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Syncytin-1 (Endogenous retrovirus group W member 1) (Env-W) (Envelope polyprotein gPr73) (Enverin) (HERV-7q Envelope protein) (HERV-W envelope protein) (HERV-W_7q21.2 provirus ancestral Env polyprotein) (Syncytin) [Cleaved into: Surface protein (SU) (gp50); Transmembrane protein (TM) (gp24)]

 SYCY1_HUMAN             Reviewed;         538 AA.
Q9UQF0; B2RPD4; O95244; O95245; Q8NHY7; Q9NRZ2; Q9NZG3;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 141.
RecName: Full=Syncytin-1;
AltName: Full=Endogenous retrovirus group W member 1;
AltName: Full=Env-W;
AltName: Full=Envelope polyprotein gPr73;
AltName: Full=Enverin;
AltName: Full=HERV-7q Envelope protein;
AltName: Full=HERV-W envelope protein;
AltName: Full=HERV-W_7q21.2 provirus ancestral Env polyprotein;
AltName: Full=Syncytin;
Contains:
RecName: Full=Surface protein;
Short=SU;
AltName: Full=gp50;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
AltName: Full=gp24;
Flags: Precursor;
Name=ERVW-1; Synonyms=ERVWE1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=9882319;
Blond J.-L., Beseme F., Duret L., Bouton O., Bedin F., Perron H.,
Mandrand B., Mallet F.;
"Molecular characterization and placental expression of HERV-W, a new
human endogenous retrovirus family.";
J. Virol. 73:1175-1185(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND VARIANT
ASN-307.
TISSUE=Testis;
PubMed=10693809; DOI=10.1038/35001608;
Sha M., Lee X., Li X.-P., Veldman G.M., Finnerty H., Racie L.,
LaVallie E., Tang X.-Y., Edouard P., Howes S., Keith J.C. Jr.,
McCoy J.M.;
"Syncytin is captive retroviral envelope protein involved in human
placental morphogenesis.";
Nature 403:785-789(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10826480; DOI=10.1089/088922200308738;
Voisset C., Bouton O., Bedin F., Duret L., Mandrand B., Mallet F.,
Paranhos-Baccala G.;
"Chromosomal distribution and coding capacity of the human endogenous
retrovirus HERV-W family.";
AIDS Res. Hum. Retroviruses 16:731-740(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-129; GLN-138;
ASN-307 AND PHE-477.
PubMed=14757826; DOI=10.1073/pnas.0305763101;
Mallet F., Bouton O., Prudhomme S., Cheynet V., Oriol G., Bonnaud B.,
Lucotte G., Duret L., Mandrand B.;
"The endogenous retroviral locus ERVWE1 is a bona fide gene involved
in hominoid placental physiology.";
Proc. Natl. Acad. Sci. U.S.A. 101:1731-1736(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-533, AND VARIANT ASN-307.
TISSUE=Placenta;
PubMed=11990458;
Alliel P.M., Perin J.-P., Goudou D., Bitoun M., Robert B., Rieger F.;
"The HERV-W/7q family in the human genome. Potential for protein
expression and gene regulation.";
Cell. Mol. Biol. 48:213-217(2002).
[8]
IDENTIFICATION.
PubMed=9835022; DOI=10.1016/S0764-4469(99)80026-2;
Alliel P.M., Perin J.-P., Pierig R., Nussbaum J.-L., Menard A.,
Rieger F.;
"Endogenous retroviruses and multiple sclerosis. II. HERV-7q.";
C. R. Acad. Sci. III, Sci. Vie 321:857-863(1998).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10708449; DOI=10.1128/JVI.74.7.3321-3329.2000;
Blond J.-L., Lavillette D., Cheynet V., Bouton O., Oriol G.,
Chapel-Fernandes S., Mandrand B., Mallet F., Cosset F.-L.;
"An envelope glycoprotein of the human endogenous retrovirus HERV-W is
expressed in the human placenta and fuses cells expressing the type D
mammalian retrovirus receptor.";
J. Virol. 74:3321-3329(2000).
[10]
FUNCTION.
PubMed=11238877; DOI=10.1128/JVI.75.7.3488-3489.2001;
An D.S., Xie Y.-M., Chen I.S.Y.;
"Envelope gene of the human endogenous retrovirus HERV-W encodes a
functional retrovirus envelope.";
J. Virol. 75:3488-3489(2001).
[11]
FUNCTION.
PubMed=11531410; DOI=10.1006/viro.2001.1045;
Perron H., Jouvin-Marche E., Michel M., Ounanian-Paraz A., Camelo S.,
Dumon A., Jolivet-Reynaud C., Marcel F., Souillet Y., Borel E.,
Gebuhrer L., Santoro L., Marcel S., Seigneurin J.M., Marche P.N.,
Lafon M.;
"Multiple sclerosis retrovirus particles and recombinant envelope
trigger an abnormal immune response in vitro, by inducing polyclonal
Vbeta16 T-lymphocyte activation.";
Virology 287:321-332(2001).
[12]
FUNCTION.
PubMed=12050356; DOI=10.1128/JVI.76.13.6442-6452.2002;
Lavillette D., Marin M., Ruggieri A., Mallet F., Cosset F.-L.,
Kabat D.;
"The envelope glycoprotein of human endogenous retrovirus type W uses
a divergent family of amino acid transporters/cell surface
receptors.";
J. Virol. 76:6442-6452(2002).
[13]
FUNCTION.
PubMed=14557543; DOI=10.1073/pnas.2132646100;
Blaise S., de Parseval N., Benit L., Heidmann T.;
"Genomewide screening for fusogenic human endogenous retrovirus
envelopes identifies syncytin 2, a gene conserved on primate
evolution.";
Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003).
[14]
FUNCTION.
PubMed=12664292; DOI=10.1007/s00705-002-0960-x;
Ponferrada V.G., Mauck B.S., Wooley D.P.;
"The envelope glycoprotein of human endogenous retrovirus HERV-W
induces cellular resistance to spleen necrosis virus.";
Arch. Virol. 148:659-675(2003).
[15]
TISSUE SPECIFICITY.
PubMed=12970426; DOI=10.1128/JVI.77.19.10414-10422.2003;
de Parseval N., Lazar V., Casella J.-F., Benit L., Heidmann T.;
"Survey of human genes of retroviral origin: identification and
transcriptome of the genes with coding capacity for complete envelope
proteins.";
J. Virol. 77:10414-10422(2003).
[16]
DEVELOPMENTAL STAGE.
PubMed=12620933; DOI=10.1095/biolreprod.102.013078;
Smallwood A., Papageorghiou A., Nicolaides K., Alley M.K.R., Jim A.,
Nargund G., Ojha K., Campbell S., Banerjee S.;
"Temporal regulation of the expression of syncytin (HERV-W),
maternally imprinted PEG10, and SGCE in human placenta.";
Biol. Reprod. 69:286-293(2003).
[17]
FUNCTION.
PubMed=15254254; DOI=10.1093/molbev/msh206;
Bonnaud B., Bouton O., Oriol G., Cheynet V., Duret L., Mallet F.;
"Evidence of selection on the domesticated ERVWE1 env retroviral
element involved in placentation.";
Mol. Biol. Evol. 21:1895-1901(2004).
[18]
INVOLVEMENT IN MULTIPLE SCLEROSIS, AND TISSUE SPECIFICITY.
PubMed=15452578; DOI=10.1038/nn1319;
Antony J.M., Van Marle G., Opii W., Butterfield D.A., Mallet F.,
Yong V.W., Wallace J.L., Deacon R.M., Warren K., Power C.;
"Human endogenous retrovirus glycoprotein-mediated induction of redox
reactants causes oligodendrocyte death and demyelination.";
Nat. Neurosci. 7:1088-1095(2004).
[19]
PROTEOLYTIC PROCESSING OF POLYPROTEIN, SUBUNIT, INTERACTION WITH
CD209/DC-SIGN, AND MUTAGENESIS OF 314-ARG--LYS-316; ARG-317 AND
CYS-405.
PubMed=15827173; DOI=10.1128/JVI.79.9.5585-5593.2005;
Cheynet V., Ruggieri A., Oriol G., Blond J.-L., Boson B., Vachot L.,
Verrier B., Cosset F.-L., Mallet F.;
"Synthesis, assembly, and processing of the Env ERVWE1/syncytin human
endogenous retroviral envelope.";
J. Virol. 79:5585-5593(2005).
[20]
FUNCTION.
PubMed=23492904; DOI=10.1038/srep01462;
Sugimoto J., Sugimoto M., Bernstein H., Jinno Y., Schust D.;
"A novel human endogenous retroviral protein inhibits cell-cell
fusion.";
Sci. Rep. 3:1462-1462(2013).
-!- 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.
-!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of
SU-TM heterodimers attached probably by a labile interchain
disulfide bond. Interacts with the C-type lectin CD209/DC-SIGN.
{ECO:0000269|PubMed:15827173}.
-!- 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}.
-!- TISSUE SPECIFICITY: Expressed at higher level in placental
syncytiotrophoblast. Expressed at intermediate level in testis.
Seems also to be found at low level in adrenal tissue, bone
marrow, breast, colon, kidney, ovary, prostate, skin, spleen,
thymus, thyroid, brain and trachea. Both mRNA and protein levels
are significantly increased in the brain of individuals with
multiple sclerosis, particularly in astrocytes and microglia.
{ECO:0000269|PubMed:10693809, ECO:0000269|PubMed:10708449,
ECO:0000269|PubMed:12970426, ECO:0000269|PubMed:15452578}.
-!- DEVELOPMENTAL STAGE: In placenta, detected at higher level during
early pregnancy and at lower level during late pregnancy.
{ECO:0000269|PubMed:12620933}.
-!- DOMAIN: The cytoplasmic region is essential for the fusiogenic
function.
-!- DOMAIN: The 17 amino acids long immunosuppressive region is
present in many retroviral envelope proteins. Synthetic peptides
derived from this relatively conserved sequence inhibit immune
function in vitro and in vivo (By similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Envelope glycoproteins are synthesized as a 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}.
-!- POLYMORPHISM: All variants have fusogenic properties.
-!- MISCELLANEOUS: Probably involved in the development of multiple
sclerosis (MS). MS is a neurodegenerative disease characterized by
the gradual accumulation of focal plaques of demyelination
particularly in the periventricular areas of the brain. It leads
to physical and cognitive disabilities. Viral particles or
intracellular RNA of HERV-W family members have been detected in
tissue from patients with multiple sclerosis or schizophrenia.
-!- MISCELLANEOUS: Orthologs in Pan troglodytes, Gorilla gorilla,
Pongo pygmaeus and Hylobates moloch.
-!- MISCELLANEOUS: It can make pseudotypes with HIV-1 virions and
confer infectivity. Can also induce cellular resistance to spleen
necrosis virus in vitro.
-!- MISCELLANEOUS: HERV-W family subgenomic RNAs have been observed.
-!- MISCELLANEOUS: This provirus is intergenic, the closest flanking
genes being ODAG and PEX1.
-!- MISCELLANEOUS: The human genome contains a high percentage of
proviral-like elements, also called endogenous retroviruses (ERVs)
that are the genomic traces of ancient infections of the germline
by exogenous retroviruses. Although most of these elements are
defective, some have conserved a functional envelope (env) gene,
most probably diverted by the host for its benefit.
-!- SIMILARITY: Belongs to the gamma type-C retroviral envelope
protein family. HERV class-I W env subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ERVWE1ID40497ch7q21.html";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=A virus for life
- Issue 50 of September 2004;
URL="https://web.expasy.org/spotlight/back_issues/050";
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EMBL; AF072503; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF072505; AAD14545.1; -; mRNA.
EMBL; AF072506; AAD14546.2; -; mRNA.
EMBL; AF072508; AAD14548.1; -; mRNA.
EMBL; AF208161; AAF28334.1; -; mRNA.
EMBL; AF513360; AAM47599.1; -; mRNA.
EMBL; AF156963; AAF74215.1; -; Genomic_DNA.
EMBL; AC007566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY101582; AAM68161.1; -; Genomic_DNA.
EMBL; AY101583; AAM68162.1; -; Genomic_DNA.
EMBL; AY101584; AAM68163.1; -; Genomic_DNA.
EMBL; AY101585; AAM68164.1; -; Genomic_DNA.
EMBL; AF520478; AAQ17561.1; -; Genomic_DNA.
EMBL; AF520480; AAQ17562.1; -; Genomic_DNA.
EMBL; AF520482; AAQ17563.1; -; Genomic_DNA.
EMBL; AF520484; AAQ17564.1; -; Genomic_DNA.
EMBL; AF520486; AAQ17565.1; -; Genomic_DNA.
EMBL; AF520488; AAQ17566.1; -; Genomic_DNA.
EMBL; AF520490; AAQ17567.1; -; Genomic_DNA.
EMBL; AF520492; AAQ17568.1; -; Genomic_DNA.
EMBL; AF520494; AAQ17569.1; -; Genomic_DNA.
EMBL; AF520496; AAQ17570.1; -; Genomic_DNA.
EMBL; AF520498; AAQ17571.1; -; Genomic_DNA.
EMBL; AF520500; AAQ17572.1; -; Genomic_DNA.
EMBL; AF520502; AAQ17573.1; -; Genomic_DNA.
EMBL; AF520504; AAQ17574.1; -; Genomic_DNA.
EMBL; AF520506; AAQ17575.1; -; Genomic_DNA.
EMBL; AF520508; AAQ17576.1; -; Genomic_DNA.
EMBL; AF520510; AAQ17577.1; -; Genomic_DNA.
EMBL; AF520512; AAQ17578.1; -; Genomic_DNA.
EMBL; AF520514; AAQ17579.1; -; Genomic_DNA.
EMBL; AF520516; AAQ17580.1; -; Genomic_DNA.
EMBL; AF520518; AAQ17581.1; -; Genomic_DNA.
EMBL; AF520520; AAQ17582.1; -; Genomic_DNA.
EMBL; AF520522; AAQ17583.1; -; Genomic_DNA.
EMBL; AF520524; AAQ17584.1; -; Genomic_DNA.
EMBL; AF520526; AAQ17585.1; -; Genomic_DNA.
EMBL; AF520528; AAQ17586.1; -; Genomic_DNA.
EMBL; AF520530; AAQ17587.1; -; Genomic_DNA.
EMBL; AF520532; AAQ17588.1; -; Genomic_DNA.
EMBL; AF520534; AAQ17589.1; -; Genomic_DNA.
EMBL; AF520536; AAQ17590.1; -; Genomic_DNA.
EMBL; AF520538; AAQ17591.1; -; Genomic_DNA.
EMBL; AF520540; AAQ17592.1; -; Genomic_DNA.
EMBL; AF520542; AAQ17593.1; -; Genomic_DNA.
EMBL; AF520544; AAQ17594.1; -; Genomic_DNA.
EMBL; AF520546; AAQ17595.1; -; Genomic_DNA.
EMBL; AF520548; AAQ17596.1; -; Genomic_DNA.
EMBL; AF520550; AAQ17597.1; -; Genomic_DNA.
EMBL; AF520552; AAQ17598.1; -; Genomic_DNA.
EMBL; AF520554; AAQ17599.1; -; Genomic_DNA.
EMBL; AF520556; AAQ17600.1; -; Genomic_DNA.
EMBL; AF520558; AAQ17601.1; -; Genomic_DNA.
EMBL; AF520560; AAQ17602.1; -; Genomic_DNA.
EMBL; AF520562; AAQ17603.1; -; Genomic_DNA.
EMBL; AF520564; AAQ17604.1; -; Genomic_DNA.
EMBL; BC137381; AAI37382.1; -; mRNA.
EMBL; AF506835; AAM33413.1; -; mRNA.
CCDS; CCDS5626.1; -.
RefSeq; NP_001124397.1; NM_001130925.1.
RefSeq; NP_055405.3; NM_014590.3.
PDB; 5HA6; X-ray; 2.00 A; A/B=343-435.
PDBsum; 5HA6; -.
ProteinModelPortal; Q9UQF0; -.
SMR; Q9UQF0; -.
STRING; 9606.ENSP00000419945; -.
TCDB; 1.G.9.1.1; the syncytin (syncytin) family.
iPTMnet; Q9UQF0; -.
PhosphoSitePlus; Q9UQF0; -.
BioMuta; ERVW-1; -.
DMDM; 47605755; -.
PaxDb; Q9UQF0; -.
PeptideAtlas; Q9UQF0; -.
PRIDE; Q9UQF0; -.
ProteomicsDB; 85550; -.
Ensembl; ENST00000493463; ENSP00000419945; ENSG00000242950.
Ensembl; ENST00000603053; ENSP00000474984; ENSG00000242950.
GeneID; 30816; -.
KEGG; hsa:30816; -.
UCSC; uc022ahe.2; human.
CTD; 30816; -.
DisGeNET; 30816; -.
EuPathDB; HostDB:ENSG00000242950.6; -.
GeneCards; ERVW-1; -.
HGNC; HGNC:13525; ERVW-1.
MIM; 604659; gene.
neXtProt; NX_Q9UQF0; -.
OpenTargets; ENSG00000242950; -.
PharmGKB; PA27878; -.
eggNOG; ENOG410JCYM; Eukaryota.
eggNOG; ENOG4111CG7; LUCA.
GeneTree; ENSGT00690000102286; -.
HOVERGEN; HBG051487; -.
InParanoid; Q9UQF0; -.
OMA; FYYKLSQ; -.
OrthoDB; EOG091G09G4; -.
PhylomeDB; Q9UQF0; -.
TreeFam; TF332233; -.
ChiTaRS; ERVW-1; human.
GeneWiki; ERVWE1; -.
GenomeRNAi; 30816; -.
PRO; PR:Q9UQF0; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000242950; -.
ExpressionAtlas; Q9UQF0; baseline and differential.
Genevisible; Q9UQF0; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0045026; P:plasma membrane fusion; IDA:UniProtKB.
GO; GO:0006949; P:syncytium formation; IDA:UniProtKB.
GO; GO:0000768; P:syncytium formation by plasma membrane fusion; IDA:UniProtKB.
InterPro; IPR018154; TLV/ENV_coat_polyprotein.
PANTHER; PTHR10424; PTHR10424; 1.
Pfam; PF00429; TLV_coat; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; ERV; Glycoprotein; Membrane;
Polymorphism; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Transposable element; Viral envelope protein;
Virion.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 538 Syncytin-1.
/FTId=PRO_0000008485.
CHAIN 21 317 Surface protein.
/FTId=PRO_0000008486.
CHAIN 318 538 Transmembrane protein.
/FTId=PRO_0000008487.
TOPO_DOM 21 443 Extracellular. {ECO:0000255}.
TRANSMEM 444 464 Helical. {ECO:0000255}.
TOPO_DOM 465 538 Cytoplasmic. {ECO:0000255}.
REGION 320 340 Fusion peptide. {ECO:0000255}.
REGION 380 396 Immunosuppression. {ECO:0000250}.
REGION 465 484 Essential for the fusiogenic function.
MOTIF 186 189 CXXC. {ECO:0000305}.
MOTIF 397 406 CX6CC. {ECO:0000305}.
SITE 317 318 Cleavage. {ECO:0000269|PubMed:15827173}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 186 405 Interchain (between SU and TM chains, or
C-189 with C-405); in linked form.
{ECO:0000305|PubMed:15827173}.
DISULFID 186 189 {ECO:0000250|UniProtKB:P23064}.
DISULFID 397 404 {ECO:0000250|UniProtKB:P60508}.
VARIANT 129 129 V -> A (in dbSNP:rs142852059).
{ECO:0000269|PubMed:14757826}.
/FTId=VAR_018638.
VARIANT 138 138 R -> Q (in dbSNP:rs55903518).
{ECO:0000269|PubMed:14757826}.
/FTId=VAR_018639.
VARIANT 307 307 S -> N (in dbSNP:rs10266695).
{ECO:0000269|PubMed:10693809,
ECO:0000269|PubMed:11990458,
ECO:0000269|PubMed:14757826}.
/FTId=VAR_018640.
VARIANT 477 477 S -> F (in dbSNP:rs141340741).
{ECO:0000269|PubMed:14757826}.
/FTId=VAR_018641.
MUTAGEN 314 316 RNK->AAA: Complete loss of cleavage
between SU and TM. Loss of fusiogenic
function. {ECO:0000269|PubMed:15827173}.
MUTAGEN 317 317 R->T: Complete loss of cleavage between
SU and TM. Loss of fusiogenic function.
{ECO:0000269|PubMed:15827173}.
MUTAGEN 405 405 C->A: Loss of fusiogenic function. No
effect on cleavage between SU and TM.
{ECO:0000269|PubMed:15827173}.
CONFLICT 13 14 LL -> VS (in Ref. 1; AAD14545).
{ECO:0000305}.
CONFLICT 56 56 S -> C (in Ref. 1; AAD14545).
{ECO:0000305}.
CONFLICT 298 298 T -> A (in Ref. 1; AAD14545/AAD14548).
{ECO:0000305}.
CONFLICT 381 381 Q -> R (in Ref. 3; AAF74215).
{ECO:0000305}.
CONFLICT 388 388 L -> S (in Ref. 1; AAD14548).
{ECO:0000305}.
HELIX 343 389 {ECO:0000244|PDB:5HA6}.
HELIX 391 393 {ECO:0000244|PDB:5HA6}.
HELIX 396 400 {ECO:0000244|PDB:5HA6}.
HELIX 411 433 {ECO:0000244|PDB:5HA6}.
SEQUENCE 538 AA; 59866 MW; C54648A3C7043870 CRC64;
MALPYHIFLF TVLLPSFTLT APPPCRCMTS SSPYQEFLWR MQRPGNIDAP SYRSLSKGTP
TFTAHTHMPR NCYHSATLCM HANTHYWTGK MINPSCPGGL GVTVCWTYFT QTGMSDGGGV
QDQAREKHVK EVISQLTRVH GTSSPYKGLD LSKLHETLRT HTRLVSLFNT TLTGLHEVSA
QNPTNCWICL PLNFRPYVSI PVPEQWNNFS TEINTTSVLV GPLVSNLEIT HTSNLTCVKF
SNTTYTTNSQ CIRWVTPPTQ IVCLPSGIFF VCGTSAYRCL NGSSESMCFL SFLVPPMTIY
TEQDLYSYVI SKPRNKRVPI LPFVIGAGVL GALGTGIGGI TTSTQFYYKL SQELNGDMER
VADSLVTLQD QLNSLAAVVL QNRRALDLLT AERGGTCLFL GEECCYYVNQ SGIVTEKVKE
IRDRIQRRAE ELRNTGPWGL LSQWMPWILP FLGPLAAIIL LLLFGPCIFN LLVNFVSSRI
EAVKLQMEPK MQSKTKIYRR PLDRPASPRS DVNDIKGTPP EEISAAQPLL RPNSAGSS


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