ERVW-1

Syncytin-1

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have 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 membranes (By similarity).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I W env subfamily.

59.939 kDa

MALPYHILLFTVLLPSFTLTAPPPCRCMTSSSPYQEFLWRMRRPGNIDAPSHRSFSKGTPTFTAHTHMPRNCYNSATLCMHANTHYWTGKMINPSCPGGLGVTVCWTYFTHTGMSDGGGVQDQAREKHVKEVISQLTRVHSTSSPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWICLPLDFRPYVSIPVPEEWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTIDTTNSQCIRWVTPPTQIVCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYNYVVSKPRNKRVPILPFVIGAGVLGALGTGIGGITTSTQFYYKLSQELNGDMERVADSLVTLQDQLNSLAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNTGPWGLLSQWMPWILPFLGPLAAIILLLLFGPCIFNLLVNFVSSRIEAVKLQMEPKMQSKTKIYRRPLDRPASPRSDVNDIKCTPPEEISTAQPLLRPNSAGSS

ERVW-1

Syncytin-1

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have 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 membranes.

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I W env subfamily.

59.866 kDa

MALPYHIFLFTVLLPSFTLTAPPPCRCMTSSSPYQEFLWRMQRPGNIDAPSYRSLSKGTPTFTAHTHMPRNCYHSATLCMHANTHYWTGKMINPSCPGGLGVTVCWTYFTQTGMSDGGGVQDQAREKHVKEVISQLTRVHGTSSPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWICLPLNFRPYVSIPVPEQWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTTYTTNSQCIRWVTPPTQIVCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYSYVISKPRNKRVPILPFVIGAGVLGALGTGIGGITTSTQFYYKLSQELNGDMERVADSLVTLQDQLNSLAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNTGPWGLLSQWMPWILPFLGPLAAIILLLLFGPCIFNLLVNFVSSRIEAVKLQMEPKMQSKTKIYRRPLDRPASPRSDVNDIKGTPPEEISAAQPLLRPNSAGSS

ERVW-1

Syncytin-1

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have 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 membranes (By similarity).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I W env subfamily.

60.1 kDa

MALPYHIFLFTVLLPSFTLTAPPPCRCMTSSSPYQEFLWRTQRPGNIDAPLYRSFSKGSPTFTAHTYMPRTCYNSATLCMHANTQYWTGKMINPSCPGGLGVTVCWTYFTHTGMSDGGGVQDQAREKHVKEVISQLTQVHSTSSPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWMCLPLDFRPYVSIPVPEQWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTTDTTNSQCIRWVTPPTRIFCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYNYVVSKPRNKRVPILPFVMGAGVLGALGTGIGSITTSTQFYYKLSRELNGDMERVADSLVTLQDQLNSLAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNIGPWGLLSQWMPWILPFLGPLAAIILLLLFGPCIFNLLVNFVSSRIEAIKLQMEPKMESKTKNYRRSLDWPASPRSDVNDIKGIPPEEISTAQPLLRPNSAGSS

ERVW-1

Syncytin-1

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have 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 membranes (By similarity).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I W env subfamily.

59.981 kDa

MALPYHIFLFTVLLPSFTLTAPPPCRCMTSSSPYQEFLWRMQRPGNIDAPSYRSFSKGTPTFTAHTHMPRNCYHSATLCMHANTHYWTGKIINPSCPGGLGVTVCWTYFTHTGMSDGGGVQDQAREKHVKEVISQLTRVHSASRPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWICLPLNFRPYVSIPVPEQWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTTDTTNSQCIRWVTPPTQIVCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYNYVVSKPRNKRVPILPFVIGAGVLGALGTGIGGITTSTQFYYKLSQELNGDMERVADSLVTLQDQLNSLAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNTGPWGLLSQWMPWILPFLGPLAAIILLLLFGPCIFNLLVNFVSSRIEAVKLQMEPKMQSKTKIYRRPLDRPASPRSDVNDIKGTPPEEILTAQPLLRPNSAGSS

ERVW-1

Syncytin-1

538 amino acids

Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have 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 membranes (By similarity).

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I W env subfamily.

59.909 kDa

MALPYHIFLFTVLLPSFTLTAPPPCRCMTSSSPYQEFLWRMHHPGNIDAPSYRSFSKGTPTFTAHTHMPRNCYNSATLCMHGNTHYWTGKMINPSCPGGLGVTVCWTYFTHTGMSDGGGVQDEAREKHVKEVISQLTQVHSTSSPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWMCLPLAFRPYVSIPVPEQWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTTNTTNSQCIRWVTPPTQVVCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYNYVVSKPRNKRVPILPFVMAAGVLGALGTGIGGITTSTQFYYKLSQELNGDMERVADSLVTLQDQLNSIAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNIGPWGLFSQWMPWILPFLGPLAAIILLLLFGPCIFNLLVNFVSSRIEAVKLQMEPKMQSKTKIYHRPLDWPASPRSDVNDIKGTPPEEISTAQPLLRPNSAGSS