ERLEC1

Endoplasmic reticulum lectin 1

483 amino acids

Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins.

54.858 kDa

MEEGGGGVRSLVPGGPVLLVLCGLLEASGGGRALPQLSDDIPFRVNWPGTEFSLPTTGVLYKEDNYVIMTTAHKEKYKCILPLVTSGDEEEEKDYKGPNPRELLEPLFKQSSCSYRIESYWTYEVCHGKHIRQYHEEKETGQKINIHEYYLGNMLAKNLLFEKEREAEEKEKSNEIPTKNIEGQMTPYYPVGMGNGTPCSLKQNRPRSSTVMYICHPESKHEILSVAEVTTCEYEVVILTPLLCSHPKYRFRASPVNDIFCQSLPGSPFKPLTLRQLEQQEEILRVPFRRNKEEDLQSTKEERFPAIHKSIAIGSQPVLTVGTTHISKLTDDQLIKEFLSGSYCFRGGVGWWKYEFCYGKHVHQYHEDKDSGKTSVVVGTWNQEEHIEWAKKNTARAYHLQDDGTQTVRMVSHFYGNGDICDITDKPRQVTVKLKCKESDSPHAVTVYMLEPHSCQYILGVESPVICKILDTADENGLLSLPN

Erlec1

Endoplasmic reticulum lectin 1

483 amino acids

Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins (By similarity).

54.906 kDa

MEEGDGGLRSLVPGGPLLLVLYGLLEASGGGRALPQLSDDIPFRVNWPGTEFSLPTTGVLYKEDNYIIMTTAHKEKYKCILPLVTSGDEEEEKDYKGPNPRELLEPLFKQSSCSYRIESYWTYEVCHGKHIRQYHEEKETGQKVNIHEYYLGNMLAKNLLYEKEREAKENEKSNEIPTKNIEGQMTPYYPVGMGNGTPCSLKQNRPRSSTVMYICHPESKHEILSVAEVTTCEYEVVILTPLLCSHPKYKFRASPVNDIFCQSLPGSPFKPLTLRQLEQQEEILRVPFRRNKEEDLPSAKEERFPAIHKPIAVGSQPVLTVGTTHISKLTDDQLIKEFLSGSYCFHGGVGWWKYEFCYGKHVHQYHEDKDNGKTSVVVGTWNQEEHVEWAKKNTARAYHLQDDGTQTVRMVSHFYGNGDICDITDKPRQVTVKLKCKESDSPHAVTVYMLEPHSCQYILGVESPVICKILDTADENGLLSLPN

ERLEC1

Endoplasmic reticulum lectin 1

483 amino acids

Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins (By similarity).

54.849 kDa

MEEGGGGVRSLVPGGPVLLVLCGLLEASGGGRALPQLSDDIPFRVNWPGTEFSLPTTGVLYKEDNYVIMTTAHKEKYKCILPLVTSGDEEEEKDYKGPNPRELLEPLFKQSSCSYRIESYWTYEVCHGKHIRQYHEEKETGQKINIHEYYLGNMLAKNLLFEKEREAEEKEKSNEIPTKNIEGQMTPYYPVGMGNGTPCSLKQNRPRSSTVMYICHPESKHEILSVAEVTTCEYEVVILTPLLCSHPKYRFRASPVNDIFCQSLPGSPFKPLTLRQLEQQEEILRVPFRRNKEEDLQSTKEERFPAIHKPIAIGSQPVLTVGTTHISKLTDDQLIKEFLSGSYCFHGGVGWWKYEFCYGKHVHQYHEDKDSGKTSVVVGTWNQEEHIEWAKKNTARAYHLQDDGTQTVRMVSHFYGNGDICDITDKPRQVTVKLKCKESDSPHAVTVYMLEPHSCQYILGVESPVICKILDTADENGLLSLPN

erlec1

Endoplasmic reticulum lectin 1

481 amino acids

Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins (By similarity).

54.698 kDa

MRRSDRLRCAGASLLVVLCGVFRSSFGGRTLPALSDDIPFRLKWPGPDFTLPTAGIPYKEDNYIIMTTADKEKYKCLLPLMANGNEEQDGEYKGPSPGALLEPLFKLSSCSYRIESYWTYEVCHGKYIRQYHEEKETGQKLSIQEYYLGKMMKKSTTEAGENQEEKESAESPKEIYTKNIEGQMTPYYPVEMINGTPCSLKQNQPRSSTVMYICHPESKHEILSVAEVTTCEYEVVILTPLLCNHPKYRFRTSPINDIFCQSMPGSPLRPQSLVKLEHQKEEIKSPLKPNKEEEQQLLREKFSTIHKPVTVGSQQQVTVGTTHISRLTDEQLIKEFLSGSYCFHGGVGWWKYEFCYGKYVHQYHEDKDTGKTTVVVGTWKADEHQEWAKKNLARAYMTTPDGVQTVKTVSHFYGGGDVCEVSEQPRQVIVKLKCKESESPHAVTVYMLEPQTCQYILGVESPVICKILDTADENGLLSIPN

erlec1

Endoplasmic reticulum lectin 1

480 amino acids

Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins (By similarity).

54.454 kDa

MRRSDRFPCAGASLLVVLCGVFPSSFGGRTLPGLSDDIPFRLKWPGPDFTLPTAGIPYKEENYIIMTTADQETYKCMLPLMANGNEEEDREYKGPSPGELLDPLFKLSSCSYRIESYWTYEVCHGKYIRQYHEEKEAGQKLNIQEYYLGKTVKKSPSEAGENQEDKERTEGHKDIHTKNIEGQMTPYYPVEMTNGTPCSLKQNQARSSTVMYICHPEAKHEILSVAEITTCEYEVVILTPLLCNHPKYKFRPSPINDIFCQSMPGSPLRPQSLEKLEHQQEEIKSPLKAKEEEQQLLKEKFSTIHKPVTVGSQQQVTVGTTHISRLTDEQLIKEFLSGSYCFHGGVGWWKYEFCYGKYVHQYHEDKDTGKTTVVVGTWKAEEHLDWAKKNLAKAYMSTADGVQTVKTVSHFYGGGDLCEVNEQPRQVVVKLKCKQSESPHAVTVYMLEPQTCQYILGVESPVICKILDTADENGLLSIPN