ERVW-1
entrez
30816
canonical
uniprot
Q9UQF0
canonical
ensembl
ENSG00000242950
resolver
ensp
ENSP00000419945
resolver
ensp
ENSP00000474984
resolver
enst
ENST00000493463
resolver
enst
ENST00000603053
resolver
genesymbol
ERVW-1
resolver
genesymbol
ERVWE1
resolver
genesymbol_syn
ERVWE1
resolver
hgnc
HGNC:13525
resolver
uniprot
B2RPD4
resolver
uniprot
D0EYG5
resolver
uniprot
O95244
resolver
uniprot
O95245
resolver
uniprot
Q8NHY7
resolver
uniprot
Q9NRZ2
resolver
uniprot
Q9NZG3
resolver
uniprot_entry
D0EYG5_HUMAN
resolver
uniprot_entry
SYCY1_HUMAN
resolver
uniprot_sec
B2RPD4
resolver
uniprot_sec
O95244
resolver
uniprot_sec
O95245
resolver
uniprot_sec
Q8NHY7
resolver
uniprot_sec
Q9NRZ2
resolver
uniprot_sec
Q9NZG3
resolver
amino_acid_sequence
MALPYHIFLFTVLLPSFTLTAPPPCRCMTSSSPYQEFLWRMQRPGNIDAPSYRSLSKGTPTFTAHTHMPRNCYHSATLCMHANTHYWTGKMINPSCPGGLGVTVCWTYFTQTGMSDGGGVQDQAREKHVKEVISQLTRVHGTSSPYKGLDLSKLHETLRTHTRLVSLFNTTLTGLHEVSAQNPTNCWICLPLNFRPYVSIPVPEQWNNFSTEINTTSVLVGPLVSNLEITHTSNLTCVKFSNTTYTTNSQCIRWVTPPTQIVCLPSGIFFVCGTSAYRCLNGSSESMCFLSFLVPPMTIYTEQDLYSYVISKPRNKRVPILPFVIGAGVLGALGTGIGGITTSTQFYYKLSQELNGDMERVADSLVTLQDQLNSLAAVVLQNRRALDLLTAERGGTCLFLGEECCYYVNQSGIVTEKVKEIRDRIQRRAEELRNTGPWGLLSQWMPWILPFLGPLAAIILLLLFGPCIFNLLVNFVSSRIEAVKLQMEPKMQSKTKIYRRPLDRPASPRSDVNDIKGTPPEEISAAQPLLRPNSAGSS
uniprot
proteins
function
FUNCTION: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449, PubMed:12050356, PubMed:23492904). {ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:12050356, ECO:0000269|PubMed:23492904}.; FUNCTION: 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.
uniprot
proteins
mass_dalton
59866
uniprot
proteins
mutagenesis
MUTAGEN 314..316; /note="RNK->AAA: Complete loss of cleavage between SU and TM. Loss of fusiogenic function."; /evidence="ECO:0000269|PubMed:15827173"; MUTAGEN 317; /note="R->T: Complete loss of cleavage between SU and TM. Loss of fusiogenic function."; /evidence="ECO:0000269|PubMed:15827173"; MUTAGEN 405; /note="C->A: Loss of fusiogenic function. No effect on cleavage between SU and TM."; /evidence="ECO:0000269|PubMed:15827173
uniprot
proteins
post_translational_modification
PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. The intracytoplasmic tail cleavage by the viral protease that is required for the fusiogenic activity of some retroviruses envelope proteins seems to have been lost during evolution. {ECO:0000269|PubMed:15827173}.; PTM: The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion. {ECO:0000305|PubMed:15827173}.
uniprot
proteins
protein_family
Gamma type-C retroviral envelope protein family
uniprot
proteins
protein_family
HERV class-I W env subfamily
uniprot
proteins
pubmed
10693809
uniprot
proteins
pubmed
10708449
uniprot
proteins
pubmed
10826480
uniprot
proteins
pubmed
11238877
uniprot
proteins
pubmed
11531410
uniprot
proteins
pubmed
11990458
uniprot
proteins
pubmed
12050356
uniprot
proteins
pubmed
12620933
uniprot
proteins
pubmed
12664292
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
12970426
uniprot
proteins
pubmed
14557543
uniprot
proteins
pubmed
14757826
uniprot
proteins
pubmed
15254254
uniprot
proteins
pubmed
15452578
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15827173
uniprot
proteins
pubmed
23492904
uniprot
proteins
pubmed
38671230
uniprot
proteins
pubmed
9835022
uniprot
proteins
pubmed
9882319
uniprot
proteins
sequence_length
538
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000305|PubMed:15827173}; Peripheral membrane protein {ECO:0000305|PubMed:15827173}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000305|PubMed:15827173}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Syncytin-1]: Virion {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 444..464; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins