SYCY1_HUMAN
ID SYCY1_HUMAN Reviewed; 538 AA.
AC Q9UQF0; B2RPD4; O95244; O95245; Q8NHY7; Q9NRZ2; Q9NZG3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Syncytin-1;
DE AltName: Full=Endogenous retrovirus group W member 1;
DE AltName: Full=Env-W;
DE AltName: Full=Envelope polyprotein gPr73;
DE AltName: Full=Enverin;
DE AltName: Full=HERV-7q Envelope protein;
DE AltName: Full=HERV-W envelope protein;
DE AltName: Full=HERV-W_7q21.2 provirus ancestral Env polyprotein;
DE AltName: Full=Syncytin;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=gp50;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=gp24;
DE Flags: Precursor;
GN Name=ERVW-1; Synonyms=ERVWE1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=9882319; DOI=10.1128/jvi.73.2.1175-1185.1999;
RA Blond J.-L., Beseme F., Duret L., Bouton O., Bedin F., Perron H.,
RA Mandrand B., Mallet F.;
RT "Molecular characterization and placental expression of HERV-W, a new human
RT endogenous retrovirus family.";
RL J. Virol. 73:1175-1185(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND VARIANT
RP ASN-307.
RC TISSUE=Testis;
RX PubMed=10693809; DOI=10.1038/35001608;
RA Sha M., Lee X., Li X.-P., Veldman G.M., Finnerty H., Racie L., LaVallie E.,
RA Tang X.-Y., Edouard P., Howes S., Keith J.C. Jr., McCoy J.M.;
RT "Syncytin is captive retroviral envelope protein involved in human
RT placental morphogenesis.";
RL Nature 403:785-789(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10826480; DOI=10.1089/088922200308738;
RA Voisset C., Bouton O., Bedin F., Duret L., Mandrand B., Mallet F.,
RA Paranhos-Baccala G.;
RT "Chromosomal distribution and coding capacity of the human endogenous
RT retrovirus HERV-W family.";
RL AIDS Res. Hum. Retroviruses 16:731-740(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-129; GLN-138; ASN-307
RP AND PHE-477.
RX PubMed=14757826; DOI=10.1073/pnas.0305763101;
RA Mallet F., Bouton O., Prudhomme S., Cheynet V., Oriol G., Bonnaud B.,
RA Lucotte G., Duret L., Mandrand B.;
RT "The endogenous retroviral locus ERVWE1 is a bona fide gene involved in
RT hominoid placental physiology.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1731-1736(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-533, AND VARIANT ASN-307.
RC TISSUE=Placenta;
RX PubMed=11990458;
RA Alliel P.M., Perin J.-P., Goudou D., Bitoun M., Robert B., Rieger F.;
RT "The HERV-W/7q family in the human genome. Potential for protein expression
RT and gene regulation.";
RL Cell. Mol. Biol. 48:213-217(2002).
RN [8]
RP IDENTIFICATION.
RX PubMed=9835022; DOI=10.1016/s0764-4469(99)80026-2;
RA Alliel P.M., Perin J.-P., Pierig R., Nussbaum J.-L., Menard A., Rieger F.;
RT "Endogenous retroviruses and multiple sclerosis. II. HERV-7q.";
RL C. R. Acad. Sci. III, Sci. Vie 321:857-863(1998).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10708449; DOI=10.1128/jvi.74.7.3321-3329.2000;
RA Blond J.-L., Lavillette D., Cheynet V., Bouton O., Oriol G.,
RA Chapel-Fernandes S., Mandrand B., Mallet F., Cosset F.-L.;
RT "An envelope glycoprotein of the human endogenous retrovirus HERV-W is
RT expressed in the human placenta and fuses cells expressing the type D
RT mammalian retrovirus receptor.";
RL J. Virol. 74:3321-3329(2000).
RN [10]
RP FUNCTION.
RX PubMed=11238877; DOI=10.1128/jvi.75.7.3488-3489.2001;
RA An D.S., Xie Y.-M., Chen I.S.Y.;
RT "Envelope gene of the human endogenous retrovirus HERV-W encodes a
RT functional retrovirus envelope.";
RL J. Virol. 75:3488-3489(2001).
RN [11]
RP FUNCTION.
RX PubMed=11531410; DOI=10.1006/viro.2001.1045;
RA Perron H., Jouvin-Marche E., Michel M., Ounanian-Paraz A., Camelo S.,
RA Dumon A., Jolivet-Reynaud C., Marcel F., Souillet Y., Borel E.,
RA Gebuhrer L., Santoro L., Marcel S., Seigneurin J.M., Marche P.N., Lafon M.;
RT "Multiple sclerosis retrovirus particles and recombinant envelope trigger
RT an abnormal immune response in vitro, by inducing polyclonal Vbeta16 T-
RT lymphocyte activation.";
RL Virology 287:321-332(2001).
RN [12]
RP FUNCTION.
RX PubMed=12050356; DOI=10.1128/jvi.76.13.6442-6452.2002;
RA Lavillette D., Marin M., Ruggieri A., Mallet F., Cosset F.-L., Kabat D.;
RT "The envelope glycoprotein of human endogenous retrovirus type W uses a
RT divergent family of amino acid transporters/cell surface receptors.";
RL J. Virol. 76:6442-6452(2002).
RN [13]
RP FUNCTION.
RX PubMed=14557543; DOI=10.1073/pnas.2132646100;
RA Blaise S., de Parseval N., Benit L., Heidmann T.;
RT "Genomewide screening for fusogenic human endogenous retrovirus envelopes
RT identifies syncytin 2, a gene conserved on primate evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003).
RN [14]
RP FUNCTION.
RX PubMed=12664292; DOI=10.1007/s00705-002-0960-x;
RA Ponferrada V.G., Mauck B.S., Wooley D.P.;
RT "The envelope glycoprotein of human endogenous retrovirus HERV-W induces
RT cellular resistance to spleen necrosis virus.";
RL Arch. Virol. 148:659-675(2003).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=12970426; DOI=10.1128/jvi.77.19.10414-10422.2003;
RA de Parseval N., Lazar V., Casella J.-F., Benit L., Heidmann T.;
RT "Survey of human genes of retroviral origin: identification and
RT transcriptome of the genes with coding capacity for complete envelope
RT proteins.";
RL J. Virol. 77:10414-10422(2003).
RN [16]
RP DEVELOPMENTAL STAGE.
RX PubMed=12620933; DOI=10.1095/biolreprod.102.013078;
RA Smallwood A., Papageorghiou A., Nicolaides K., Alley M.K.R., Jim A.,
RA Nargund G., Ojha K., Campbell S., Banerjee S.;
RT "Temporal regulation of the expression of syncytin (HERV-W), maternally
RT imprinted PEG10, and SGCE in human placenta.";
RL Biol. Reprod. 69:286-293(2003).
RN [17]
RP FUNCTION.
RX PubMed=15254254; DOI=10.1093/molbev/msh206;
RA Bonnaud B., Bouton O., Oriol G., Cheynet V., Duret L., Mallet F.;
RT "Evidence of selection on the domesticated ERVWE1 env retroviral element
RT involved in placentation.";
RL Mol. Biol. Evol. 21:1895-1901(2004).
RN [18]
RP INVOLVEMENT IN MULTIPLE SCLEROSIS, AND TISSUE SPECIFICITY.
RX PubMed=15452578; DOI=10.1038/nn1319;
RA Antony J.M., Van Marle G., Opii W., Butterfield D.A., Mallet F., Yong V.W.,
RA Wallace J.L., Deacon R.M., Warren K., Power C.;
RT "Human endogenous retrovirus glycoprotein-mediated induction of redox
RT reactants causes oligodendrocyte death and demyelination.";
RL Nat. Neurosci. 7:1088-1095(2004).
RN [19]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, SUBUNIT, INTERACTION WITH
RP CD209/DC-SIGN, AND MUTAGENESIS OF 314-ARG--LYS-316; ARG-317 AND CYS-405.
RX PubMed=15827173; DOI=10.1128/jvi.79.9.5585-5593.2005;
RA Cheynet V., Ruggieri A., Oriol G., Blond J.-L., Boson B., Vachot L.,
RA Verrier B., Cosset F.-L., Mallet F.;
RT "Synthesis, assembly, and processing of the Env ERVWE1/syncytin human
RT endogenous retroviral envelope.";
RL J. Virol. 79:5585-5593(2005).
RN [20]
RP FUNCTION.
RX PubMed=23492904; DOI=10.1038/srep01462;
RA Sugimoto J., Sugimoto M., Bernstein H., Jinno Y., Schust D.;
RT "A novel human endogenous retroviral protein inhibits cell-cell fusion.";
RL Sci. Rep. 3:1462-1462(2013).
CC -!- FUNCTION: This endogenous retroviral envelope protein has retained its
CC original fusogenic properties and participates in trophoblast fusion
CC and the formation of a syncytium during placenta morphogenesis. May
CC induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449,
CC PubMed:12050356, PubMed:23492904). {ECO:0000269|PubMed:10708449,
CC ECO:0000269|PubMed:12050356, ECO:0000269|PubMed:23492904}.
CC -!- FUNCTION: Endogenous envelope proteins may have kept, lost or modified
CC their original function during evolution. Retroviral envelope proteins
CC mediate receptor recognition and membrane fusion during early
CC infection. The surface protein (SU) mediates receptor recognition,
CC while the transmembrane protein (TM) acts as a class I viral fusion
CC protein. The protein may have at least 3 conformational states: pre-
CC fusion native state, pre-hairpin intermediate state, and post-fusion
CC hairpin state. During viral and target cell membrane fusion, the coiled
CC coil regions (heptad repeats) assume a trimer-of-hairpins structure,
CC positioning the fusion peptide in close proximity to the C-terminal
CC region of the ectodomain. The formation of this structure appears to
CC drive apposition and subsequent fusion of membranes.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached probably by a labile interchain disulfide
CC bond. Interacts with the C-type lectin CD209/DC-SIGN.
CC {ECO:0000269|PubMed:15827173}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Cell membrane
CC {ECO:0000305|PubMed:15827173}; Peripheral membrane protein
CC {ECO:0000305|PubMed:15827173}. Note=The surface protein is not anchored
CC to the membrane, but localizes to the extracellular surface through its
CC binding to TM. {ECO:0000305|PubMed:15827173}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Syncytin-1]: Virion {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at higher level in placental
CC syncytiotrophoblast. Expressed at intermediate level in testis. Seems
CC also to be found at low level in adrenal tissue, bone marrow, breast,
CC colon, kidney, ovary, prostate, skin, spleen, thymus, thyroid, brain
CC and trachea. Both mRNA and protein levels are significantly increased
CC in the brain of individuals with multiple sclerosis, particularly in
CC astrocytes and microglia. {ECO:0000269|PubMed:10693809,
CC ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:12970426,
CC ECO:0000269|PubMed:15452578}.
CC -!- DEVELOPMENTAL STAGE: In placenta, detected at higher level during early
CC pregnancy and at lower level during late pregnancy.
CC {ECO:0000269|PubMed:12620933}.
CC -!- DOMAIN: The cytoplasmic region is essential for the fusiogenic
CC function.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC heavily N-glycosylated and processed likely by furin in the Golgi to
CC yield the mature SU and TM proteins. The cleavage site between SU and
CC TM requires the minimal sequence [KR]-X-[KR]-R. The intracytoplasmic
CC tail cleavage by the viral protease that is required for the fusiogenic
CC activity of some retroviruses envelope proteins seems to have been lost
CC during evolution. {ECO:0000269|PubMed:15827173}.
CC -!- PTM: The CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane protein. Isomerization of the intersubunit
CC disulfide bond to an SU intrachain disulfide bond is thought to occur
CC upon receptor recognition in order to allow membrane fusion.
CC {ECO:0000305|PubMed:15827173}.
CC -!- POLYMORPHISM: All variants have fusogenic properties.
CC -!- MISCELLANEOUS: Probably involved in the development of multiple
CC sclerosis (MS). MS is a neurodegenerative disease characterized by the
CC gradual accumulation of focal plaques of demyelination particularly in
CC the periventricular areas of the brain. It leads to physical and
CC cognitive disabilities. Viral particles or intracellular RNA of HERV-W
CC family members have been detected in tissue from patients with multiple
CC sclerosis or schizophrenia.
CC -!- MISCELLANEOUS: Orthologs in P.troglodytes, G.gorilla, P.pygmaeus and
CC H.moloch.
CC -!- MISCELLANEOUS: It can make pseudotypes with HIV-1 virions and confer
CC infectivity. Can also induce cellular resistance to spleen necrosis
CC virus in vitro.
CC -!- MISCELLANEOUS: HERV-W family subgenomic RNAs have been observed.
CC -!- MISCELLANEOUS: This provirus is intergenic, the closest flanking genes
CC being ODAG and PEX1.
CC -!- MISCELLANEOUS: The human genome contains a high percentage of proviral-
CC like elements, also called endogenous retroviruses (ERVs) that are the
CC genomic traces of ancient infections of the germline by exogenous
CC retroviruses. Although most of these elements are defective, some have
CC conserved a functional envelope (env) gene, most probably diverted by
CC the host for its benefit.
CC -!- SIMILARITY: Belongs to the gamma type-C retroviral envelope protein
CC family. HERV class-I W env subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ERVWE1ID40497ch7q21.html";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A virus for life - Issue 50
CC of September 2004;
CC URL="https://web.expasy.org/spotlight/back_issues/050";
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DR EMBL; AF072503; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF072505; AAD14545.1; -; mRNA.
DR EMBL; AF072506; AAD14546.2; -; mRNA.
DR EMBL; AF072508; AAD14548.1; -; mRNA.
DR EMBL; AF208161; AAF28334.1; -; mRNA.
DR EMBL; AF513360; AAM47599.1; -; mRNA.
DR EMBL; AF156963; AAF74215.1; -; Genomic_DNA.
DR EMBL; AC007566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY101582; AAM68161.1; -; Genomic_DNA.
DR EMBL; AY101583; AAM68162.1; -; Genomic_DNA.
DR EMBL; AY101584; AAM68163.1; -; Genomic_DNA.
DR EMBL; AY101585; AAM68164.1; -; Genomic_DNA.
DR EMBL; AF520478; AAQ17561.1; -; Genomic_DNA.
DR EMBL; AF520480; AAQ17562.1; -; Genomic_DNA.
DR EMBL; AF520482; AAQ17563.1; -; Genomic_DNA.
DR EMBL; AF520484; AAQ17564.1; -; Genomic_DNA.
DR EMBL; AF520486; AAQ17565.1; -; Genomic_DNA.
DR EMBL; AF520488; AAQ17566.1; -; Genomic_DNA.
DR EMBL; AF520490; AAQ17567.1; -; Genomic_DNA.
DR EMBL; AF520492; AAQ17568.1; -; Genomic_DNA.
DR EMBL; AF520494; AAQ17569.1; -; Genomic_DNA.
DR EMBL; AF520496; AAQ17570.1; -; Genomic_DNA.
DR EMBL; AF520498; AAQ17571.1; -; Genomic_DNA.
DR EMBL; AF520500; AAQ17572.1; -; Genomic_DNA.
DR EMBL; AF520502; AAQ17573.1; -; Genomic_DNA.
DR EMBL; AF520504; AAQ17574.1; -; Genomic_DNA.
DR EMBL; AF520506; AAQ17575.1; -; Genomic_DNA.
DR EMBL; AF520508; AAQ17576.1; -; Genomic_DNA.
DR EMBL; AF520510; AAQ17577.1; -; Genomic_DNA.
DR EMBL; AF520512; AAQ17578.1; -; Genomic_DNA.
DR EMBL; AF520514; AAQ17579.1; -; Genomic_DNA.
DR EMBL; AF520516; AAQ17580.1; -; Genomic_DNA.
DR EMBL; AF520518; AAQ17581.1; -; Genomic_DNA.
DR EMBL; AF520520; AAQ17582.1; -; Genomic_DNA.
DR EMBL; AF520522; AAQ17583.1; -; Genomic_DNA.
DR EMBL; AF520524; AAQ17584.1; -; Genomic_DNA.
DR EMBL; AF520526; AAQ17585.1; -; Genomic_DNA.
DR EMBL; AF520528; AAQ17586.1; -; Genomic_DNA.
DR EMBL; AF520530; AAQ17587.1; -; Genomic_DNA.
DR EMBL; AF520532; AAQ17588.1; -; Genomic_DNA.
DR EMBL; AF520534; AAQ17589.1; -; Genomic_DNA.
DR EMBL; AF520536; AAQ17590.1; -; Genomic_DNA.
DR EMBL; AF520538; AAQ17591.1; -; Genomic_DNA.
DR EMBL; AF520540; AAQ17592.1; -; Genomic_DNA.
DR EMBL; AF520542; AAQ17593.1; -; Genomic_DNA.
DR EMBL; AF520544; AAQ17594.1; -; Genomic_DNA.
DR EMBL; AF520546; AAQ17595.1; -; Genomic_DNA.
DR EMBL; AF520548; AAQ17596.1; -; Genomic_DNA.
DR EMBL; AF520550; AAQ17597.1; -; Genomic_DNA.
DR EMBL; AF520552; AAQ17598.1; -; Genomic_DNA.
DR EMBL; AF520554; AAQ17599.1; -; Genomic_DNA.
DR EMBL; AF520556; AAQ17600.1; -; Genomic_DNA.
DR EMBL; AF520558; AAQ17601.1; -; Genomic_DNA.
DR EMBL; AF520560; AAQ17602.1; -; Genomic_DNA.
DR EMBL; AF520562; AAQ17603.1; -; Genomic_DNA.
DR EMBL; AF520564; AAQ17604.1; -; Genomic_DNA.
DR EMBL; BC137381; AAI37382.1; -; mRNA.
DR EMBL; AF506835; AAM33413.1; -; mRNA.
DR CCDS; CCDS5626.1; -.
DR RefSeq; NP_001124397.1; NM_001130925.1.
DR RefSeq; NP_055405.3; NM_014590.3.
DR PDB; 5HA6; X-ray; 2.00 A; A/B=343-435.
DR PDB; 6RX1; X-ray; 2.10 A; A=342-435.
DR PDBsum; 5HA6; -.
DR PDBsum; 6RX1; -.
DR AlphaFoldDB; Q9UQF0; -.
DR SMR; Q9UQF0; -.
DR BioGRID; 119040; 2.
DR IntAct; Q9UQF0; 1.
DR STRING; 9606.ENSP00000419945; -.
DR ChEMBL; CHEMBL4662944; -.
DR GuidetoPHARMACOLOGY; 3182; -.
DR TCDB; 1.G.9.1.1; the syncytin (syncytin) family.
DR GlyGen; Q9UQF0; 7 sites.
DR iPTMnet; Q9UQF0; -.
DR PhosphoSitePlus; Q9UQF0; -.
DR BioMuta; ERVW-1; -.
DR DMDM; 47605755; -.
DR MassIVE; Q9UQF0; -.
DR PaxDb; Q9UQF0; -.
DR PeptideAtlas; Q9UQF0; -.
DR PRIDE; Q9UQF0; -.
DR ProteomicsDB; 85550; -.
DR Antibodypedia; 29999; 250 antibodies from 23 providers.
DR DNASU; 30816; -.
DR Ensembl; ENST00000493463.2; ENSP00000419945.1; ENSG00000242950.7.
DR Ensembl; ENST00000603053.2; ENSP00000474984.1; ENSG00000242950.7.
DR GeneID; 30816; -.
DR KEGG; hsa:30816; -.
DR MANE-Select; ENST00000603053.2; ENSP00000474984.1; NM_001130925.2; NP_001124397.1.
DR UCSC; uc022ahe.2; human.
DR CTD; 30816; -.
DR DisGeNET; 30816; -.
DR GeneCards; ERVW-1; -.
DR HGNC; HGNC:13525; ERVW-1.
DR HPA; ENSG00000242950; Tissue enriched (placenta).
DR MIM; 604659; gene.
DR neXtProt; NX_Q9UQF0; -.
DR OpenTargets; ENSG00000242950; -.
DR PharmGKB; PA27878; -.
DR VEuPathDB; HostDB:ENSG00000242950; -.
DR eggNOG; ENOG502SD08; Eukaryota.
DR GeneTree; ENSGT00690000102286; -.
DR HOGENOM; CLU_037857_0_0_1; -.
DR InParanoid; Q9UQF0; -.
DR OMA; FVNQSGI; -.
DR OrthoDB; 925621at2759; -.
DR PhylomeDB; Q9UQF0; -.
DR TreeFam; TF332233; -.
DR PathwayCommons; Q9UQF0; -.
DR SignaLink; Q9UQF0; -.
DR BioGRID-ORCS; 30816; 344 hits in 975 CRISPR screens.
DR ChiTaRS; ERVW-1; human.
DR GeneWiki; ERVWE1; -.
DR GenomeRNAi; 30816; -.
DR Pharos; Q9UQF0; Tbio.
DR PRO; PR:Q9UQF0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UQF0; protein.
DR Bgee; ENSG00000242950; Expressed in placenta and 101 other tissues.
DR ExpressionAtlas; Q9UQF0; baseline and differential.
DR Genevisible; Q9UQF0; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0007520; P:myoblast fusion; IMP:MGI.
DR GO; GO:0006949; P:syncytium formation; IDA:UniProtKB.
DR GO; GO:0000768; P:syncytium formation by plasma membrane fusion; IDA:UniProtKB.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cleavage on pair of basic residues;
KW Disulfide bond; ERV; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transposable element;
KW Viral envelope protein; Virion.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..538
FT /note="Syncytin-1"
FT /id="PRO_0000008485"
FT CHAIN 21..317
FT /note="Surface protein"
FT /id="PRO_0000008486"
FT CHAIN 318..538
FT /note="Transmembrane protein"
FT /id="PRO_0000008487"
FT TOPO_DOM 21..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 320..340
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 380..396
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT REGION 465..484
FT /note="Essential for the fusiogenic function"
FT REGION 496..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..189
FT /note="CXXC"
FT /evidence="ECO:0000305"
FT MOTIF 397..406
FT /note="CX6CC"
FT /evidence="ECO:0000305"
FT COMPBIAS 496..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 317..318
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:15827173"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 186..405
FT /note="Interchain (between SU and TM chains, or C-189 with
FT C-405); in linked form"
FT /evidence="ECO:0000305|PubMed:15827173"
FT DISULFID 186..189
FT /evidence="ECO:0000250|UniProtKB:P23064"
FT DISULFID 397..404
FT /evidence="ECO:0000250|UniProtKB:P60508"
FT VARIANT 129
FT /note="V -> A (in dbSNP:rs142852059)"
FT /evidence="ECO:0000269|PubMed:14757826"
FT /id="VAR_018638"
FT VARIANT 138
FT /note="R -> Q (in dbSNP:rs55903518)"
FT /evidence="ECO:0000269|PubMed:14757826"
FT /id="VAR_018639"
FT VARIANT 307
FT /note="S -> N (in dbSNP:rs10266695)"
FT /evidence="ECO:0000269|PubMed:10693809,
FT ECO:0000269|PubMed:11990458, ECO:0000269|PubMed:14757826"
FT /id="VAR_018640"
FT VARIANT 477
FT /note="S -> F (in dbSNP:rs141340741)"
FT /evidence="ECO:0000269|PubMed:14757826"
FT /id="VAR_018641"
FT MUTAGEN 314..316
FT /note="RNK->AAA: Complete loss of cleavage between SU and
FT TM. Loss of fusiogenic function."
FT /evidence="ECO:0000269|PubMed:15827173"
FT MUTAGEN 317
FT /note="R->T: Complete loss of cleavage between SU and TM.
FT Loss of fusiogenic function."
FT /evidence="ECO:0000269|PubMed:15827173"
FT MUTAGEN 405
FT /note="C->A: Loss of fusiogenic function. No effect on
FT cleavage between SU and TM."
FT /evidence="ECO:0000269|PubMed:15827173"
FT CONFLICT 13..14
FT /note="LL -> VS (in Ref. 1; AAD14545)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> C (in Ref. 1; AAD14545)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="T -> A (in Ref. 1; AAD14545/AAD14548)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="Q -> R (in Ref. 3; AAF74215)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="L -> S (in Ref. 1; AAD14548)"
FT /evidence="ECO:0000305"
FT HELIX 343..389
FT /evidence="ECO:0007829|PDB:5HA6"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:5HA6"
FT HELIX 396..400
FT /evidence="ECO:0007829|PDB:5HA6"
FT HELIX 411..433
FT /evidence="ECO:0007829|PDB:5HA6"
SQ 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
