKWTNLWNWFNISNWLWYIKIFIMIIGGLIGLRIIFAVLAIVNRVRQGYSPLSFQTLIPNPTEADRPGGIEEGGGEQGRTRSIRLVNGFLALAWDDLRNLCLFSYHRLRDFVLIAARTVGTLGLRGWEILKYLVNLVWYWGQELKNSAISLLNTTAIAVAEGTDRIIEIAQRAFRAILHIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate SF162)
Length
847 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.136 kDa
Sequence
MRVKGIRKNYQHLWRGGTLLLGMLMICSAVEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEIVLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLHCTNLKNATNTKSSNWKEMDRGEIKNCSFKVTTSIRNKMQKEYALFYKLDVVPIDNDNTSYKLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNDKKFNGSGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEGVVIRSENFTDNAKTIIVQLKESVEINCTRPNNNTRKSITIGPGRAFYATGDIIGDIRQAHCNISGEKWNNTLKQIVTKLQAQFGNKTIVFKQSSGGDPEIVMHSFNCGGEFFYCNSTQLFNSTWNNTIGPNNTNGTITLPCRIKQIINRWQEVGKAMYAPPIRGQIRCSSNITGLLLTRDGGKEISNTTEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVTLGAMFLGFLGAAGSTMGARSLTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLDQIWNNMTWMEWEREIDNYTNLIYTLIEESQNQQEKNEQELLELDKWASLWNWFDISKWLWYIKIFIMIVGGLVGLRIVFTVLSIVNRVRQGYSPLSFQTRFPAPRGPDRPEGIEEEGGERDRDRSSPLVHGLLALIWDDLRSLCLFSYHRLRDLILIAARIVELLGRRGWEALKYWGNLLQYWIQELKNSAVSLFDAIAIAVAEGTDRIIEVAQRIGRAFLHIPRRIRQGFERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate WMJ22)
Length
847 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.466 kDa
Sequence
MRVKGIMRNCQHLWIWGTMLFGMWMICSAVEQLWVTVYYGVPVWKEATTTLFCASDAKAYSTEAHNVWATHACVPTDPNPQEVILGNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDKNITDWKNTTIIGGGEVKNCSFNITTSRRDKVHKEYALFYKLDVVPIKGDNNSSRYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVIRSENFTDNAKTIIVHLNESVEINCTRPYNNVRRSLSIGPGRAFRTREIIGIIRQAHCNISRAKWNNTLKQIVEKLREQFKNKTIVFNHSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWNGTDIKGDNKNSTLITLPCRIKQIINMWQGVGKAMYAPPIQGQIRCSSNITGLLLTRDGGNSSSREEIFRPGGGNMRDNWRSELYKYKVVRIEPLGVAPTKAKRRVVQREKRAVGTIGAMFLGFLGAAGSTMGAGSLTLTVQARQLLSGIVQQQNNLLRAIDAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNASWSNKSMNQIWDNLTWMEWEREIDNYTSIIYSLIEESQNQQGKNEQELLELDKWASLWNWFDITNWLWYIKIFIMIVGGLIGLRIVFTVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSVRLVHGFLALIWDDLRSLCLFSYHRLRDLLLIVKRIVELLGRRGWEALKYWWNLLQYWSKELKNSAVGLLNAIAIAVAEGTDRVIEVVQRICRAIIHIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype D (isolate NDK)
Length
846 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
96.476 kDa
Sequence
MRAREKERNCQNLWKWGIMLLGMLMTCSAAEDLWVTVYYGVPIWKEATTTLFCASDAKAYKKEAHNIWATHACVPTDPNPQEIELENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDELRNSKGNGKVEEEEKRKNCSFNVRDKREQVYALFYKLDIVPIDNNNRTNSTNYRLINCDTSTITQACPKISFEPIPIHFCAPAGFAILKCRDKKFNGTGPCSNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNVKTIIVQLNASIVINCTRPYKYTRQRTSIGLRQSLYTITGKKKKTGYIGQAHCKISRAEWNKALQQVATKLGNLLNKTTITFKPSSGGDPEITSHMLNCGGDFFYCNTSRLFNSTWNQTNSTGFNNGTVTLPCRIKQIVNLWQRVGKAMYAPPIEGLIKCSSNITGLLLTRDGGANNSSHETIRPGGGDMRDNWRSELYKYKVVKIEPIGVAPTKARRRVVEREKRAIGLGAVFLGFLGAAGSTMGAASVTLTVQARQLMSGIVHQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGRHICTTNVPWNSSWSNRSLDEIWQNMTWMEWEREIDNYTGLIYSLIEESQIQQEKNEKELLELDKWASLWNWFSITKWLWYIKLFIMIVGGLIGLRIVFAVLSVVNRVRQGYSPLSFQTLLPVPRGPDRPEEIEEEGGERGRDRSIRLVNGLFALFWDDLRNLCLFSYHRLRDSILIAARIVELLGRRGWEALKYLWNLLQYWSQELRNSASSLLDTIAIAVAERTDRVIEVVQRACRAILNVPRRIRQGLERLLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype F1 (isolate 93BR020)
Length
846 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.565 kDa
Sequence
MRVRGMQRNWQHLGKWGLLFLGTLIICNAAENLWVTVYYGVPVWKEATTTLFCASDAKSYEKEAHNVWATHACVPTDPNPQEVVLENVTERFNMWENNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLDCRNIATNGTNDTIAINDTLKEDPEAIQNCSFNTTTEIRDKQLKVHALFYKLDIVQINKDDNRTYRLINCDASTITQACPKVSWDPIPIHYCAPAGYAILKCNEKNFTGTGSCKNVSTVQCTHGIKPVVSTQLLLNGSLAEGEIVIRSQNISDNAKTIIVHLNESVQINCTRPNNNTRKRISLGPGRVFYTTGEIIGDIRKAHCNVSGTQWRNTLAKVKAKLGSYFPNATIKFNSSSGGDLEITRHNFNCMGEFFYCNTDELFNDTKFNDTGFNGTITLPCRIKQIVNMWQEVGRAMYANPIAGNITCNSNITGLLLTRDGGLNSTNETFRPGGGNMKDNWRSELYKYKVVEIEPLGVAPTKAKRQVVKRERRAVGLGALFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLKDQQLLGLWGCSGKLICTTNVPWNSSWSNKSLEEIWGNMTWMEWEKEVSNYSKEIYRLIEDSQNQQEKNEQELLALDKWASLWNWFDITQWLWYIKIFIMIVGGLIGLRIVFTVLSIVNRVRKGYSPLSFQTHIPSPREPDRPEGIEEGGGEQGKDRSVRLVTGFLALAWDDLRNLCLFSYRHLRDFILIAARIVDRGLKRGWEALKYLGNLTQYWGQELKNSAISLLNATAIAVAEWTDRVIEALQRAGRAILNIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate SBLISY)
Length
846 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
97.694 kDa
Sequence
MSGKIQLLVAFLLTSACLIYCTKYVTVFYGVPVWKNASIPLFCATKNRDTWGTIQCLPDNDDYQEIPLNVTEAFDAWDNIVTEQAVEDVWNLFETSIKPCVKLTPLCVTMNCNASTESAVATTSPSGPDMINDTDPCIQLNNCSGLREEDMVECQFNMTGLELDKKKQYSETWYSKDVVCESDNSTDRKRCYMNHCNTSVITESCDKHYWDAMRFRYCAPPGFVLLRCNDTNYSGFEPNCSKVVASTCTRMMETQPSTWLGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTILCRRPENKTVVPITLMSGRRFHSQKIINKKPRQAWCRFKGEWREAMQEVKQTLVKHPRYKGTNDTNKINFTAPEKDSDPEVAYMWTNCRGEFLYCNMTWFLNWVENKTGQQHNYVPCHIEQIINTWHKVGKNVYLPPREGELSCESTVTSIIANIDVDGDNRTNITFSAEVAELYRLELGDYKLVEVTPIGFAPTAEKRYSSAPGRHKRGVLVLGFLGFLTTAGAAMGAASLTLSAQSRTLFRGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLADQARLNSWGCAFRQVCHTTVPWVNDTLTPEWNNMTWQEWEHKIRFLEANISESLEQAQIQQEKNMYELQKLNSWDVFGNWFDLTSWIKYIQYGVMIVVGIVALRIVIYVVQMLSRLRKGYRPVFSSPPGYIQQIHIHKDWEQPDREETEEDVGNDVGSRSWPWPIEYIHFLIRLLIRLLTRLYNSCRDLLSRLYLILQPLRDWLRLKAAYLQYGCEWIQEAFQALARVTRETLTSAGRSLWGALGRIGRGILAVPRRIRQGAEIALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056)
Length
845 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.827 kDa
Sequence
METQRNYPSLWRWGTLILGMLLICSAAQNLWVTVYYGVPVWKEAKTTLFCASDAKAYETEKHNVWATHACVPTDPNPQEMVMENVTESFNMWENNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCTNVRNNTSNSTSSMEAGGELTNCSFNVTTVLRDKQQKVHALFYRLDVVPIDNNSTQYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGLCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEQIIIRTKNISDNTKNIIVQLKTPVNITCTRPNNNTRTSIHLGPGRAFYATGDIIGDIRQAHCNISRTDWNKTLHQVVTQLGIHLNNRTISFKPNSGGDMEVRTHSFNCRGEFFYCNTSGLFNSSWEMHTNYTSNDTKGNENITLPCRIKQIVNMWQRVGRAMYAPPIQGNIMCVSNITGLILTIDEGNASAENYTFRPGGGDMRDNWRSELYKYKVVKIEPLGIAPTKTRRRVVEREKRAVGMGASFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIQARQHMLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTNVPWNSSWSNKSQSEIWDNMTWMEWDKQISNYTEEIYRLLEVSQTQQEKNEQDLLALDKWASLWTWFDISHWLWYIKIFIMIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLVPNPRGPDRPEGTEEGGGEQDRDRSVRLVNGFLPVVWDDLRSLSLFSYRLLRDLLLIVVRTVELLGRRGREALKYLWNLLQYWGQELKNSAIDLLNTTAIAVAEGTDGIIVIVQRAWRAILHIPRRIRQGFERSLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype F2 (isolate MP255)
Length
843 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.678 kDa
Sequence
MRVREMQRNWQHLGKWGLLFLGILIICNANATDDLWVTVYYGVPVWKEPTTTLFCASDAKAYDPEVHNVWATYACVPTDPNPQELVLGNVTENFNMWENNMVDQMHLDIISLWDQSLKPCVKSTPLCVTLNCTDVNITMSDINGTSLKEDQGEIKNCSFNVTTELKDKKRKQQALFYRLDVEPIKNSSNIYKLISCNMSTVTQACPKVSFDPIPIHYCAPAGYAILKCNDKRFNGTGPCEKVSTVQCTHGIRPVVSTQLLLNGSLAQEDIIIRSKNITDNTKNIIVQFNRSVIIDCRRPNNNTRKGIRIGPGQTFFATGEIIGDIRKAYCNINRTLWNETLKNVSGEFKKHFNFSVAFNSSSGGDVEITTHSFNCRGEFFYYNTSGLFNETEVANNTNENITLPCRIRQFVNMWQRIGRAMYAPPIEGEIQCTSNITGLLLTRDGSKDIDGKEILRPIGGDMRDNWRSELYKYKVVRIEPVGVAPTKAKRRVVQRAKRAVGMGAVLFGFLGAAGSTMGAAAITLTAQARQLLSGIVQQQSNLLKAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTNVRWNSSWSNKSYDDIWDNMTWMQWEKEIDNYTKTIYSLIEDAQNQQERNEQELLALDKWDSLWSWFSITNWLWYIKIFIMIVGGLIGLRIVFAVLSVVNRVRQGYSPLSLQTLIPNPRGPDRPGGIEEEGGEPDRDRSMRLVSGFLPLTWDDLRSLCSFSYRHLRDLLLIAARTVDRGVKGGWEALKYLWNLTQHWGRELKNSAISLFDTIAIAVAEGTDRIIEVLQRAGRAVLHIPRRIRQGAERFLL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate YU-2)
Length
843 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.648 kDa
Sequence
MRATEIRKNYQHLWKGGTLLLGMLMICSAAEQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVKLENVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLRNATNTTSSSWETMEKGEIKNCSFNITTSIRDKVQKEYALFYNLDVVPIDNASYRLISCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIVIRSENFTNNAKTIIVQLNESVVINCTRPNNNTRKSINIGPGRALYTTGEIIGDIRQAHCNLSKTQWENTLEQIAIKLKEQFGNNKTIIFNPSSGGDPEIVTHSFNCGGEFFYCNSTQLFTWNDTRKLNNTGRNITLPCRIKQIINMWQEVGKAMYAPPIRGQIRCSSNITGLLLTRDGGKDTNGTEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGLGALFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTTVPWNTSWSNKSLNEIWDNMTWMKWEREIDNYTHIIYSLIEQSQNQQEKNEQELLALDKWASLWNWFDITKWLWYIKIFIMIVGGLIGLRIVFVVLSIVNRVRQGYSPLSFQTHLPAQRGPDRPDGIEEEGGERDRDRSGPLVDGFLAIIWVDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWGVLKYWWNLLQYWIQELKNSAVSLLNATAIAVAEGTDRVIEILQRAFRAVLHIPVRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype K (isolate 96CM-MP535)
Length
842 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.231 kDa
Sequence
MRVRGMQRNWQTLGNWGILFLGILIICSNADKLWVTVYYGVPVWKEATPTLFCASDAKAYEKEVHNVWATHACVPTDPNPQEVEMENVTENFNMWKNNMVEQMHTDIISLWDESLKPCVELTPLCVTLNCTDYKGTNSTNNATSTVVSPAEIKNCSFNITTEIKDKKKKESALFYRLDVLPLNGEGNNSSTEYRLINCNTSTITQTCPKVTFEPIPIHYCAPAGFAILKCKDKRFNGTGPCKNVSTVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSENITDNTKNIIVQLNETVQINCTRPNNNTRKSIHMGPGKAFYTTGDIIGDIRQAHCNISGEKWNMTLSRVKEKLKEHFKNGTITFKPPNPGGDPEILTHMFNCAGEFFYCNTTKLFNETGENGTITLPCRIKQIINMWQKVGKAIYAPPIAGSINCSSNITGMILTRDGGNNTHNETFRPGGGDMRDNWRSELYKYKVVQIEPLGIAPTRARRRVVQREKRAVGLGAVFFGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIEAQQHLLQLTVWGIKQLRARILAVERYLKDQQLLGIWGCSGKLICTTNVPWNSSWSNKSWEEIWNNMTWMEWEKEIGNYSDTIYKLIEESQTQQEKNEQDLLALDKWASLWNWFDITKWLWYIKIFIMIIGGLIGLRIAFAVLSVVNRVRQGYSPLSFQTLIPTSRGADRPEGIEEEGGEQDKNRSVRLVSGFLALAWDDLRNLCLFSYRQLRNLILIVTRILERGLRGGWEALKYLWNLVQYWSQELKNSAISLLNTTAIAVAGGTDRIIEIGQRAFRALLHIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group N (isolate YBF30)
Length
842 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
95.186 kDa
Sequence
MGMKSGWLLFYLLVSLIKVIGSEQHWVTVYYGVPVWREAETTLFCASDAKAHSTEAHNIWATQACVPTDPNPQEVLLPNVTEKFNMWENKMADQMQEDIISLWEQSLKPCVKLTPLCVTMLCNDSYGEERNNTNMTTREPDIGYKQMKNCSFNATTELTDKKKQVYSLFYVEDVVPINAYNKTYRLINCNTTAVTQACPKTSFEPIPIHYCAPPGFAIMKCNEGNFSGNGSCTNVSTVQCTHGIKPVISTQLILNGSLNTDGIVIRNDSHSNLLVQWNETVPINCTRPGNNTGGQVQIGPAMTFYNIEKIVGDIRQAYCNVSKELWEPMWNRTREEIKKILGKNNITFRARERNEGDLEVTHLMFNCRGEFFYCNTSKLFNEELLNETGEPITLPCRIRQIVNLWTRVGKGIYAPPIRGVLNCTSNITGLVLEYSGGPDTKETIVYPSGGNMVNLWRQELYKYKVVSIEPIGVAPGKAKRRTVSREKRAAFGLGALFLGFLGAAGSTMGAASITLTVQARTLLSGIVQQQNILLRAIEAQQHLLQLSIWGIKQLQAKVLAIERYLRDQQILSLWGCSGKTICYTTVPWNETWSNNTSYDTIWNNLTWQQWDEKVRNYSGVIFGLIEQAQEQQNTNEKSLLELDQWDSLWSWFGITKWLWYIKIAIMIVAGIVGIRIISIVITIIARVRQGYSPLSLQTLIPTARGPDRPEETEGGVGEQDRGRSVRLVSGFSALVWEDLRNLLIFLYHRLTDSLLILRRTLELLGQSLSRGLQLLNELRTHLWGILAYWGKELRDSAISLLNTTAIVVAEGTDRIIELAQRIGRGILHIPRRIRQGLERALI

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group N (isolate YBF106)
Length
836 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
94.101 kDa
Sequence
MGMQSGWPFFCLLISLTIGSDPHWVTVYYGVPVWRDAETVLFCASDAKAHSTEAHNIWATQACVPTDPNPQEVLLTNVTEYFNMWENKMAEQMQEDIISLWEQSLKPCVKLTPLCVTMLCNNSNGNSAGNSTTNRTEDLEDRQMKNCSFNITTEIRDRKKQVYSLFYVEDVVPIKDGTDNNTYRLINCNTTAVTQACPKTTFEPIPIHYCAPPGFAIMKCNEGNFSGNGSCTNVSTVQCTHGIKPVISTQLILNGSLDTDDIVIRHHGGNLLVQWNETVSINCTRPGNNTGGQVQIGPAMTFYNIEKIVGDVRQAYCNVSEEWGSMWNKTKKKIKRLLGNNTTFKAQDKNGGDLEVTHLMFNCXGEFFYCNTSRLFNESENKTNKTIILPCRIKQIVBLWTRVXKGIYAPPIRGNLSCXSSITGLILEHSGENGNKTVYPSGGNMVNLWRQELYKYKVVSIEPIGVAPGKAKRRTVSREKRAAFGLGALFLGFLGAAGSTMGAASITLTVQARTLLSGIVQQQNNLLRAIEAQQHLLQLSIWGIKQLRAKVLAIERYLRDQQILSLWGCSGKTICYTTVPWNDTWSSNTSYDTIWXNLTWQQWDRKVRNYSGVIFDLIEQAQEQQNTNEKALLELDQWASLWNWFDITKWLWYIKIAIMVVAGIIGIRIISAIITIIARVRQGYSPLSLQTLIPTAARGPDRPEETEEGVGGQDRGRSVRLVSGFLALIWEDLRNLLIFLYHRLADSLLIIRRTLEILGQSLSRGLQLLNELRIRLWGIIAYWGKELKDSAISLLNTTAIVVAEGTDRFIELAQRIGRGILHIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate EK505)
Length
835 amino acids
Function
Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.
Similarity
Belongs to the HIV-1 env protein family.
Mass
94.48 kDa
Sequence
MKVTEMQKNWLICCLLIGLIKIIGSELWVTVYYGVPVWRDAETVLFCASDAKAHSTEAHNIWATQACVPTDPNPQEVLIPNVTERFDMWKNNMVDQMQEDIISLWEQSLKPCVKLTPLCVTLSCSSWRSVNNSVNQTNHVQMQNCSFNVTTELRDKKKQVYSLFYMGDIIPLDTNNSSGNNSQYRLINCNTTAVTQACPKISFEPIPIYYCAPPGFAIIKCNDQDFNGTGECNNVSTVQCTHGIKPVISTQLILNGSLATSNIVIRNNSKDTLLVQLNESIPINCTRPGNKTRGQVQIGPGMTFYNIENIIGDTRQAYCEVNRTWEQIWNTTKQIIINNRKNITFIPNPGGDLEVTNLMINCGGEFFYCNTSQLFTNQNGNTTGNITLQCRIRQIVNLWTRVGKGIYAPPIKGPINCLSNITGIILDYTKSGTEKYTIYPTGGDMTNLWRQELYKYKVVSIEPIGVAPGKAKRHTVTRQKRAAFGLGALFLGFLGAAGSTMGAASITLTVQARKLLSGIVQQQNNLLRAIEAQQHLLQLSVWGIKQLQARVLAIERYLRDQQILGLWGCSGKSVCYTNVPWNTTWSNNNSYDTIWGNMTWQNWDEQVRNYSGVIFGLLEQAQEQQSINEKSLLELDQWSSLWNWFDITKWLWYIKIFIMVVAGIVGIRIISIIMSMVARVRQGYSPLSLQTLIPTTRGPDRPERTEEDAGELDNGRSVRLVSGFLALAWEDFRNLLLFLYHRLTDCLSILRRTLELLRQNIHKGLQLLNELRIYLWGIIAYWGRELKISAINLLDTTAVAVAEGTDRIIELVQRIGRGILHIPRRIRQGLERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 1 group M subtype F1 (isolate VI850)
Length
832 amino acids
Function
Transmembrane protein gp41: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm.
Similarity
Belongs to the HIV-1 env protein family.
Mass
93.81 kDa
Sequence
MRVRGMQRNWQHLGKWGLLFLGILIICNAADNLWVTVYYGVPVWKEATTTLFCASDAKAYEREAHNVWATHACVPTDPNPQEVFLKNVTENFDMWKNNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCTNATNNSQEKPGAMQNCSFNMTTEVRDKKLKLSALFYRLDIVPIGNNNSSEYRLINCNTSTITQACPKVSWDPIPIHYCAPAGYAILKCNDKRFNGTGPCKNVSTVQCTHGIKPVVSTQLLLNGSLAEEGIVIRSQNISNNAKTIIVHLNESVQINCTRPNNNTRKGIHLGPGQTFYATGAIIGDIRKAHCNISGTQWNNTLEYVKAELKSHFPNNTAIKFNQSSGGDLEITMHSFNCRGEFFYCDTSGLFNDTGSNNGTITLPCRIKQIVNMWQGVGRAMYTSPIAGNITCNSNITGLLLTRDGGNESNIETFRPEGGNMKDNWRSELYKYKVVEIEPLGVAPTKAKRQVVQREKRAAGLGALFLGFLGDSREHMGAASITLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARVLAVERYLKDQQLLGIWGCSGKLICTTNVPWNSSWSNKSQEEIWNNMTWMEWEKEISNYSNIIYKLIEESQNQQEKNEQELLALDKWASLWNWFDISNWLWYIKIFIMIVGGLIGLRIVFAVLSIVNRVRKGYSPLSLQTLIPSPRGPDRPEGIEEGGGEQGKDRSVRLVTGFLALAWDDLRNLCLFSYRHLRDFILIAARIVDRGLRRGWEALKYLGNLTRYWSQELKNSAISLFNTTAIVVAEGTDRIIEVLQRAGRAVLNIPRRIRQGAERALL

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus (isolate GB1)
Length
821 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
94.41 kDa
Sequence
MSTGNVYQELIRRYLVVVKKLYEGKYEVSRSFSYTMFSLLVGIIGKQYVTVFYGVPVWKEAKTHLICATDNSSLWVTTNCIPSLPDYDEVEIPDIKENFTGLIRENQIVYQAWHAMGSMLDTILKPCVKINPYCVKMQCQETENVSATTAKPITTPTTTSTVASSTEIYLDVDKNNTEEKVERNHVCRYNITGLCRDSKEEIVTNFRGDDVKCENNTCYMNHCNESVNTEDCQKGLLIRCILGCVPPGYVMLRYNEKLNNNKLCSNISAVQCTQHLVATVSSFFGFNGTMHKEGELIPIDDKYRGPEEFHQRKFVYKVPGKYGLKIECHRKGNRSVVSTPSATGLLFYHGLEPGKNLKKGMCTFKGRWGLALWSLAKELNKLNDSIKVNQTCKNFTSTGEENKQNTDKQKEFAKCIKTLKIDNYTTSGDRAAEMMMMTCQGEMFFCNVTRIMRAWNDPNEKKWYPYASCQIRQIVDDWMQVGRKIYLPPTSGFNNHIRCTHRVTEMYFEMQKIDSNETKMQIKFLPPSETSNQFVAYGAHYKLVKIMPIGIAPTDVKRHTLPEHHKEKRGAVILGILGLLSLAGSAMGSVSVALTVQSQSLVTGIVEQQKQLLKLIEQQSELLKLTIWGVKNLQTRLTSLENYIKDQALLSQWGCSWAQVCHTSVEWTNTSITPNWTSETWKEWETRTDYLQQNITEMLKQAYDREQRNTYELQKLGDLTSWASWFDFTWWVQYLKWGVFLVLGIIGLRILLALWNTISRFRQGYRPVFSQDCQQNLYRKRPDNGEEESNSLELGEHNSENLKEESLNRSLIEDLTSFARE

Gene
env
Protein
Envelope glycoprotein
Organism
Jembrana disease virus
Length
781 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
88.837 kDa
Sequence
MMEEGRKEEPEERGEKSTMRDLLQRAVDKGHLTAREALDRWTLEDHGEIHPWIILFCFAGAIGVIGGWGLRGELNVCMLIVLVVLVPIYWGIGEAARNIDSLDWKWIRKVFIVIIFVLVGLLGGCSAQRQHVAMLLSPPGIRLPSTVDIPWFCISNAPIPDCVHWTVQKPDQKHQQIENVMELQEVLDNATFFEVPDLFDRVYLELARLDANSTGVPVNIPPTGISQVKGDCSTGDIQGMNETLSTRGTLGERTFLSIRPGGWFTNTTVWFCVHWPFGFIQRKENLSEGSAQVRNCLDPINVTEPRVANYSYCPLEYKGKNYINKGLKCVGGRVDLSSNPEQHTDLLACGTFCQNFRNCDMVSRDILIGYHPSQQKQHIYINHTFWEQANTQWILVQVPNYGFVPVPDTERPWKGGKPRGKRAVGMVIFLLVLAIMAMTASVTAAATLVKQHATAQVVGRLSTNLTYITKIQNQYLHLFQNLNTRVNNLHHRVTYLEFLAEVHEVQTGLGCVPRGRYCHFDWRPEEVGLNMTLWNSTTWQQWMSYYDQIEENIWNLKYNWSEALEKGKSNTDGLEPDVFRYLADLSSSFTWGSWVDKLVWLAYILLAYFAFKVLQCIMSNLGAQTRYQLLNAQEDTDPAGDGDQPDDHRSGDTPRSGVPSGGWSQKLSEGKKIGCLILRTEWQNWRNDLRTLRWLTLGGKILQLPLSLLVLLVRILLHILSPTFQNQRGWTVGRKGTGGDDRELSPELEYLSWTGSSQEMVEMRDLKEEDIPEEGIRPVEM

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Simian immunodeficiency virus agm.vervet (isolate AGM155)
Length
768 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
86.859 kDa
Sequence
MTKFLGIFIVLGIGIGIGISTKQQWITVFYGVPVWKNSSVQAFCMTPTTRLWATTNCIPDDHDYTEVPLNITEPFEAWADRNPLVAQAGSNIHLLFEQTLKPCVKLSPLCIKMNCVELKGSATSTPATSTTAGTKLPCVRNKTDSNLQSCNDTIIEKEMNDEAASNCTFAMAGYIRDQKKNYSVVWNDAEIFCKRSTSHNGTKECYMIHCNDSVIKEACDKTYWDELRLRYCAPAGYALLKCNDWDYAGFKPECSNVSVVHCTTLMNTTVTTGLLLNGSYSENRTQIWQKHGVSNDSVLILLNKHYNLTVTCKRPGNKTVLPVTIMAGLVFHSQKYNTRLRQAWCHFQGNWKGAWKEVQEEIVKLPKERYQGTNDTNKIFLQRQFGDPEAANLWFNCQGEFFYCKMDWFLNYLNNLTVDADHNHCKNNAGKGRSPGPCVQRTYVACHIRSVINDWYTISKKTYAPPREGHLQCTSTVTGMTVELNYNNQNRTNVTLSPQIETIWAAELGRYKLVEITPIGFAPTEVRRYTGGQERQKRVPFVLGFLGFLGAAGTAMGAAATALTVQSQHLLAGILQQQKNLLAAVGAQQQMLKLTIWGVKNLNARVTALEKYLADQARLNAWGCAWKQVCHTTVPWTWNNTPEWNNMTWLEWEKQIEGLEGNITKQLEQAREQEEKNLDAYQKLSDWSSFWSWFDFSKWLNILKIGFLAVIGVIGLRLLYTLYTCIARVRQGYSPLSPQIHIHPWKGQPDNAGEPEEGGRTGKSKSTH

Gene
env
Protein
Envelope glycoprotein gp160
Organism
Human immunodeficiency virus type 2 subtype A (isolate ST/24.1C#2)
Length
712 amino acids
Function
The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity).
Mass
81.723 kDa
Sequence
MCGRNQLFVASLLASACLIYCVQYVTVFYGVPVWRNASIPLFCATKNRDTWGTIQCLPDNDDYQEIALNVTEAFDAWNNTVTEQAVEDVWSLFETSIKPCVKLTPLCVAMRCNSTTAKNTTSTPTTTTTANTTIGENSSCIRTDNCTGLGEEEMVDCQFNMTGLERDKKKLYNETWYSKDVVCESKDTKKEKTCYMNHCNTSVITESCDKHYWDTMRFRYCAPPGFALLRCNDTNYSGFEPNCSKVVAATCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKFYNLTILCKRPGNKTVVPITLMSGLVFHSQPINRRPRQAWCWFKGEWKEAMKEVKLTLAKHPRYKGTNDTEKIRFIAPGERSDPEVAYMWTNCRGEFLYCNMTWFLNWVENRTNQTQHNYVPCHIKQIINTWHKVGKNVYLPPREGQLTCNSTVTSIIANIDGGENQTNITFSAEVAELYRLELGDYKLIEVTPIGFAPTSIKRYSSAPVRNKRGVFVLGFLGFLTTAGAAMGAASLTLSAQSRTSLAGIVQQQQQLLDVVKRQQEMLRLTVWGTKNLQARVTAIEKYLKDQAQLNSWGCAFRQVCHTTVPWVNDTLTPDWNNITWQEWEQRIRNLEANISESLEQAQIQQEKNMYELQKLNSWDVFSNWFDLTSWIKYIQYGVYIVVGIIVLRMVIYVVQMLSRLRKGYRPVFSSPPAYS

Gene
env
Protein
Envelope glycoprotein gp70
Organism
Mouse mammary tumor virus (strain BR6)
Length
688 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
77.177 kDa
Sequence
MPKHQSGSPTDSSDLLLSGKKQRPHLALRRKRRREMRKINRKVPRMNLVPIKEKTAWQHLQALISEAEEVLKTSQTPQTSLTLFLALLSVLGPPPVTGESYWAYLPKPPILHPVGWGSTDPIRVLTNQTMYLGGSPDFHGFRNMSGNVHFEGKSDTLPICLSFSFSTPTGCFQVDKQVFLSDTPTVDNNKPGGKGDKRRMWELWLTTLGNSGANTKLVPIKKKLPPKYPHCQIAFKKDAFWEGDESAPPRWLPCAFPDQGVSFSPKGALGLLWDFSLPSPSVDQSDQIKSKKNLFGNYTPPVNKEVHRWYEAGWVEPTWFWENSPKDPNDRDFTALVPHTELFRLVAASRHLILKRPGFQEHEMIPTSACVTYPYAILLGLPQLIDIEKRGSTFHISCSSCRLTNCLDSSAYDYAAIIVKRPPYVLLPVDIGDEPWFDDSAIQTFRYATDLIRAKRFVAAIILGISALIAIITSFAVATTALVKEMQTATFVNNLHRNVTLALSEQRIIDLKLEARLNALEEVVLELGQDVANLKTRMSTRCHANYDFICVTPLPYNATENWERTRAHLLGIWNDNEISYNIQELTNLISDMSKQHIDAVDLSGLAQSFANGVKALNPLDWTQYFIFIGVGALLLVIVLMIFPIVFQCLAKSLDQVQSDLNVLLLKKKKGGNAAPAAEMVELPRVSYT

Gene
env
Protein
Envelope glycoprotein gp70
Organism
Mouse mammary tumor virus (strain C3H)
Length
688 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
77.271 kDa
Sequence
MPNHQSGSPTGSSDLLLDGKKQRAHLALRRKRRREMRKINRKVRRMNLAPIKEKTAWQHLQALIFEAEEVLKTSQTPQTSLTLFLALLSVLGPPPVSGESYWAYLPKPPILHPVGWGNTDPIRVLTNQTIYLGGSPDFHGFRNMSGNVHFEEKSDTLPICFSFSFSTPTGCFQVDKQVFLSDTPTVDNNKPGGKGDKRRMWELWLTTLGNSGANTKLVPIKKKLPPKYPHCQIAFKKDAFWEGDESAPPRWLPCAFPDQGVSFSPKGALGLLWDFSLPSPSVDQSDQIKSKKDLFGNYTPPVNKEVHRWYEAGWVEPTWFWENSPKDPNDRDFTALVPHTELFRLVAASRYLILKRPGFQEHEMIPTSACVTYPYVILLGLPQLIDIEKRGSTFHISCSSCRLTNCLDSSAYDYAAIIVKRPPYVLLPVDIGDEPWFDDSAIQTFRYATDLIRAKRFVAAIILGISALIAIITSFAVATTALVKEMQTATFVNNLHRNVTLALSEQRIIDLKLEARLNALEEVVLDLGQDVANLKTRMSTRCHANYDFICVTPLPYNASESWERTKAHLLGIWNDNEISYNIQELTNLIGDMSKQHIDTVDLSGLAQSFANGVKALNPLDWTQYFIFIGVGALLLVIVLMIFPIVFQCLAKSLDQVQSDLNVLLLKKKKGGNAAPAAEMVELPRVSYT

Gene
env
Protein
Envelope glycoprotein gp70
Organism
Mouse mammary tumor virus (strain GR)
Length
688 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
77.221 kDa
Sequence
MPNHQSGSPTGSSDLLLSGKKQRPHLALRRKRRREMRKINRKVRRMNLAPIKEKTAWQHLQALISEAEEVLKTSQTPQNSLTLFLALLSVLGPPPVTGESYWAYLPKPPILHPVGWGSTDPIRVLTNQTMYLGGSPDFHGFRNMSGNVHFEGKSDTLPICFSFSFSTPTGCFQVDKQVFLSDTPTVDNNKPGGKGDKRRMWELWLHTLGNSGANTKLVPIKKKLPPKYPHCQIAFKKDAFWEGDESAPPRWLPCAFPDKGVSFSPKGALGLLWDFSLPSPSVDQSDQIKSKKDLFGNYTPPVNKEVHRWYEAGWVEPTWFWENSPKDPNDRDFTALVPHTELFRLVAASRHLILKRPGFQEHEMIPTSACVTYPYAILLGLPQLIDIEKRGSTFHISCSSCRLTNCLDSSAYDYAAIIVKRPPYVLLPVDIGDEPWFDDSAIQTFRYATDLIRAKRFVAAIILGISALIAIITSFAVATTALVKEMQTATFVNNLHRNVTLALSEQRIIDLKLEARLNALEEVVLELGQDVANLKTRMSTRCHANYDFICVTPLPYNATEDWERTRAHLLGIWNDNEISYNIQELTNLISDMSKQHIDAVDLSGLAQSFANGVKALNPLDWTQYFIFIGVGALLLVIVLMIFPIVFQCLAKSLDQVQSDLNVLLLKKKKGGNAAPAAEMVELPRVSYT

Gene
env
Protein
Envelope glycoprotein
Organism
Gibbon ape leukemia virus
Length
685 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
75.837 kDa
Sequence
MVLLPGSMLLTSNLHHLRHQMSPGSWKRLIILLSCVFGGGGTSLQNKNPHQPMTLTWQVLSQTGDVVWDTKAVQPPWTWWPTLKPDVCALAASLESWDIPGTDVSSSKRVRPPDSDYTAAYKQITWGAIGCSYPRARTRMASSTFYVCPRDGRTLSEARRCGGLESLYCKEWDCETTGTGYWLSKSSKDLITVKWDQNSEWTQKFQQCHQTGWCNPLKIDFTDKGKLSKDWITGKTWGLRFYVSGHPGVQFTIRLKITNMPAVAVGPDLVLVEQGPPRTSLALPPPLPPREAPPPSLPDSNSTALATSAQTPTVRKTIVTLNTPPPTTGDRLFDLVQGAFLTLNATNPGATESCWLCLAMGPPYYEAIASSGEVAYSTDLDRCRWGTQGKLTLTEVSGHGLCIGKVPFTHQHLCNQTLSINSSGDHQYLLPSNHSWWACSTGLTPCLSTSVFNQTRDFCIQVQLIPRIYYYPEEVLLQAYDNSHPRTKREAVSLTLAVLLGLGITAGIGTGSTALIKGPIDLQQGLTSLQIAIDADLRALQDSVSKLEDSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYIDHSGAVRDSMKKLKEKLDKRQLERQKSQNWYEGWFNNSPWFTTLLSTIAGPLLLLLLLLILGPCIINKLVQFINDRISAVKILVLRQKYQALENEGNL

Gene
env
Protein
Envelope glycoprotein
Organism
Gibbon ape leukemia virus
Length
685 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
75.837 kDa
Sequence
MVLLPGSMLLTSNLHHLRHQMSPGSWKRLIILLSCVFGGGGTSLQNKNPHQPMTLTWQVLSQTGDVVWDTKAVQPPWTWWPTLKPDVCALAASLESWDIPGTDVSSSKRVRPPDSDYTAAYKQITWGAIGCSYPRARTRMASSTFYVCPRDGRTLSEARRCGGLESLYCKEWDCETTGTGYWLSKSSKDLITVKWDQNSEWTQKFQQCHQTGWCNPLKIDFTDKGKLSKDWITGKTWGLRFYVSGHPGVQFTIRLKITNMPAVAVGPDLVLVEQGPPRTSLALPPPLPPREAPPPSLPDSNSTALATSAQTPTVRKTIVTLNTPPPTTGDRLFDLVQGAFLTLNATNPGATESCWLCLAMGPPYYEAIASSGEVAYSTDLDRCRWGTQGKLTLTEVSGHGLCIGKVPFTHQHLCNQTLSINSSGDHQYLLPSNHSWWACSTGLTPCLSTSVFNQTRDFCIQVQLIPRIYYYPEEVLLQAYDNSHPRTKREAVSLTLAVLLGLGITAGIGTGSTALIKGPIDLQQGLTSLQIAIDADLRALQDSVSKLEDSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYIDHSGAVRDSMKKLKEKLDKRQLERQKSQNWYEGWFNNSPWFTTLLSTIAGPLLLLLLLLILGPCIINKLVQFINDRISAVKILVLRQKYQALENEGNL

Gene
env
Protein
Envelope glycoprotein
Organism
Friend murine leukemia virus (isolate FB29)
Length
676 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
74.05 kDa
Sequence
MACSTLSKSPKDKIDPRDLLIPLILFLSLKGARSAAPGSSPHQVYNITWEVTNGDRETVWAISGNHPLWTWWPVLTPDLCMLALSGPPHWGLEYQAPYSSPPGPPCCSGSSGNVAGCARDCNEPLTSLTPRCNTAWNRLKLDQVTHKSSEGFYVCPGSHRPREAKSCGGPDSFYCASWGCETTGRVYWKPSSSWDYITVDNNLTSNQAVQVCKDNKWCNPLAIRFTNAGKQVTSWTTGHYWGLRLYVSGQDPGLTFGIRLSYQNLGPRIPIGPNPVLADQLSFPLPNPLPKPAKSPPASSSTPTLISPSPTPTQPPPAGTGDRLLNLVQGAYQALNLTNPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVASQHKLTLSEVTGRGLCIGTVPKTHQALCNTTLKAGKGSYYLVAPTGTMWACNTGLTPCLSATVLNRTTDYCVLVELWPRVTYHPPSYVYSQFEKSHRHKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLHAAVQDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLSQRQKLFESSQGWFEGWFNRSPWFTTLISTIMGPLIILLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPLEYEPQ

Gene
env
Protein
Envelope glycoprotein
Organism
Friend murine leukemia virus (isolate PVC-211)
Length
676 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.946 kDa
Sequence
MACSTLSKSPKDKIDPRDLLIPLILFLSLKGARSAAPGSSPHQVYNITWEVTNGDRETVWAISGNHPLWTWWPDLTPDLCMLALSGPPHWGLEYRAPYSSPPGPPCCSGSSGNRAGCARDCDEPLTSLTPRCNTAWNRLKLDQVTHKSSGGFYVCPGSHRPRKAKSCGGPDSFYCASWGCETTGRAYWKPSSSWDYITVDNNLTTNQAAQVCKDNKWCNPLAIQFTNAGKQVTSWTIGHYWGLRLYVSGQDPGLTFGIRLKYQNLGPRVPIGPNPVLADQLSFPLPNPLPKPAKSPSASNSTPTLISPSPAPTQPPPAGTGDRLLNLVQGAYQALNLTNPDKTQECWLCLVSAPPYYEGVAVLGTYSNHTSAPANCSAGSQHKLTLSEVTGQGLCIGTVPKTHQALCNTTLKTGKGSYYLVAPAGTMWACNTGLTPCLSATVLNRTTDYCVLVELWPRVTYHPPSYVYSQFEKSYRHKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLHAAVQDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLTQRQKLFESSQGWFEGLFNRSPWFTTLISTIMGPLIILLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPLEYEPQ

Gene
env
Protein
Envelope glycoprotein
Organism
Friend murine leukemia virus (isolate 57)
Length
675 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
74.025 kDa
Sequence
MACSTLPKSPKDKIDPRDLLIPLILFLSLKGARSAAPGSSPHQVYNITWEVTNGDRETVWAISGNHPLWTWWPVLTPDLCMLALSGPPHWGLEYQAPYSSPPGPPCCSGSSGSSAGCSRDCDEPLTSLTPRCNTAWNRLKLDQVTHKSSEGFYVCPGSHRPREAKSCGGPDSFYCASWGCETTGRVYWKPSSSWDYITVDNNLTTSQAVQVCKDNKWCNPLAIQFTNAGKQVTSWTTGHYWGLRLYVSGRDPGLTFGIRLRYQNLGPRVPIGPNPVLADQLSLPRPNPLPKPAKSPPASNSTPTLISPSPTPTQPPPAGTGDRLLNLVQGAYQALNLTNPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVASQHKLTLSEVTGRGLCIGTVPKTHQALCNTTLKIDKGSYYLVAPTGTTWACNTGLTPCLSATVLNRTTDYCVLVELWPRVTYHPPSYVYSQFEKSYRHKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLHAAVQDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLTQRQKLFESSQGWFEGLFNRSPWFTTLISTIMGPLIILLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPLEYEP

Gene
env
Protein
Envelope glycoprotein
Organism
AKV murine leukemia virus
Length
669 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.756 kDa
Sequence
MESTTLSKPFKNQVNPWGPLIVLLILGGVNPVTLGNSPHQVFNLTWEVTNGDRETVWAITGNHPLWTWWPDLTPDLCMLALHGPSYWGLEYRAPFSPPPGPPCCSGSSDSTPGCSRDCEEPLTSYTPRCNTAWNRLKLSKVTHAHNGGFYVCPGPHRPRWARSCGGPESFYCASWGCETTGRASWKPSSSWDYITVSNNLTSDQATPVCKGNEWCNSLTIRFTSFGKQATSWVTGHWWGLRLYVSGHDPGLIFGIRLKITDSGPRVPIGPNPVLSDRRPPSRPRPTRSPPPSNSTPTETPLTLPEPPPAGVENRLLNLVKGAYQALNLTSPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVASQHKLTLSEVTGQGLCIGAVPKTHQVLCNTTQKTSDGSYYLAAPTGTTWACSTGLTPCISTTILDLTTDYCVLVELWPRVTYHSPSYVYHQFERRAKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLQAAMHDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLSQRQKLFESQQGWFEGLFNKSPWFTTLISTIMGPLIILLLILLFGPCILNRLVQFIKDRISVVQALVLTQQYHQLKTIEDCKSRE

Gene
env
Protein
Envelope glycoprotein
Organism
Hortulanus murine leukemia virus
Length
666 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.035 kDa
Sequence
MDRPALPKSIKDKTNPWGPIILGILIMLGGALGKGSPHKVFNLTWEVYNQEYETVWATSGSHPLWTWWPTLTPDLCMLAQLAKPSWGLSDYPPYSKPPGPPCCTTDNNPPGCSRDCNGPLTYLTPRCSTAWNRLKLVLTTHHLNQGFYVCPGPHRPRHARNCGGPDDFYCAHWGCETTGQAYWKPSSSWDYIRVSNNASSSDATTACKNNNWCSPLAISFTDPGKRATSWTSGFTWGLRLYISGHPGLIFGVRLKISDLGPRVPIGPNPVLSEQRPPSQPEPARLPPSSNLTQGGTPSAPTGPPQEGTGDRLLDLVQGAYQALNATSPDKTQECWLCLVSSPPYYEGVAVVGPYSNHTTAPANCSADSQHKLTLSEVTGKPLPRKGSQDPPGPVQYHSGARQKYSLSGGSRGTMWACNTGLTPCLSTAVLNLTTDYCVLVELWPRVTYHSLDFVYRQVEGRTRYQREPVSLTLALLLGGLTMGGIAAGVGTGTSALVKTQQFEQLHAAIQADLKEVESSITNLEKSLTSLSEVVLQNRRGLDLLFLEKGGLCAALKEECCFYADHTGLVRDSMAKLRERLNQRQKLFEAGQGWFEGLFNRSPWLTTLISTIMGPLIILLLILMFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPLEHGRAIVK

Gene
env
Protein
Envelope glycoprotein
Organism
Moloney murine leukemia virus (isolate Shinnick)
Length
665 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.302 kDa
Sequence
MARSTLSKPLKNKVNPRGPLIPLILLMLRGVSTASPGSSPHQVYNITWEVTNGDRETVWATSGNHPLWTWWPDLTPDLCMLAHHGPSYWGLEYQSPFSSPPGPPCCSGGSSPGCSRDCEEPLTSLTPRCNTAWNRLKLDQTTHKSNEGFYVCPGPHRPRESKSCGGPDSFYCAYWGCETTGRAYWKPSSSWDFITVNNNLTSDQAVQVCKDNKWCNPLVIRFTDAGRRVTSWTTGHYWGLRLYVSGQDPGLTFGIRLRYQNLGPRVPIGPNPVLADQQPLSKPKPVKSPSVTKPPSGTPLSPTQLPPAGTENRLLNLVDGAYQALNLTSPDKTQECWLCLVAGPPYYEGVAVLGTYSNHTSAPANCSVASQHKLTLSEVTGQGLCIGAVPKTHQALCNTTQTSSRGSYYLVAPTGTMWACSTGLTPCISTTILNLTTDYCVLVELWPRVTYHSPSYVYGLFERSNRHKREPVSLTLALLLGGLTMGGIAAGIGTGTTALMATQQFQQLQAAVQDDLREVEKSISNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLNQRQKLFESTQGWFEGLFNRSPWFTTLISTIMGPLIVLLMILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPIEYEP

Gene
env
Protein
Envelope glycoprotein
Organism
Radiation murine leukemia virus
Length
665 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.083 kDa
Sequence
MESTTLSKPFKNQVNPWGPLIVLLILGRVNPVALGNSPHQVFNLSWEVTNEDRETVWAITGNHPLWTWWPDLTPDLCMLALHGPSYWGLEYQAPFSPPPGPPCCSGSSGSTPGCSRDCEEPLTSYTPRCNTAWNRLKLSKVTHAHNEGFYVCPGPHRPRWARSCGGPESFYCASWGCETTGRASWKPSSSWDYITVSNNLTSGQATPVCKNNTWCNSLTIRFTSLGKQATSWVTGHWWGLRLYVSGHDPGLIFGIRLKITDSGPRVPIGPNPVLSDQRPPSQPRSPPHSNSTPTETPLTLPEPPPAGVENRLLNLVKGAYQALNLTSPDRTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVALQHKLTLSEVTGQGLCVGAVPKTHQALCNTTQNTSGGSYYLAAPAGTIWACNTGLTPCLSTTVLNLTTDYCVLVELWPRVTYHSPSYVYHQFERRGKYKREPVSLTLALLLGGLTMGGIAAGIGTGTTALVATQQLQAAVHDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGVVRDSMAKLRERLNQRQKLFESGQGWFERLFNGSPWFTTLISTIMGPLIVLLLILLLGPCILNRLVQFVKDRISVVQALVLTQQYHQLKSIDPEEMESRE

Gene
env
Protein
Envelope glycoprotein
Organism
Radiation murine leukemia virus (strain Kaplan)
Length
665 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.085 kDa
Sequence
MESTTLSKPFKNQVNPWGPLIVLLILGRVNPVALGNSPHQVFNLSWEVTNEDRETVWAITGNHPLWTWWPDLTPDLCMLALHGPSYWGLEYQAPFSPPPGPPCCSRSSGSTPGCSRDCEEPLTSYTPRCNTAWNRLKLSKVTHAHNEGFYVCPGPHRPRWARSCGGPESFYCASWGCETTGRASWKPSSSWDYITVSNNLTSGQATPVCKNNTWCNSLTIRFTSLGKQATSWVTGHWWGLRLYVSGHDPGLIFGIRLKITDSGPRVPIGPNPVLSDQRPPSQPRSPPHSNSTPTETPLTLPEPPPAGVENRLLNLVKGAYQALNLTSPDRTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVASQHKLTLSEVTGRGLCVGAVPKTHQALCNTTQNTSGGSYYLAAPAGTIWACNTGLTPCLSTTVLNLTTDYCVLVELWPRVTYHSPSYVYHQFEGRAKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQLQAAVHDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGVVRDSMAKLRERLNQRQKLFESGQGWFERLFNGSPWFTTLISTIMGPLIVLLLILLLGPCILNRLVQFVKDRISVVQALVLTQQYHQLKSIDPEEMESRE

Gene
env
Protein
Envelope glycoprotein
Organism
Feline leukemia virus (strain B/lambda-B1)
Length
662 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.132 kDa
Sequence
MEGPTHPKPSKDKTFSWDLMILVGVLLRLDVGMANPSPHQIYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDQPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSITGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITLPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGNRLINLVQGTYLALNVTNPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSDPQHKLTISEVSGQGSCIGTVPKTHQALCKKTQKGHKGTHYLAAPSGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFDKTVRLRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFGQLQMAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIKQYDPDQP

Gene
env
Protein
Envelope glycoprotein
Organism
Feline sarcoma virus (strain Gardner-Arnstein)
Length
662 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.15 kDa
Sequence
MESPTHPKPSKDKTLSWNLVFLVGILFTIDIGMANPSPHQVYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDQPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSTTGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGDRLINLVQGTYLALNATDPNRTKDCWLCLVSRPPYYEGIAILGNYSNQTNPPPSCLSIPQHKLTISEVSGQGLCIGTVPKTHQALCNETQQGHTGAHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFAKAARFRREPISLTVALMLGGLTVGGIAAGVGTGTKALIETAQFRQLQMAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIKQYDPDRP

Gene
env
Protein
Envelope glycoprotein
Organism
Feline leukemia virus (strain B/lambda-B1)
Length
662 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.132 kDa
Sequence
MEGPTHPKPSKDKTFSWDLMILVGVLLRLDVGMANPSPHQIYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDQPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSITGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITLPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGNRLINLVQGTYLALNVTNPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSDPQHKLTISEVSGQGSCIGTVPKTHQALCKKTQKGHKGTHYLAAPSGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFDKTVRLRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFGQLQMAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIKQYDPDQP

Gene
env
Protein
Envelope glycoprotein
Organism
Feline sarcoma virus (strain Gardner-Arnstein)
Length
662 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
73.15 kDa
Sequence
MESPTHPKPSKDKTLSWNLVFLVGILFTIDIGMANPSPHQVYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDQPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSTTGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGDRLINLVQGTYLALNATDPNRTKDCWLCLVSRPPYYEGIAILGNYSNQTNPPPSCLSIPQHKLTISEVSGQGLCIGTVPKTHQALCNETQQGHTGAHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFAKAARFRREPISLTVALMLGGLTVGGIAAGVGTGTKALIETAQFRQLQMAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIKQYDPDRP

Gene
env
Protein
Envelope glycoprotein
Organism
Cas-Br-E murine leukemia virus
Length
661 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
72.625 kDa
Sequence
MEGPAFSKSPKDKTIERAFLGVLGILFVTGGLASRDNPHQVYNITWEVTNGEQDTVWAVTGNHPLWTWWPDLTPDLCMLALHGPTHWGLDNHPPYSSPPGPPCCSGDAGAVSGCARDCDEPLTSYSPRCNTAWNRLKLARVTHAPKEGFYICPGSHRPRWARSCGGLDAYYCASWGCETTGRAAWNPTSSWDYITVSNNLTSSQATKACKNNGWCNPLVIRFTGPGKRATSWTTGHFWGLRLYISGHDPGLTFGIRLKVTDLGPRVPIGPNPVLSDQRPPSRPVPARPPPPSASPSTPTIPPQQGTGDRLLNLVQGAYLTLNMTDPTRTQECWLCLVSEPPYYEGVAVLREYTSHETAPANCSSGSQHKLTLSEVTGQGRCLGTVPKTHQALCNRTEPTVSGSNYLVAPEGTLWACSTGLTPCLSTTVLNLTTDYCVLVELWPKVTYHSPDYVYTQFEPGARFRREPVSLTLALLPEGLTMGGIAAGVGTGTTALVATQQFQQLQAAMHNDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLNQRQKLFESGQGWFEGLFNRSPWFTTLISTIMGPLIVLLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPIEYEP

Gene
env
Protein
Envelope glycoprotein
Organism
Koala retrovirus
Length
659 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
72.86 kDa
Sequence
MLLISNPRHLGHPMSPGNWKRLIILLSCVFGGAEMNQQHNNPHQPMTLTWQVLSQTGSVVWEKKAVEPPWTWWPSLEPDVCALVAGLESWDIPELTASASQQARPPDSNYEHAYNQITWGTLGCSYPRARTRIARSQFYVCPRDGRSLSEARRCGGLESLYCKEWGCETAGTAYWQPRSSWDLITVGQGHPTGTCERTGWCNPLKIEFTEPGKRFRNWLQGRTWGLRFYVTGHPGVQLTIRLVITSPPPVVVGPDPVLAEQGPPRKIPFLPRVPVPTLSPPASPIPTVQASPPAPSTPSPTTGDRLFGLVQGAFLALNATNPEATESCWLCLALGPPYYEGIATPGQVTYASTDSQCRWGGKGKLTLTEVSGLGLCIGKVPPTHQHLCNLTIPLNASHTHKYLLPSNRSWWACNSGLTPCLSTSVFNQSNDFCIQIQLVPRIYYHPDGTLLQAYESPHSRNKREPVSLTLAVLLGLGVAAGIGTGSTALIKGPIDLQQGLTSLQIAMDTDLRALQDSISKLEDSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYVDHSGAVRDSMRRLKERLDKRQLEHQKNLSWYEGWFNRSPWLTTLLSALAGPLLLLLLLLTLGPCVINKLVQFINDRVSAVRILVLRHKYQTLDNEDNL

Gene
env
Protein
Envelope glycoprotein
Organism
Feline sarcoma virus (strain SM)
Length
645 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
71.594 kDa
Sequence
MEGPTHPKPFKDKTFSWDLIILVGVVRVLLRLDVGMANPSPHQVYNVTWVITNVQTNSQANATSMLGTLTDAYPTLHVDLCDLVGDTWEPIVLDPSNVKHGARYSSSKYGCKTTDRKKQQQTYPFYVCPGHAPSMGPKGTHCGGAHDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSSQDTSCDKNCNPLVLQFTQKGRQASWDGPKLWGLRLYRTGYDPIALFSVSRQVSTIMPPQAMGPNLVLPEQKPPSRQSQTKSKVATQKPQTNGTTPRSVAPATMSPKRIGTRDRLINLVQGTYLALNATDPNKTKDCWLCLVSRPPYYEGIAILGNYSNQTNPPPSCLSTPQHKLTISEVSGQGLCIGTVPRTHQALCNKTQQGHTGAHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYIYTHFDKAVRFRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQIAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQGGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIQQYDPDRP

Gene
env
Protein
Envelope glycoprotein
Organism
Feline sarcoma virus (strain SM)
Length
645 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
71.594 kDa
Sequence
MEGPTHPKPFKDKTFSWDLIILVGVVRVLLRLDVGMANPSPHQVYNVTWVITNVQTNSQANATSMLGTLTDAYPTLHVDLCDLVGDTWEPIVLDPSNVKHGARYSSSKYGCKTTDRKKQQQTYPFYVCPGHAPSMGPKGTHCGGAHDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSSQDTSCDKNCNPLVLQFTQKGRQASWDGPKLWGLRLYRTGYDPIALFSVSRQVSTIMPPQAMGPNLVLPEQKPPSRQSQTKSKVATQKPQTNGTTPRSVAPATMSPKRIGTRDRLINLVQGTYLALNATDPNKTKDCWLCLVSRPPYYEGIAILGNYSNQTNPPPSCLSTPQHKLTISEVSGQGLCIGTVPRTHQALCNKTQQGHTGAHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYIYTHFDKAVRFRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQIAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQGGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIQQYDPDRP

Gene
env
Protein
Envelope glycoprotein
Organism
Xenotropic MuLV-related virus (isolate VP35)
Length
645 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
69.814 kDa
Sequence
MESPAFSKPLKDKINPWGPLIIMGILVRAGASVQRDSPHQVFNVTWKITNLMTGQTANATSLLGTMTDTFPKLYFDLCDLVGDNWDDPEPDIGDGCRSPGGRKRTRLYDFYVCPGHTVLTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKGQGPCFDSSVGSGSIQGATPGGRCNPLVLEFTDAGKRASWDAPKTWGLRLYRSTGADPVTLFSLTRQVLNVGPRVPIGPNPVITEQLPPSQPVQIMLPRPPRPPPSGAASMVPGAPPPSQQPGTGDRLLNLVEGAYQALNLTSPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVTSQHKLTLSEVTGQGLCIGAVPKTHQALCNTTQKTSDGSYYLASPAGTIWACSTGLTPCLSTTVLNLTTDYCVLVELWPKVTYHSPNYVYGQFGKKTKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATKQFEQLQAAIHTDLGALEKSVSALEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKKECCFYADHTGVVRDSMAKLRERLNQRQKLFESGQGWFEGLFNRSPWFTTLISTIMGPLIVLLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKSIDPEEVESRE

Gene
env
Protein
Envelope glycoprotein
Organism
Xenotropic MuLV-related virus (isolate VP42)
Length
645 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
69.887 kDa
Sequence
MESPAFSKPLKDKINPWGPLIIMGILVRAGASVQRDSPHQVFNVTWKITNLMTGQTANATSLLGTMTDTFPKLYFDLCDLVGDNWDDPEPDIGDGCRSPGGRKRTRLYDFYVCPGHTVLTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKGQGPCFDSSVGSGSIQGATPGGRCNPLVLEFTDAGKRASWDAPKTWGLRLYRSTGADPVTLFSLTRQVLNVGPRVPIGPNPVITEQLPPSQPVQIMLPRPPRPPPSGAASMVPGAPPPSQQPGTGDRLLNLVEGAYQALNLTSPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVTSQHKLTLSEVTGQGLCIGAVPKTHQALCNTTQKTSDGSYYLASPAGTIWACSTGLTPCLSTTVLNLTTDYCVLVELWPKVTYHSPNYVYGQFEKKTKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATKQFEQLQAAIHTDLGALEKSVSALEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGVVRDSMAKLRERLNQRQKLFESGQGWFEGLFNRSPWFTTLISTIMGPLIVLLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKSIDPEEVESRE

Gene
env
Protein
Envelope glycoprotein
Organism
Xenotropic MuLV-related virus (isolate VP62)
Length
645 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
69.876 kDa
Sequence
MESPAFSKPLKDKINPWGPLIIMGILVRAGASVQRDSPHQVFNVTWKITNLMTGQTANATSLLGTMTDTFPKLYFDLCDLVGDNWDDPEPDIGDGCRSPGGRKRTRLYDFYVCPGHTVLTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKGQGPCFDSSVGSGSIQGATPGGRCNPLVLEFTDAGKRASWDAPKTWGLRLYRSTGADPVTLFSLTRQVLNVGPRVPIGPNPVITEQLPPSQPVQIMLPRTPRPPPSGAASMVPGAPPPSQQPGTGDRLLNLVEGAYLALNLTSPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVTSQHKLTLSEVTGQGLCIGAVPKTHQALCNTTQKTSDGSYYLASPAGTIWACSTGLTPCLSTTVLNLTTDYCVLVELWPKVTYHSPNYVYGQFEKKTKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATKQFEQLQAAIHTDLGALEKSVSALEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGVVRDSMAKLRERLNQRQKLFESGQGWFEGLFNRSPWFTTLISTIMGPLIVLLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKSIDPEEVESRE

Gene
env
Protein
Envelope glycoprotein
Organism
Feline leukemia virus (strain A/Glasgow-1)
Length
642 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
71.053 kDa
Sequence
MESPTHPKPSKDKTLSWNLAFLVGILFTIDIGMANPSPHQIYNVTWVITNVQTNTQANATSMLGTLTDAYPTLHVDLCDLVGDTWEPIVLNPTNVKHGARYSSSKYGCKTTDRKKQQQTYPFYVCPGHAPSLGPKGTHCGGAQDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSSQDNSCEGKCNPLVLQFTQKGRQASWDGPKMWGLRLYRTGYDPIALFTVSRQVSTITPPQAMGPNLVLPDQKPPSRQSQTGSKVATQRPQTNESAPRSVAPTTMGPKRIGTGDRLINLVQGTYLALNATDPNKTKDCWLCLVSRPPYYEGIAILGNYSNQTNPPPSCLSTPQHKLTISEVSGQGMCIGTVPKTHQALCNKTQQGHTGAHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFAKAVRFRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQMAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIKQYDPDRP

Gene
env
Protein
Envelope glycoprotein
Organism
Feline leukemia virus (strain A/Glasgow-1)
Length
642 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
71.053 kDa
Sequence
MESPTHPKPSKDKTLSWNLAFLVGILFTIDIGMANPSPHQIYNVTWVITNVQTNTQANATSMLGTLTDAYPTLHVDLCDLVGDTWEPIVLNPTNVKHGARYSSSKYGCKTTDRKKQQQTYPFYVCPGHAPSLGPKGTHCGGAQDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSSQDNSCEGKCNPLVLQFTQKGRQASWDGPKMWGLRLYRTGYDPIALFTVSRQVSTITPPQAMGPNLVLPDQKPPSRQSQTGSKVATQRPQTNESAPRSVAPTTMGPKRIGTGDRLINLVQGTYLALNATDPNKTKDCWLCLVSRPPYYEGIAILGNYSNQTNPPPSCLSTPQHKLTISEVSGQGMCIGTVPKTHQALCNKTQQGHTGAHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFAKAVRFRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQMAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLFGPCILNRLVQFVKDRISVVQALILTQQYQQIKQYDPDRP

Gene
env
Protein
Envelope glycoprotein
Organism
Rauscher mink cell focus-inducing virus
Length
640 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
70.072 kDa
Sequence
MACSTFSKPLKDKINPWGPLIILGILIRAGVSVQHDSPHKVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLVGDYWDDPEPDIGDGCRTPGGRRRTRLYDFYVCPGHTVPIGCGGPGEGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDQGPCYDSSVSSDIKGATPGGRCNPLVLEFTDAGKKASWDGPKVWGLRLYRSTGTDPVTRFSLTRRVLNIGPRVPIGPNPVIIDQLPPSRPVQIMLPRPPQPPPPGAASIVPETAPPSQQPGTGDRLLNLVDGAYQALNLTSPDKTQECWLCLVAEPPYYEGVAVLGTYSNHTSAPTNCSVASQHKLTLSEVTGQGLCIGTVPKTHQALCNTTLKTNKGSYYLVAPAGTTWACNTGLTPCLSATVLNRTTDYCVLVELWPRVTYHPPSYVYSQFEKSYRHKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLHAAVQDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLTQRQKLFESSQGWFEGLFNRSPWFTTLISTIMGPLIILLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPLEYEPQ

Gene
env
Protein
Envelope glycoprotein
Organism
Mink cell focus-forming murine leukemia virus (isolate CI-3)
Length
640 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
69.726 kDa
Sequence
MEGPAFSKPLKDKINPWGPLIILGILIRAGVSVQHDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLVGDDWDETGLGCRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPRNQGPCYDSSAVSSDIKGATPGGRCNPLVLEFTDAGKKASWDGPKVWGLRLYRSTGTDPVTRFSLTRQVLNIGPRVPIGPNPVITDQLPPSRPVQIMLPRPPQPPPPGAASIVPETAPPSQQLGTGDRLLNLVNGAYQALNLTSPDKTQECWLCLVAGPPYYEGVAVLGTYSNHTSAPANCSVASQHKLTLSGVAGRGLCIAAFPKTHQALCNTTQKTSDGSYHLAAPAGTIWACNTGLTPCLSTTVLDLTTDYCVLVELWPKVTYHSPSYVYGQFEKKKTKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLQAAMHDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLSQRQKLFESQQGWFEGLFNKSPWFTTLISTIMGPLIILLLILLFGPWILNRLVQFIKDRISVVQALVLTQQYHQLKTIGDCKSRE

Gene
env
Protein
Envelope glycoprotein
Organism
Feline leukemia virus (strain C/Sarma)
Length
639 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
71.162 kDa
Sequence
MESPTHPKPSKDKTFPWNLVFLVGILFQIDMGMANPSPHQVYNVTWVITNVQTNSRANATSMLGTLTDAYPTLYVDLCDLVGDTWEPIAPDPRSWARYSSSTHGCKTTDRKKQQQTYPFYVCPGHAPSMGPKGTYCGGAQDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSNQDNSCKGKCNPLVLQFTQKGRQASWDRPKMWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQTKSKVTTQRPQITSSTPRSVASATMGPKRIGTGDRLINLVQGTYLALNATDPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSTPQHKLTISEVSGQGLCIGTVPKTHQALCKKTQKGHKGTHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYIYTHFDKAVRFRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQIAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLLGPCILNRLVQFVKDRISVVQALILTQQYQQIQQYDSDRP

Gene
env
Protein
Envelope glycoprotein
Organism
Feline leukemia virus (strain C/Sarma)
Length
639 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
71.162 kDa
Sequence
MESPTHPKPSKDKTFPWNLVFLVGILFQIDMGMANPSPHQVYNVTWVITNVQTNSRANATSMLGTLTDAYPTLYVDLCDLVGDTWEPIAPDPRSWARYSSSTHGCKTTDRKKQQQTYPFYVCPGHAPSMGPKGTYCGGAQDGFCAAWGCETTGEAWWKPTSSWDYITVKRGSNQDNSCKGKCNPLVLQFTQKGRQASWDRPKMWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQTKSKVTTQRPQITSSTPRSVASATMGPKRIGTGDRLINLVQGTYLALNATDPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSTPQHKLTISEVSGQGLCIGTVPKTHQALCKKTQKGHKGTHYLAAPNGTYWACNTGLTPCISMAVLNWTSDFCVLIELWPRVTYHQPEYIYTHFDKAVRFRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQIAMHTDIQALEESISALEKSLTSLSEVVLQNRRGLDILFLQEGGLCAALKEECCFYADHTGLVRDNMAKLRERLKQRQQLFDSQQGWFEGWFNKSPWFTTLISSIMGPLLILLLILLLGPCILNRLVQFVKDRISVVQALILTQQYQQIQQYDSDRP

Gene
env
Protein
Envelope glycoprotein
Organism
Mink cell focus-forming murine leukemia virus
Length
636 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
69.113 kDa
Sequence
MEGPAFSKPLKDKINPWGPLIILGILIRAGVSVQHDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLIGDDWDETGLGCRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPRNQGPCYDSSVVSSGIQGATPGGRCNPLVLEFTDAGKKASWDGPKVWGLRLYRSTGIDPVTRFSLTRQVLNIGPRLPIGPNPVITGQLPPSRPVQIRLPRPPQPPPPGAASIVPETAPPSQQPGTGDRLLNLVDGAYQALNLTSPDKTQECWLCLVAGPPYYEGVAVLGTYSNHTSAPANCSVASQHKLTLSEVTGQGLCVGAVPKTHQALCNTTQKTSDGSYYLAAPAGTIWACNTGLTPCLSTTVLNLTTDYCVLVELWPKVTYHSPDYVYTQFEPGARFRREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLQAAVHNDLKEVEKSITNLEKSLTSLSEVALQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLNQRQKLFESGQGWFEGLFNRSPWFTTLISTIMGPLIVLLLILLFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKPIEYEP

Gene
env
Protein
Envelope glycoprotein
Organism
Sheep pulmonary adenomatosis virus
Length
615 amino acids
Function
The envelope proteins induce cell transformation leading to ovine pulmonary adenocarcinoma (OPA), a contagious lung cancer of sheep and goat. They bind to the HYAL2 receptor for cell entry. Env proteins probably do not act as oncogenes by themselves, but may rather liberate an oncogenic factor that would normally be negatively regulated. One mechanism of transformation seems to involve activation of the phosphoinositide-3-OH kinase (PI3K)/Akt pathway but does not involve the virus receptor HYAL2, and the other seems to involve Env binding to HYAL2, HYAL2 degradation, and activation of the MST1R receptor tyrosine kinase, which is normally suppressed by HYAL2.
Mass
69.343 kDa
Sequence
MPKRRAGFRKGWYARQRNSLTHQMQRMTLSEPTSELPTQRQIEALMPYAWNEAHVQPPVTPTNILIMLLLLLQRVQNGAAAAFWAYIPDPPMIQSLGWDREIVPVYVNDTSLLGGKSDIHISPQQANISFYGLTTQYPMCFSYQSQHPHCIQVSADISYPRVTISGIDEKTGKKSYGNGTGPLDIPFCDKHLSIGIGIDTPWTLCRARVASVYNINNANATFLWDWAPGGTPDFPEYRGQHPPIFSVNTAPIYQTELWKLLAAFGHGNSLYLQPNISGTKYGDVGVTGFLYPRACVPYPFMLIQGHMEITLSLNIYHLNCSNCILTNCIRGVAKGEQVIIVKQPAFVMLPVEIAEAWYDETALELLQRINTALSRPKRGLSLIILGIVSLITLIATAVTACVSLAQSIQAAHTVDSLSYNVTKVMGTQEDIDKKIEDRLSALYDVVRVLGEQVQSINFRMKIQCHANYKWICVTKKPYNTSDFPWDKVKKHLQGIWFNTNLSLDLLQLHNEILDIENSPKATLNIADTVDNFLQNLFSNFPSLHSLWKTLIGLGIFVIIIAIVIFVFPCVVRGLVRDFLKMRVEMLHMKYRTMLQHRHLMELLKNKERGAAGDDP

Gene
env
Protein
Envelope glycoprotein gp95
Organism
Avian leukosis virus RSA
Length
606 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
66.325 kDa
Sequence
MEAVIKAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDNCTTLGTDRLVSSADFTGGPDNSTTLTYRKVSCLLLKLNVSMWDEPHELQLLGSQSLPNITNIAQISGITGGCVGFRPQGVPWYLGWSRQEATRFLLRHPSFSKSTEPFTVVTADRHNLFMGSEYCGAYGYRFWNMYNCSQVGRQYRCGNARSPRPGLPEIQCTRRGGKWVNQSQEINESEPFSFTVNCTASSLGNASGCCGKAGTILPGKWVDSTQGSFTKPKALPPAIFLICGDRAWQGIPSRPVGGPCYLGKLTMLAPKHTDILKVLVNSSRTGIRRKRSTSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDVAGMCCFNLSDHSESIQKKFQLMKEHVNKIGVDSDPIGSWLRGLFGGIGEWAVHLLKGLLLGLVVILLLVVCLPCLLQIVCGNIRKMINNSISYHTEYKKLQKACGQPESRIV

Gene
env
Protein
Envelope glycoprotein gp95
Organism
Rous sarcoma virus (strain Prague C)
Length
603 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
65.661 kDa
Sequence
MRRALFLQAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDTNCSTVGTDRLVLSASITGGPDNSTTLTYRKVSCLLLKLNVSMWDEPPELQLLGSQSLPNVTNITQVSGVAGGCVYFAPRATGLFLGWSKQGLSRFLLRHPFTSTSNSTEPFTVVTADRHNLFMGSEYCGAYGYRFWEIYNCSQTRNTYRCGDVGGTGLPETWCRGKGGIWVNQSKEINETEPFSFTANCTGSNLGNVSGCCGEPITILPLGAWIDSTQGSFTKPKALPPAIFLICGDRAWQGIPSRPVGGPCYLGKLTMLAPNHTDILKILANSSRTGIRRKRSVSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDVAGMCCFNLSDHSESIQKKFQLMKKHVNKIGVDSDPIGSWLRGIFGGIGEWAVHLLKGLLLGLVVILLLLVCLPCLLQFVSSSIRKMINSSINYHTEYRKMQGGAV

Gene
env
Protein
Envelope glycoprotein
Organism
Simian retrovirus SRV-1
Length
587 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
64.475 kDa
Sequence
MNFNHHFTWSLVIISQIFQVQAGFGDPREALLEIQQKHGKPCDCAGGYVSSPPTNSLTTVSCSTYTAYSVTNSLKWQCVSTPTTASPTHIGSCPSQCNSQSYDSVHATCYNHYQQCTIGNKTYLTATMIRDKSPSSGDGNVPTILGNNQNLIIAGCPENKKGQVVCWNSQPSVHMSDGGGPQDKVREIIVNKKFEELHKSLFPELSYHPLALPEARGKEKIDAHTFDLLATVHSLLNVSSQRQLAEDCWLCLRSGDPVPLALPYDNTSCSNSTFFFNCSNCSCLITPPFLVQPFNFTHSVCLYADYQNNSFDIDVGLAGFTNCSSYINISKPSSPLCAPNSSVFVCGNNKAYTYLPTNWTGSCVLATLLPDIDIIPGSEPVPIPAIDHFLGRPKRAIQFIPLVIGLGITTAVSTGTAGLGVSLTQYTKLSHQLISDVQAISSTIQDLQDQVDSLAEVVLQNRRGLDLLTAEQGGICLALQEKCCFYANKSGIVRDKIKNLQDDLEKRRKQLIDNPFWTGFHGLLPYVMPLLGPLLCLLLVLSFGPIIFNKLMTFIKHQIESIQAKPIQVHYHRLEQEDHGGSYLNLT

Gene
env
Protein
Envelope glycoprotein
Organism
Mason-Pfizer monkey virus
Length
586 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
63.883 kDa
Sequence
MNFNYHFIWSLVILSQISQVQAGFGDPREALAEIQQKHGKPCDCAGGYVSSPPINSLTTVSCSTHTAYSVTNSLKWQCVSTPTTPSNTHIGSCPGECNTISYDSVHASCYNHYQQCNIGNKTYLTATITGDRTPAIGDGNVPTVLGTSHNLITAGCPNGKKGQVVCWNSRPSVHISDGGGPQDKARDIIVNKKFEELHRSLFPELSYHPLALPEARGKEKIDAHTLDLLATVHSLLNASQPSLAEDCWLCLQSGDPVPLALPYNDTLCSNFACLSNHSCPLTPPFLVQPFNFTDSNCLYAHYQNNSFDIDVGLASFTNCSSYYNVSTASKPSNSLCAPNSSVFVCGNNKAYTYLPTNWTGSCVLATLLPDIDIIPGSEPVPIPAIDHFLGKAKRAIQLIPLFVGLGITTAVSTGAAGLGVSITQYTKLSHQLISDVQAISSTIQDLQDQVDSLAEVVLQNRRGLDLLTAEQGGICLALQEKCCFYANKSGIVRDKIKNLQDDLERRRRQLIDNPFWTSFHGFLPYVMPLLGPLLCLLLVLSFGPIIFNKLMTFIKHQIESIQAKPIQVHYHRLEQEDSGGSYLTLT

Gene
env
Protein
Envelope glycoprotein
Organism
Mouse intracisternal a-particle MIAE
Length
584 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
65.025 kDa
Sequence
MVQKMLTSRGLFLILTMLNLSQVPSIMGEQRWAILSTFPKPMPVRHDAIVFPKFFTTNKTVDLPYLLYDPTAPLGENRSLLEQGSLCFQINGPGNCINLTARALGKFNEHRGWVSTTQDTSNVEITFTNRTFWQEVNWVNGTFLPPNFSDKEHLHQPKIAPHCSLEDEGLILPWSDCQSSIIRWVDQSKTFSFSPNMIDDPEKEFVMKKGLFIQDFRMHPFHKWVLCGVNGSCTELNPLIFIQGGAVGKASFTGISRFAQYWGIHDASQDSYGYTNTSVEITGFNKTLVNQINYPSTPVCVYPPFLFILSNDSFEVCSNDSCWISQCWDVTKNTRAMVARIPRWIPVPVETPSTLSMFRQKRDFGITAAMIIAISASAAAATAAGYAMVSAVSGTKLNQLSADLADAITVQTSASTKLKGGLMILNQCLDLAEEQIGVLHQMAQLGCERKLEALCITSVQYENFTYAANLSRQLSLYLAGNWSERFDETLEALIAAVLKINSTRMDLSLTEGLSSWISSAFSYFKEWVGVGLFGVATCCGLVVMLWLVCKLRTQQTRDKVVITQALAAIEQGASPEIWLSMLKN

Gene
env
Protein
Envelope glycoprotein
Organism
Avian reticuloendotheliosis virus
Length
582 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
64.138 kDa
Sequence
MDCLTDLRSTEGKVDQAGKTLILLVVWWGFGTTAEGHPLQQLWELPCDCSGGYVSPDLPITPTPSIAVASPLPDLRVWLQGSWGWGGGFRQQWECVFKPKIIPSVQEQPGPCECLTIATQMHSTCYEKAQECTLLGKTYFTAILQKTKLGSYEDGPNKLLQASCTGIWETSMLGPRCPCVCLDGGGPTDRFGRICAEGLEEIIRHSYPSVQYHPLALPRPRGVDLDPQTSDILEATHQVLNATNPQLAENCWLCMTLGTQSPQPSRRMAMSLSMEIAVLASLSGATHRVNRCQLLCREADNRTGIPVGYVHFTNCTSIQESLTRRVIYEILRDYVLHRVMYLCVEQHAYTALPNKWIGLCILASIVPDMSIIPGEEPIPLPSIEYTAGRHKRAVQFIPLLVGLGITGATLAGGTGLGVSVHTYHKLSNQLIEDVQALSGTINDLQDQIDSLAEVVLQNRRGLDLLTAEQGGICLALQEKCCFYANKSGIVRDKIRKLQEDLLARKRALYDNPLWNGLNGFLPYLLPSLGPLFGLILFLTLGPCIRKTLTRIIHDKIQGSKNPRISPAVQATPNRDGYPRSMV

Gene
env
Protein
Envelope glycoprotein
Organism
Squirrel monkey retrovirus
Length
575 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
62.245 kDa
Sequence
MLCILILLLHPRLCPVTKGGLGKPSGDIYTALFGAPCDCKGGTQTNNYATPTYTQVTDCGDKNAYLTYDTNWNGVSSPKWLCVRKPPSIPVINGRPGPCPSECTNNIKSQMHSSCYSSFSQCTQGNNTYFTAILQRTKSTSETNPVTSGLQPHGVLQAGCDGTVGKSVCWNQQAPIHVSDGGGPQDAVRELYVQKQIELVIQSQFPKLSYHPLARSKPRGPDIDAQMLDILSATHQALNISNPSLAQNCWLCLNQGTSMPLAFPVNISSFNASQNNCTPSLPFRVQPMPSQVYPCFFKGAQNNSFDIPVGVANFVNCSSSSNHSEALCPGPGQAFVCGNNLAFTALPANWTGSCVLAALLPDIDIISGDDPVPIPTFDYIAGRQKRAVTLIPLLVGLGVSTAVATGTAGLGVAVQSYTKLSHQLINDVQALSSTINDLQDQLDSLAEVVLQNRRGLDLLTAEQGGICLALQERCCFYANKSGIVRDKIKNLQEDLEKRRKALADNLFLTGLNGLLPYLLPFLGPLFAIILFFSFAPWILRRVTALIRDQLNSLLGKPIQIHYHQLATRDLEYGRL

Gene
env
Protein
Envelope glycoprotein
Organism
Simian retrovirus SRV-2
Length
574 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
62.952 kDa
Sequence
MTLKDIPFWRVLLIFQTARVYAGFGDPREAITMIHQQHGKPCDCAGGYVNAAPTVYLAAVSCSSHTAYQPSDSLKWRCVSNPTLANGENIGNCPCKTFKESVHSSCYTAYQECFFGNKTYYTAILASNRAPTIGTSNVPTVLGNTHNLLSAGCTGNVGQPICWNPKAPVHISDGGGPQDKAREIAVQKRLEEIHKSLFPELRYHPLALPKARGKEKIDAQTFNLLTATYSLLNKSNPNLANECWLCLPSGNPIPLAIPSNDSFLGSNLSCPIIPPLLVQPLEFMNLINASCFYSPFQNNSFDVDVGLVEFANCSTTLNISHSLCAPNSSVFVCGNNKAYTYLPSNWTGTCVLATLLPDIDIVPGDAPVPVPAIDHYLHRARRAVQFIPLLVGLGITTAVSTGTAGLGYSITQYTKLSRQLISDVQAISSTIQDLQDQVDSLAEVVLQNRRGLDLLTAEQGGICLALQEKCCFYANKSGIVRDKIKRLQEDLEKRRKEIIDNPFWTGLHGLLPYLLPLLGPLFCLLLLITFGPLIFNKIITFVKQQIDAIQAKPIQVHYHRLEQEDNGGVYLRVS

Gene
env
Protein
Envelope glycoprotein
Organism
Simian retrovirus SRV-2 (isolate 2R-18B1)
Length
574 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
63.014 kDa
Sequence
MTVKDIPFWRVLLIFQTARVYAGFGDPREAITIIHQQHGKPCDCAGGYVITAPTVYLATVSCSSHTAYQPSDSLKWRCVSNPTLANGENIGNCPCQTFKESVHSSCYTTYQECFFGNKTYYTAILASNRAPTIGTSNVPTVLGNTHNLLSAGCTGTVGQHICWNPKAPVHISDGGGPQDKAREIAVQKRLEEIHRSLFPELRYHPLALPKARGKEKIDAQTFNLLTATYSLLNKSNPNLANECWLCLPSGNPVPLAIPSNDSFLGSNLSCPIIPPLLVQPLEFINLINASCLYSPSQNNSFDVDVGLVEFTNCSTTLNISHSLCAPNSSVFVCGNNKAYTYLPTNWTGTCVLATLLPDIDIVPGDAPVPVPAIDHYLHRARRAVQFIPLLVGLGITTAVSTGTTGLGYSITQYTKLSRQLISDVQAISSTIQDLQDQVDSLAEVVLQNRRGLDLFTAEQGGICLALQEKCCFYANKSGIVRDKIKALQEDLEKRRKEIIDNPFWTGLHGLLPYLLPLLRPLLCLLLLITFGPLIFNKIIAFVKQQMDAIQAKPIQVHYHRLEQEDNGGVYLRVS

Gene
env
Protein
Envelope glycoprotein
Organism
Avian spleen necrosis virus
Length
567 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
61.597 kDa
Sequence
MDCLTNLRSAEGKVDQASKILILLVAWWGFGTTAEGYPLQQLWELPCDCSGGYVSSIPTYYTYSLDCGGSTAYLTYGSGTGSWSWGGGFKQQWECVFKPKIIPSVQGQPGPCPSECLQIATQMHSTCYEKTQECTLLGKTYFTAILQKTKLGSYEDGPNKLIQASCTGTVGKPVCWDPVAPVYVSDGGGPTDMIREESVRERLEEIIRHSYPSVQYHPLALPRSRGVDLDPQTSDILEATHQVLNATNPKLAENCWLCMTLGTPIPAAIPTNGNVTLDGNCSLSLPFGCNPPGSIDVSCYAGEADNRTGIPVGYVHFTNCTSIQEVTNETSQMGNLTRLCPPPGHVFVCGNNMAYTALPNKWIGLCILASIVPDISIISGEEPIPLPSIEYTARRHKRAVQFIPLLVGLGISGATLAGGTGLGVSVHTYHKLSNQLIEDVQALSGTINDLQDQIDSLAEVVLQNRRGLDLLTAEQGGICLALQEKCCFYANKSGIVRDKIRKLQEDLIERKRALYDNPLWSGLNGFLPYLLPLLGPLFGLILFLTLGPCIMKTLTRIIHDKIQAVKS

Gene
env
Protein
Envelope glycoprotein
Organism
Baboon endogenous virus (strain M7)
Length
563 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
61.879 kDa
Sequence
MGFTTKIIFLYNLVLVYAGFDDPRKAIELVQKRYGRPCDCSGGQVSEPPSDRVSQVTCSGKTAYLMPDQRWKCKSIPKDTSPSGPLQECPCNSYQSSVHSSCYTSYQQCRSGNKTYYTATLLKTQTGGTSDVQVLGSTNKLIQSPCNGIKGQSICWSTTAPIHVSDGGGPLDTTRIKSVQRKLEEIHKALYPELQYHPLAIPKVRDNLMVDAQTLNILNATYNLLLMSNTSLVDDCWLCLKLGPPTPLAIPNFLLSYVTRSSDNISCLIIPPLLVQPMQFSNSSCLFSPSYNSTEEIDLGHVAFSNCTSITNVTGPICAVNGSVFLCGNNMAYTYLPTNWTGLCVLATLLPDIDIIPGDEPVPIPAIDHFIYRPKRAIQFIPLLAGLGITAAFTTGATGLGVSVTQYTKLSNQLISDVQILSSTIQDLQDQVDSLAEVVLQNRRGLDLLTAEQGGICLALQEKCCFYVNKSGIVRDKIKTLQEELERRRKDLASNPLWTGLQGLLPYLLPFLGPLLTLLLLLTIGPCIFNRLTAFINDKLNIIHAMVLTQQYQVLRTDEEAQD

Gene
env
Protein
Envelope glycoprotein
Organism
Feline sarcoma virus (strain Snyder-Theilen)
Length
534 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.349 kDa
Fragment
single
Sequence
MEGPTHPKPSKDKTFSWDLMILVGVLLRLDVGMANPSPHQIYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDHPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSITGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGNRLINLVQGTYLALNVTNPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSDPQHKLTISEVSGQGLCIGTVPKTHQALCKKTQKGHKGTHYLAAPSGTYWACNTGLIPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFDKTVRLRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQMAMHTDIQALEESISALEKSLTSLSEVVL

Gene
env
Protein
Envelope glycoprotein
Organism
Feline sarcoma virus (strain Snyder-Theilen)
Length
534 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.349 kDa
Fragment
single
Sequence
MEGPTHPKPSKDKTFSWDLMILVGVLLRLDVGMANPSPHQIYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDHPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSITGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGNRLINLVQGTYLALNVTNPNKTKDCWLCLVSRPPYYEGIAVLGNYSNQTNPPPSCLSDPQHKLTISEVSGQGLCIGTVPKTHQALCKKTQKGHKGTHYLAAPSGTYWACNTGLIPCISMAVLNWTSDFCVLIELWPRVTYHQPEYVYTHFDKTVRLRREPISLTVALMLGGLTVGGIAAGVGTGTKALLETAQFRQLQMAMHTDIQALEESISALEKSLTSLSEVVL

Gene
env
Protein
Envelope glycoprotein
Organism
Bovine leukemia virus
Length
515 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.64 kDa
Sequence
MPKERRSRRRPQPIIRWVSLTLTLLALCQPIQTWRCSLSLGNQQWMTTYNQEAKFSISIDQILEAHNQSPFCPRSPRYTLDFVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADHFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISGSGPGLALPDAQIFWVNTSLFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTVSSAPPTRVRRSPVAALTLGLALSVGLTGINVAVSALSHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQSLCPTINEPCCFLRIQNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKCLTSRLLKLLRQAPHFPEISFPPKPDSDYQALLPSAPEIYSHLSPTKPDYINLRPCP

Gene
env
Protein
Envelope glycoprotein
Organism
Bovine leukemia virus (isolate American FLK)
Length
515 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.485 kDa
Sequence
MPKKRRSRRRPQPIIRWVSLTLTLLALCRPIQTWRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPFCAKSPRYTLDSVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADRFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISSSGPGLALPDAQIFWVNTSSFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTASSAPPTRVRRSPVAALTLGLALSVGLTGINVAVSALSHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQSLCPTINEPCCFLRIQNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKCLTSRLLKLLRQAPHFPEISLTPKPDSDYQALLPSAPEIYSHLSPVKPDYINLRPCP

Gene
env
Protein
Envelope glycoprotein
Organism
Bovine leukemia virus (isolate Australian)
Length
515 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.445 kDa
Sequence
MPKERRSRRRPEPIIRWVSLTLTLLALCQPIQTWRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPFCAKSPRYTLDSVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADRFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISSSGPGLALPDAQIFWVNTSSFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTASSAPPTRVRRSPVAALTLGLALSVGLTGIKVAVSALSHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQSLCPTINEPCCFLRIQNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALLLLFLAPCLIKCLTSRLSKLLRQAPHFPEISFPPKPDSDYQALLPSAPEIYSHLSPTKPDYINLRPCP

Gene
env
Protein
Envelope glycoprotein
Organism
Bovine leukemia virus (isolate American VDM)
Length
515 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.486 kDa
Sequence
MPKERRSRRRPQPIIRWVSLTLTLLALCRPIQTWRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPFCAKSPRYTLDSVNGYPKIYWPPPKGRRRFGARAMVTYDCEPRCPYVGADRFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISSSGPGLALPDAQIFWVNTSSFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTASSAPPTRVRRSPVAALTLGLALSVGLTGINVAVSALSHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQSLCPTINEPCCFLRIQNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKCLTSRLLKLLRQAPHFPEISLTPKPDSDYQALLPSAPEIYSHLSPVKPDYINLRPCP

Gene
env
Protein
Envelope glycoprotein
Organism
Bovine leukemia virus (isolate Belgium LB285)
Length
515 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.581 kDa
Sequence
MPKERRSRRRPQPIIRWVSLTLTLLSLCQPIQTWRCSLSLGNQQWMTTYNQEAKFSIAIDQILEAHNQSPFCPRSPRYTLDFVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADHFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISNSGPGLALPDAQIFWVNTSLFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTASSAPPTRVRRSPAAALTLGLALSVGLTGINVAVSALSHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQSLCPTINEPCCFLRIQNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKCLTSRLLKLLRQAPHFPEISLAPKPDSDYQALLPSAPEIYSHLSPTKPDYINLRPCP

Gene
env
Protein
Envelope glycoprotein
Organism
Bovine leukemia virus (isolate Belgium LB59)
Length
515 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.69 kDa
Sequence
MPKERRSRRRPQPIIRWVSLTLTLLALCQPIQTWRCSLSLGNQQWMTTYNQEAKFFISIDQILEAHNQSPFCPRSPRYTLDFVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADHFDCPHWDNASQADQGSFYVNHQTLFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISSSGPGLALPDAQIFWVNTSLFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTASSAPPTRVRRSPVAALTLGLALSVGLTGINVAVSALSHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQSLCPTINEPCCFLRIQNDSIIRLGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKCLTSRLLKLLRQAPHFPEISFPPKPDSDYQALLPSAPEIYSHLSPTKPDYINLRPCP

Gene
env
Protein
Envelope glycoprotein
Organism
Bovine leukemia virus (isolate Japanese BLV-1)
Length
515 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
58.472 kDa
Sequence
MPKERRSRRRPQPIIRWVSLTLTLLALCRPIQTWRCSLSLGNQQWMTAYNQEAKFSISIDQILEAHNQSPFCAKSPRYTLDSVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADRFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISSSGPGLALPDAQIFWVNSSSFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTASSAPPTRVRRSPVAALTLGLALSVGLTGINVAVSALSHQRLTSLIHVLEQDQQRLITAINQTHYNLLNVASVVAQNRRGLDWLYIRLGFQSLCPTINEPCCFLRIQNDSIILRGDLQPLSQRVSTDWQWPWNWDLGLTAWVRETIHSVLSLFLLALFLLFLAPCLIKCLTSRLLKLLRQAPHFPEISLTPKPDSDYQALLPSAPEIYSHLSPVKPDYINLRPCP

Gene
env
Protein
Retrovirus-related Env polyprotein from transposon gypsy
Organism
Drosophila melanogaster
Length
509 amino acids
Mass
56.852 kDa
Sequence
TFPLQLGSKLCQGKSEHCSITLSLISRFTLMMFIPLVVANARITDFSHANYIPVLDGDVLVFEQRDLLKHSSNLSEYASMIDETQKLSESFPHSHMRKLLEVDTDHLRTLLSVLKVHHRIARSLDFLGTALKVVAGTPDATDLFKIKITEAQLVESNSRQIAINSETQKQINKLTDTINKVINARKGDLVDTPHLYEALLARNRMLSTEIQNLILTITLVKSNIINPTILDHADLKPLVEQDTPIVSLIEASKIRVLQSENSIHILIAYPRVKFSCKKVAVYPVSHQHTILRLDEDTLAECEHDTFAVTGCTDTTHFTFCERSRRETCVRSLHAGNAAQCHTQPSHLREINPVDDGVVIINEAAAHVSTDGSPETLIEGTYLVTFERTATINGSEFVNLRKTLSKQPGIVRSPLLNIVGHDPVLSIPLLHRMSNENLHSIQNLMDDVESEGSPRLWFVAGVVLNFGLIGSLALYLALRRRRASREIQRTIDTFNMTEDGHKLEGGVVNN

Gene
env
Protein
Envelope glycoprotein gp63
Organism
Human T-cell leukemia virus 3 (strain Pyl43)
Length
493 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
54.775 kDa
Sequence
MGKSGLYFSLICFYTLFPSSFGNPSRCTLFIGASSYHSDPCGSNHPRCTWRLDLFSLTKDQSLSPPCPGLVTYSQYHKPYSLYVFPHWIAKPDRRGLGYYSASYSDPCAIQCPYLGCQSWTCPYTGPVSNPHWKYTSDLNFTQEVSSISLHLHFSKCGSSFSFLLDAPGYDPVWLLSSQATQIPPTPAPLIQDSDLQHILEPSIPWSSKILNLILLALKSTNYSCMVCVDRSSLSSWHVLYDPLKAPSSPDPQAQSILRPSLAIPASNITPPFPWTHCYRPPLQAISSENCNNSVILPPFSLSPIPDVSRPRKRRAVPIAIWLVSALAAGTGIAGGVTGSLSLASSKSLLREVDQDIDHLTRAIVKNHDNILRVAQYAAQNRRGLDLLFWEQGGLCKAIQEQCCFLNISNTHVSVLQERPPLEKRVITGWGLNWDLGLSQWAREALQTGITLLALFLLLIVVGPCVIRQLQTLPSRLQHRSQPYSLLNYETNL

Gene
env
Protein
Envelope glycoprotein gp63
Organism
Human T-cell leukemia virus 3 (strain Pyl43)
Length
493 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
54.775 kDa
Sequence
MGKSGLYFSLICFYTLFPSSFGNPSRCTLFIGASSYHSDPCGSNHPRCTWRLDLFSLTKDQSLSPPCPGLVTYSQYHKPYSLYVFPHWIAKPDRRGLGYYSASYSDPCAIQCPYLGCQSWTCPYTGPVSNPHWKYTSDLNFTQEVSSISLHLHFSKCGSSFSFLLDAPGYDPVWLLSSQATQIPPTPAPLIQDSDLQHILEPSIPWSSKILNLILLALKSTNYSCMVCVDRSSLSSWHVLYDPLKAPSSPDPQAQSILRPSLAIPASNITPPFPWTHCYRPPLQAISSENCNNSVILPPFSLSPIPDVSRPRKRRAVPIAIWLVSALAAGTGIAGGVTGSLSLASSKSLLREVDQDIDHLTRAIVKNHDNILRVAQYAAQNRRGLDLLFWEQGGLCKAIQEQCCFLNISNTHVSVLQERPPLEKRVITGWGLNWDLGLSQWAREALQTGITLLALFLLLIVVGPCVIRQLQTLPSRLQHRSQPYSLLNYETNL

Gene
env
Protein
Envelope glycoprotein gp63
Organism
Human T-cell leukemia virus 3 (strain 2026ND)
Length
491 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
54.673 kDa
Sequence
MGKFCLYFCLIYILFSASSGNPSRCTLFIGASSYHSDPCGSDHPRCTWRLDLFSLTRDQSLSPPCPDLVTYSQYHRPYSLYVFPHWITKPNRRGLGYYSASYSDPCAIQCPYLGCQSWTCPYTGPVSSPHWKYSSDLNFTQEVSSISLHLHFSKCGSSFSFLLDAPGYDPVWFLSSQATQAPPTPAPLIQDSDLQHILEPSIPWSSKILNLILLTLKSSNYSCMVCVDRSSLSSWHVLYDPLKAPNPPDPKAQSILRPSLAIPASNVTPPFPWTHCYRPLLQAISSEHCNNSVVLPPFSLSPLPNVSRPRKRRAVPIAIWLVSALAAGTGIAGGVTGSLSLASSKSLLREVDQDIDHLTQAIVKNHDNILRVAQYAAQNRRGLDLLFWEQGGLCKAIQEQCCFLNISNTHVSVLQERPPLEKRVITGWGLNWDLGLSQWAREALQTGITLLALFLLLIVVGPCVIRQLQALPSRLQHRSQPYSLLNYETNL

Gene
env
Protein
Envelope glycoprotein gp63
Organism
Human T-cell leukemia virus 3 (strain 2026ND)
Length
491 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
54.673 kDa
Sequence
MGKFCLYFCLIYILFSASSGNPSRCTLFIGASSYHSDPCGSDHPRCTWRLDLFSLTRDQSLSPPCPDLVTYSQYHRPYSLYVFPHWITKPNRRGLGYYSASYSDPCAIQCPYLGCQSWTCPYTGPVSSPHWKYSSDLNFTQEVSSISLHLHFSKCGSSFSFLLDAPGYDPVWFLSSQATQAPPTPAPLIQDSDLQHILEPSIPWSSKILNLILLTLKSSNYSCMVCVDRSSLSSWHVLYDPLKAPNPPDPKAQSILRPSLAIPASNVTPPFPWTHCYRPLLQAISSEHCNNSVVLPPFSLSPLPNVSRPRKRRAVPIAIWLVSALAAGTGIAGGVTGSLSLASSKSLLREVDQDIDHLTQAIVKNHDNILRVAQYAAQNRRGLDLLFWEQGGLCKAIQEQCCFLNISNTHVSVLQERPPLEKRVITGWGLNWDLGLSQWAREALQTGITLLALFLLLIVVGPCVIRQLQALPSRLQHRSQPYSLLNYETNL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.948 kDa
Sequence
MGKFLATLILFFQFCPLIFGDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWTKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQHDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGVAGGITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCRFPNITNSHVPILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLIKPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.912 kDa
Sequence
MGKFLATLILFFQFCPLILGDYSPSCCTLTVGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSHLNINLHFSKCGFSFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLSHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSPSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGVAGRITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (isolate Zaire EL subtype B)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.946 kDa
Sequence
MGKFLATLILFFQFCPLILSDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGMAGGITGSMSLASGRSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (isolate Melanesia mel5 subtype C)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.946 kDa
Sequence
MGKFLATLILFFQFCPLILSDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGMAGGITGSMSLASGRSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (strain Japan MT-2 subtype A)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.856 kDa
Sequence
MGKFLATLILFFQFCPLILGDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGVAGGITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (isolate Caribbea CH subtype A)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.87 kDa
Sequence
MGKFLATLILFFQFCPLILGDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVAYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTTPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAIGAGVAGGITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSMLQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.948 kDa
Sequence
MGKFLATLILFFQFCPLIFGDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWTKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQHDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGVAGGITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCRFPNITNSHVPILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLIKPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.912 kDa
Sequence
MGKFLATLILFFQFCPLILGDYSPSCCTLTVGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSHLNINLHFSKCGFSFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLSHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSPSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGVAGRITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (isolate Zaire EL subtype B)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.946 kDa
Sequence
MGKFLATLILFFQFCPLILSDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGMAGGITGSMSLASGRSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (isolate Melanesia mel5 subtype C)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.946 kDa
Sequence
MGKFLATLILFFQFCPLILSDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGMAGGITGSMSLASGRSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (strain Japan MT-2 subtype A)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.856 kDa
Sequence
MGKFLATLILFFQFCPLILGDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVSYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTAPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAMGAGVAGGITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSILQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp62
Organism
Human T-cell leukemia virus 1 (isolate Caribbea CH subtype A)
Length
488 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
53.87 kDa
Sequence
MGKFLATLILFFQFCPLILGDYSPSCCTLTIGVSSYHSKPCNPAQPVCSWTLDLLALSADQALQPPCPNLVAYSSYHATYSLYLFPHWIKKPNRNGGGYYSASYSDPCSLKCPYLGCQSWTCPYTGAVSSPYWKFQQDVNFTQEVSRLNINLHFSKCGFPFSLLVDAPGYDPIWFLNTEPSQLPPTTPPLLPHSNLDHILEPSIPWKSKLLTLVQLTLQSTNYTCIVCIDRASLSTWHVLYSPNVSVPSSSSTPLLYPSLALPAPHLTLPFNWTHCFDPQIQAIVSSPCHNSLILPPFSLSPVPTLGSRSRRAVPVAVWLVSALAIGAGVAGGITGSMSLASGKSLLHEVDKDISQLTQAIVKNHKNLLKIAQYAAQNRRGLDLLFWEQGGLCKALQEQCCFLNITNSHVSMLQERPPLENRVLTGWGLNWDLGLSQWAREALQTGITLVALLLLVILAGPCILRQLRHLPSRVRYPHYSLINPESSL

Gene
env
Protein
Envelope glycoprotein gp63
Organism
Human T-cell leukemia virus 2
Length
486 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
54.158 kDa
Sequence
MGNVFFLLLFSLTHFPLAQQSRCTLTIGISSYHSSPCSPTQPVCTWNLDLNSLTTDQRLHPPCPNLITYSGFHKTYSLYLFPHWIKKPNRQGLGYYSPSYNDPCSLQCPYLGCQAWTSAYTGPVSSPSWKFHSDVNFTQEVSQVSLRLHFSKCGSSMTLLVDAPGYDPLWFITSEPTQPPPTSPPLVHDSDLEHVLTPSTSWTTKILKFIQLTLQSTNYSCMVCVDRSSLSSWHVLYTPNISIPQQTSSRTILFPSLALPAPPSQPFPWTHCYQPRLQAITTDNCNNSIILPPFSLAPVPPPATRRRRAVPIAVWLVSALAAGTGIAGGVTGSLSLASSKSLLLEVDKDISHLTQAIVKNHQNILRVAQYAAQNRRGLDLLFWEQGGLCKAIQEQCCFLNISNTHVSVLQERPPLEKRVITGWGLNWDLGLSQWAREALQTGITILALLLLVILFGPCILRQIQALPQRLQNRHNQYSLINPETML

Gene
env
Protein
Retrovirus-related Env polyprotein from transposon 297
Organism
Drosophila melanogaster
Length
471 amino acids
Mass
55.246 kDa
Sequence
TLNFTGTWYPITLLFILITAVHGQQIQINNIDTNHGYLLFSDKPVQIPSSFEHHSLKINLTEIDIVVDYFEQRLRTDYHAPQINFLYNKIKRELARITLKHRNKRGFINIVGSGFKYLFGTLDENDRVEIQKKLEINVHNSVKLHELNDAIRLINDGMQKIQNYENNHTIIDSLLFELMQFTEYIEDLEMAMQLSRLGLFNPKLLNYDKLENVNSQNILNIKTSTWINYNDNQVLIISHIPIYLSLISTIKIIPYPDSNGYQLDYTDTQSYFEKENKVYNTENKEVKNECVTNIIKHLNPICNFKPVHTNEIIKYIEPNTIVTWNLTQTILNQNCQNSINKIKIEGNKMIRVTQCKIEINNINFSETLLEPEIDLTPLYTPLNITKIKIVKHNDIIEMISENNITLYIQMIIVIIALILLYSYLRYVSFKPFMMLYAKLKIRKNQNQNTPQQTEIEEIPFPTLYPSIPAQV

Gene
env
Protein
Truncated surface protein
Organism
Human immunodeficiency virus type 1 group M subtype U (isolate Z3)
Length
460 amino acids
Mass
51.298 kDa
Sequence
MRVKEIQRNYQHLWKWSLIILGMIMICKAIEKSWVTVYYGVPVWKDAETTLFCASDAKAYEKESHNVWATHACVPSDPSPQELVLGNVTENFNMWKNKMVEQMHEDIISLWDQSLKPCVKLTFLCVTLNCIDVKNSTNNNTEEATITNCSFKVPTELKDKTETVHTLFYKLDVVPLNVTNNSSISSTYRLINCNTSTITQACPKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCKNVSTVQCTHGIRPVVSTQLLLNGSLSEEEVIIRSENITNNAKTIIVQLNETVKINCTRPGSDKKIRQSIRIGPGKVFYAKGGITGQAHCNITDGEWRNTLQQVAIALRRQFNNKSIIFNSSSGGDIEITTHTFNCGGEFFYCNTSELFTGIWNGTWDKNCTSTESNCTGNITLPCRIKQVVRTWQGVGQAMYAPPIEGTIRCSSNITGLLLTRDGGNGKCNSK

Gene
env
Protein
Retrovirus-related Env polyprotein from copia-like transposable element 17.6
Organism
Drosophila melanogaster
Length
456 amino acids
Mass
53.419 kDa
Sequence
MLITTVHGQQIEINNIDTNHGYLLFSDKPVQIPSSFEHHCLRINLTEIDTIADYFEQRLRTDYHAPQVKFLYNKMRRELAGIALRHRNKRGLINIVGSVFKYLFGTLDENDRVDIQRKLETNAHNSVNLHELNDAIQLINDGMQKIQNYENNSNIINSLLYELMQFTEYIEDVEMGMQLSRLGLFNPKLLNYDKLENVNSQNILNIKTSTWINYNDNQLLIISHIPINFSLINTVKIIPYPDSNGYQLEYTDTQSYFERENKVYNNENKEINNECVTNIIKHLKPICNFESIHTDEIIKYIEPNTIVTWNLTQTSLKQNCQNSFNNIKIKGNKMIKVTQCKIEINSIILSENLFKPEIDLTPLYTPLNITKIKTVKHNDINEMISQNNITLYIFMTTVIIILILLYLYLRYVSFNPFMMLYAKLKLRKNQNQNTAQQIEMEDVPLPLLYPSIPAQV

Gene
env
Protein
Envelope glycoprotein
Organism
Friend murine leukemia virus
Length
445 amino acids
Function
The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).
Mass
48.615 kDa
Fragment
single
Sequence
AAPGSSPHQVYNITWEVTNGDRETVWAISGNHPLWTWWPVLTPDLCMLALHGPPHWGLEYQAPYSSPPGPPCCSGSGGSSPGCSRDCNEPLTSLTPRCNTAWNRLKLDQVTHKSSEGFYVCPGSHRPREAKSCGGPDSFYCASWGCETTGRAYWKPSSSWDYITVDNNLTTNQAVQVCKDNKWCNPLAIQFTNAGRQVTSWITGHYWGLRLYVSGQDPGLTFGIRLKYQNLGPRVPIGPNPVLADQLSFPLPNPLPKPAKSPPVSNSTPTMISPSPTPTQPPPAGTGDRLLNLVQGAYQALNLTNPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPTNCSVASQHKLTLSEVTGRGLCIGTVPKTHQALCNTTLKTNKGSYYLVAPAGTTWACNTGLTPCLSATVLNRTTDYCVLVELWPRVTYHPPSYVYSQFEKSYRHKR

Gene
env
Protein
Truncated surface protein
Organism
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Length
421 amino acids
Mass
47.493 kDa
Sequence
MRAKGTRKNYQHLWRWGTMLLGMLMICSAAEQLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLQNVTENFNMWKNNTVEQMHEDIISLWDQSLKPCVKSTPLCVTLNCTDLTNATYANGSSEERGEIRNCSFNVTTIIRNKIQKEYALFYRLDIVPIDKDNTSYTLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNDKKFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEGEVVIRSENFTNNAKTIIVQLNKSVEINCTRPNNNTKKGIAIGPGRTLYAREKIIGDIRQAHCNISKAKWNDTLKQIVTKLKEQFRNKTIVFNQSSGGDPEIVMHSFNCGGEFFYCKTTQLFNSTWLFNSTWNDTERSDNNETIIIPCRIKQIINSGRK

Gene
env
Protein
Glycoprotein 55
Organism
Friend spleen focus-forming virus (isolate 502)
Length
409 amino acids
Function
This envelope-like membrane glycoprotein is responsible for ligand-independent activation of the erythropoietin receptor EPOR leading to the abnormally rapid proliferation of erythroid precursor cells. In the first stage of Friend disease, constitutive activation of EPOR by gp55 causes uncontrolled, polyclonal proliferation of infected erythroblasts, leading to polycythemia (massive increase in the number of mature red cells). Host susceptibility to SSFV-induced erythroblastosis depends on the expression of the truncated isoform of MST1R receptor tyrosine kinase (MST1R isoform sf-Stk). Interaction with SSFV gp 55 results in constitutive tyrosine phosphorylation and activation of MST1R isoform sf-Stk.
Mass
44.777 kDa
Sequence
MKGPAFSKPLKDKINPWGPLIVLGILIRAGVSVQHDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPMLHFDLCDLIGDDWDETGLECRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDRGPCYDSSVSSGVQGATPGGRCNPLVLKFTDAGKKASWDSPKVWGLRLYRPTGIDPVTRFSLTRQVLNIGPRIPIGPNPVIIGQLPPSRPVQVRLPRPPQPPPTGAASMVPGTAPPSQQPGTGDRLLNLVQGAYQALNLTNPDKTQECWLCLVSGPPYYEGVAVLGTNSNHTSALKEKCCFYADHTGLVRDSMAKLRKRLTQRQKLFESSQGWFEGSFNRSPWFTTLISTIMGLLIILLLLLILLLWTLHS

Gene
env
Protein
Glycoprotein 55
Organism
Friend spleen focus-forming virus (strain Lilly-Steeves)
Length
409 amino acids
Function
This envelope-like membrane glycoprotein is responsible for ligand-independent activation of the erythropoietin receptor EPOR leading to the abnormally rapid proliferation of erythroid precursor cells. In the first stage of Friend disease, constitutive activation of EPOR by gp55 causes uncontrolled, polyclonal proliferation of infected erythroblasts, leading to polycythemia (massive increase in the number of mature red cells). Host susceptibility to SSFV-induced erythroblastosis depends on the expression of the truncated isoform of MST1R receptor tyrosine kinase (MST1R isoform sf-Stk). Interaction with SSFV gp 55 results in constitutive tyrosine phosphorylation and activation of MST1R isoform sf-Stk (By similarity).
Mass
44.7 kDa
Sequence
MEGPASSKPLKDKTNPWGPLIILGILIRAGVSVQLDSPHQVSNVTWRVTNLMTGQTANATSLLGTMTEAFPKLYFDLCDLMGDDWDETGLGCRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDQGPCYDSSVSSGVLGATPGGRCNPLVLEFTDAGRKASWDAPKVWGLRLYRSTGTDPVTRFSLTRQVLDIGPRVPIGSNPVTTDQLPLSRPVQTMPPRPLQPPPPGAASIVPETAPPPQQPGAGDRLLNLVDGAYQALNLTNPDKIQECWLCLVSGPPYYEGVVVLGTYFNHTIALKEKCCFYADHTGLVRDSMAKLRKRLTQRQKLFESSRGWFEGSSNRSPWFTTLISAIMGSLIILLLLLILLIWTLYS

Gene
env
Protein
Glycoprotein 55
Organism
Friend spleen focus-forming virus (isolate 502)
Length
409 amino acids
Function
This envelope-like membrane glycoprotein is responsible for ligand-independent activation of the erythropoietin receptor EPOR leading to the abnormally rapid proliferation of erythroid precursor cells. In the first stage of Friend disease, constitutive activation of EPOR by gp55 causes uncontrolled, polyclonal proliferation of infected erythroblasts, leading to polycythemia (massive increase in the number of mature red cells). Host susceptibility to SSFV-induced erythroblastosis depends on the expression of the truncated isoform of MST1R receptor tyrosine kinase (MST1R isoform sf-Stk). Interaction with SSFV gp 55 results in constitutive tyrosine phosphorylation and activation of MST1R isoform sf-Stk.
Mass
44.777 kDa
Sequence
MKGPAFSKPLKDKINPWGPLIVLGILIRAGVSVQHDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPMLHFDLCDLIGDDWDETGLECRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDRGPCYDSSVSSGVQGATPGGRCNPLVLKFTDAGKKASWDSPKVWGLRLYRPTGIDPVTRFSLTRQVLNIGPRIPIGPNPVIIGQLPPSRPVQVRLPRPPQPPPTGAASMVPGTAPPSQQPGTGDRLLNLVQGAYQALNLTNPDKTQECWLCLVSGPPYYEGVAVLGTNSNHTSALKEKCCFYADHTGLVRDSMAKLRKRLTQRQKLFESSQGWFEGSFNRSPWFTTLISTIMGLLIILLLLLILLLWTLHS

Gene
env
Protein
Glycoprotein 55
Organism
Friend spleen focus-forming virus (strain Lilly-Steeves)
Length
409 amino acids
Function
This envelope-like membrane glycoprotein is responsible for ligand-independent activation of the erythropoietin receptor EPOR leading to the abnormally rapid proliferation of erythroid precursor cells. In the first stage of Friend disease, constitutive activation of EPOR by gp55 causes uncontrolled, polyclonal proliferation of infected erythroblasts, leading to polycythemia (massive increase in the number of mature red cells). Host susceptibility to SSFV-induced erythroblastosis depends on the expression of the truncated isoform of MST1R receptor tyrosine kinase (MST1R isoform sf-Stk). Interaction with SSFV gp 55 results in constitutive tyrosine phosphorylation and activation of MST1R isoform sf-Stk (By similarity).
Mass
44.7 kDa
Sequence
MEGPASSKPLKDKTNPWGPLIILGILIRAGVSVQLDSPHQVSNVTWRVTNLMTGQTANATSLLGTMTEAFPKLYFDLCDLMGDDWDETGLGCRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDQGPCYDSSVSSGVLGATPGGRCNPLVLEFTDAGRKASWDAPKVWGLRLYRSTGTDPVTRFSLTRQVLDIGPRVPIGSNPVTTDQLPLSRPVQTMPPRPLQPPPPGAASIVPETAPPPQQPGAGDRLLNLVDGAYQALNLTNPDKIQECWLCLVSGPPYYEGVVVLGTYFNHTIALKEKCCFYADHTGLVRDSMAKLRKRLTQRQKLFESSRGWFEGSSNRSPWFTTLISAIMGSLIILLLLLILLIWTLYS

Gene
env
Protein
Glycoprotein 55
Organism
Rauscher spleen focus-forming virus
Length
408 amino acids
Function
Envelope-like membrane glycoprotein.
Mass
44.94 kDa
Sequence
MEGPAFSKPLKDKINPWGPLIILGILIRAGVSVQHDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLIGDDWDETGLGCRTPGGRKRARTFDFYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPRNQGPCYDSSAVSSDIKGATPGGRCNPLVLEFTDAGKKASWDGPKVWGLRLYRSTGTDPVTRFSLTRQVLNIGPRVPIGPNPVITDQLPPSRPVQIMLPRPPQPPPPGAASIVPETAPPSQQPGTGDRLLNLVDGAYQALNLTNPDKTQDCWLCLVSGPPYYEGVAVLGTYYNHTSALKEECCFYADHTGLVRDSMAKLRERLTQRQKLFESSQGWFEELFNRSTWFTTLIFTIIGPLIILLLILLFWTLHS

Gene
env
Protein
Glycoprotein 42
Organism
Friend spleen focus-forming virus (strain BB6)
Length
356 amino acids
Function
This envelope-like membrane glycoprotein is responsible for ligand-independent activation of the erythropoietin receptor EPOR leading to the abnormally rapid proliferation of erythroid precursor cells. In the first stage of Friend disease, constitutive activation of the EPOR by gp42 causes uncontrolled, polyclonal proliferation of infected erythroblasts, leading to polycythemia (massive increase in the number of mature red cells). Host susceptibility to SSFV-induced erythroblastosis usually depends on the expression of the truncated isoform of MST1R receptor tyrosine kinase (MST1R isoform sf-Stk), but the deletion mutant BB6 apparently can overcome its absence.
Mass
38.778 kDa
Sequence
MEGPAFSKPLKDKINPWGPLIVLGILIRAGVSVQRDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLIGNDWDETRLGCRTPGEGKRARTFDLYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDRGPCYDSSVSSGVQGATPGGRCNPLVLKFTDAGKKASWDAPKVWGLRLYRSTGTDPVTRFSLTRQVLNIGPRVPIGPNPVISDQLPPSRPAQIMLPRPPQPPPPGTASIVPETAPPSQQPGTRDRLLNLVNKAYQALNLTSPDKTQECWLCLVSRPPYYEGVAVLGTNSNHTTLISTIMGLLIILLLLLILLLWTLHS

Gene
env
Protein
Glycoprotein 42
Organism
Friend spleen focus-forming virus (strain BB6)
Length
356 amino acids
Function
This envelope-like membrane glycoprotein is responsible for ligand-independent activation of the erythropoietin receptor EPOR leading to the abnormally rapid proliferation of erythroid precursor cells. In the first stage of Friend disease, constitutive activation of the EPOR by gp42 causes uncontrolled, polyclonal proliferation of infected erythroblasts, leading to polycythemia (massive increase in the number of mature red cells). Host susceptibility to SSFV-induced erythroblastosis usually depends on the expression of the truncated isoform of MST1R receptor tyrosine kinase (MST1R isoform sf-Stk), but the deletion mutant BB6 apparently can overcome its absence.
Mass
38.778 kDa
Sequence
MEGPAFSKPLKDKINPWGPLIVLGILIRAGVSVQRDSPHQVFNVTWRVTNLMTGQTANATSLLGTMTDAFPKLYFDLCDLIGNDWDETRLGCRTPGEGKRARTFDLYVCPGHTVPTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKDRGPCYDSSVSSGVQGATPGGRCNPLVLKFTDAGKKASWDAPKVWGLRLYRSTGTDPVTRFSLTRQVLNIGPRVPIGPNPVISDQLPPSRPAQIMLPRPPQPPPPGTASIVPETAPPSQQPGTRDRLLNLVNKAYQALNLTSPDKTQECWLCLVSRPPYYEGVAVLGTNSNHTTLISTIMGLLIILLLLLILLLWTLHS

Gene
env
Protein
Envelope glycoprotein
Organism
Avian retrovirus RPL30
Length
257 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
27.916 kDa
Fragment
single
Sequence
FPILPGVWVDSTQGNFTKPKALPPAIFLICGDRAWQGIPSRPVGGPCYLGKLTMLAPNHTDIHKILANSSQTGVRHFRSVSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCKDIAGMCCFNLSDHSEAIQKKFQLMKEHVNKIGVDSDPIGSWLRGLFGGIGEWAIHLLKGLLLGLVVILLLVVCLPCLLQFVSSSTRKM

Gene
env
Protein
Envelope glycoprotein
Organism
FBJ murine osteosarcoma virus
Length
211 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
23.708 kDa
Fragment
single
Sequence
QFKRRAKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLQAAMHDDLKKVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLSQRQKLFESQQGWFEGLFNKSPWFTTLISTIMGPLIILLLILLFGPCILNRLVQFIKDRISVVQALVLTQQYHQLKSIDPEKVESRE

Gene
env
Protein
Envelope glycoprotein
Organism
Kirsten murine leukemia virus
Length
201 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
22.389 kDa
Fragment
single
Sequence
RRARYKKEPVSLTLALLLGGLTMGGIAAGVGTGTTALVATQQFQQLQAAIHDDLKEVEKSITNLEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKEECCFYADHTGLVRDSMAKLRERLSQRQKLFESQQGWFEGLFNKSPWFTTLISTVMGPLIILLLILLFGPCILNRLVQFIKDRISVVQALVLTQQYHQLKTIGD

Gene
env
Protein
Envelope glycoprotein
Organism
UR2 sarcoma virus
Length
174 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
19.338 kDa
Fragment
single
Sequence
VAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDIAGMCCFNLSDHSESIQKKFQLMKEHVNKIGVDSDPIGSWLRGLFGGIGEWAVHLLKGLLLGLVVILLLVVCLPCLLQFVSSSIRKMIDNSLGYREERKKFQEAYKQPERVV

Gene
env
Protein
Envelope glycoprotein
Organism
Myeloproliferative leukemia virus
Length
100 amino acids
Mass
10.925 kDa
Sequence
MACSTLPKSPKDKIDPRDLLIPLILFLSLKGARSAAPGSSPHQVYNITWEVTNGDRETVWAISGRLYVSGRDPGLTFGIRLRYQNLGPRVPIGPNPVLAD

Gene
env
Protein
Envelope glycoprotein
Organism
Woolly monkey sarcoma virus
Length
77 amino acids
Function
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Mass
8.985 kDa
Fragment
single
Sequence
LERQKNQNWYEGWFNSSPWFTTLLSTIAGPLLLLLLLLILGPCIINRLVQFINNRVSAVKILVLRQKYQTLDNEDNL