Q9N2J8
uniprot
Q9N2J8
canonical
amino_acid_sequence
MILAGRAPSNTSTLMKFYSLLLYSLLFSFPFLYHPLPLPSYLHHTINLTHSLPAASNPSLANNCWLCISLSSSAYIAVPTLQTDRATSPVSLHLRTSFNSPHLYPPEELIYFLDRSSKTSPDISHQPAAALLHIYLKNLSPYINSTPPIFGPLTTQTTIPVAAPLCISRQRPTGIPLGNISPSRCSFTLHLQSPTTHVTETIGVFQLHIIDKPSINTDKLKNVSSNYCLGRHLPYISLHPWLPSPCSSDSPPRPSSCLLTPSPQNNSERLLVDTQRFLIHHENRTSSSMQLAHQSPLQPLTAAALAGSLGVWVQDTPFSTPSHPFSLHLQFCLTQGLFFLCGSSTYMCLPANWTGTCTLVFLTPKIQFANGTKELPVPLMTLTPQKRVIPLIPLMVGLGLSASTIALSTGIAGISTSVTTFRSPSNDFSASITDISQTLSVLQAQVDSLAAVVLQNRRGLGLSILLNEECCFYLNQSGLVYENIKKLKDRAQKLANQASNYAESPWALSNWMSWVLPILSPLIPIFLLLLFGPCIFHLVSQFIQNRIQAITNHSI
uniprot
proteins
function
FUNCTION: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties. {ECO:0000269|PubMed:14557543}.; FUNCTION: SU mediates receptor recognition. {ECO:0000250}.; FUNCTION: TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
60911
uniprot
proteins
post_translational_modification
PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM proteins. {ECO:0000250}.
uniprot
proteins
protein_family
Gamma type-C retroviral envelope protein family
uniprot
proteins
protein_family
HERV class-I H env subfamily
uniprot
proteins
pubmed
11162811
uniprot
proteins
pubmed
12970426
uniprot
proteins
pubmed
14557543
uniprot
proteins
sequence_length
555
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Virion.; SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 516..536; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins