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Q9UQF0

- SYCY1_HUMAN

UniProt

Q9UQF0 - SYCY1_HUMAN

Protein

Syncytin-1

Gene

ERVW-1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    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).3 Publications
    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei317 – 3182Cleavage

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. syncytium formation Source: UniProtKB

    Protein family/group databases

    TCDBi1.G.9.1.1. the syncytin (syncytin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Syncytin-1
    Alternative name(s):
    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 the following 2 chains:
    Surface protein
    Short name:
    SU
    Alternative name(s):
    gp50
    Transmembrane protein
    Short name:
    TM
    Alternative name(s):
    gp24
    Gene namesi
    Name:ERVW-1
    Synonyms:ERVWE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:13525. ERVW-1.

    Subcellular locationi

    Chain Surface protein : Cell membrane By similarity; Peripheral membrane protein By similarity
    Note: The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM.By similarity
    Chain Syncytin-1 : Virion By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell
    3. viral envelope Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane, Viral envelope protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi314 – 3163RNK → AAA: Complete loss of cleavage between SU and TM. Loss of fusiogenic function.
    Mutagenesisi317 – 3171R → T: Complete loss of cleavage between SU and TM. Loss of fusiogenic function. 1 Publication
    Mutagenesisi405 – 4051C → A: Loss of fusiogenic function. No effect on cleavage between SU and TM. 1 Publication

    Organism-specific databases

    PharmGKBiPA27878.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 538518Syncytin-1PRO_0000008485Add
    BLAST
    Chaini21 – 317297Surface proteinPRO_0000008486Add
    BLAST
    Chaini318 – 538221Transmembrane proteinPRO_0000008487Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi186 ↔ 405Interchain (between SU and TM chains, or C-189 with C-405); in linked formBy similarity
    Disulfide bondi186 ↔ 189By similarity
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi397 ↔ 404By similarity
    Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    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.1 Publication
    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 By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9UQF0.
    PRIDEiQ9UQF0.

    PTM databases

    PhosphoSiteiQ9UQF0.

    Expressioni

    Tissue specificityi

    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.4 Publications

    Developmental stagei

    In placenta, detected at higher level during early pregnancy and at lower level during late pregnancy.1 Publication

    Gene expression databases

    ArrayExpressiQ9UQF0.
    BgeeiQ9UQF0.
    GenevestigatoriQ9UQF0.

    Interactioni

    Subunit structurei

    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.1 Publication

    Protein-protein interaction databases

    BioGridi119040. 2 interactions.
    STRINGi9606.ENSP00000419945.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UQF0.
    SMRiQ9UQF0. Positions 357-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 443423ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini465 – 53874CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei444 – 46421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni320 – 34021Fusion peptideSequence AnalysisAdd
    BLAST
    Regioni380 – 39617ImmunosuppressionBy similarityAdd
    BLAST
    Regioni465 – 48420Essential for the fusiogenic functionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi186 – 1894CXXCBy similarity
    Motifi397 – 4059CX6CCBy similarity

    Domaini

    The cytoplasmic region is essential for the fusiogenic function.
    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.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG131568.
    HOVERGENiHBG051487.
    InParanoidiQ9UQF0.
    OMAiHANTHYW.
    OrthoDBiEOG70ZZQM.
    PhylomeDBiQ9UQF0.
    TreeFamiTF332233.

    Family and domain databases

    InterProiIPR018154. TLV/ENV_coat_polyprotein.
    [Graphical view]
    PANTHERiPTHR10424. PTHR10424. 1 hit.
    PfamiPF00429. TLV_coat. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UQF0-1 [UniParc]FASTAAdd to Basket

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    MALPYHIFLF TVLLPSFTLT APPPCRCMTS SSPYQEFLWR MQRPGNIDAP    50
    SYRSLSKGTP TFTAHTHMPR NCYHSATLCM HANTHYWTGK MINPSCPGGL 100
    GVTVCWTYFT QTGMSDGGGV QDQAREKHVK EVISQLTRVH GTSSPYKGLD 150
    LSKLHETLRT HTRLVSLFNT TLTGLHEVSA QNPTNCWICL PLNFRPYVSI 200
    PVPEQWNNFS TEINTTSVLV GPLVSNLEIT HTSNLTCVKF SNTTYTTNSQ 250
    CIRWVTPPTQ IVCLPSGIFF VCGTSAYRCL NGSSESMCFL SFLVPPMTIY 300
    TEQDLYSYVI SKPRNKRVPI LPFVIGAGVL GALGTGIGGI TTSTQFYYKL 350
    SQELNGDMER VADSLVTLQD QLNSLAAVVL QNRRALDLLT AERGGTCLFL 400
    GEECCYYVNQ SGIVTEKVKE IRDRIQRRAE ELRNTGPWGL LSQWMPWILP 450
    FLGPLAAIIL LLLFGPCIFN LLVNFVSSRI EAVKLQMEPK MQSKTKIYRR 500
    PLDRPASPRS DVNDIKGTPP EEISAAQPLL RPNSAGSS 538
    Length:538
    Mass (Da):59,866
    Last modified:May 1, 2000 - v1
    Checksum:iC54648A3C7043870
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 142LL → VS in AAD14545. (PubMed:9882319)Curated
    Sequence conflicti56 – 561S → C in AAD14545. (PubMed:9882319)Curated
    Sequence conflicti298 – 2981T → A in AAD14545. (PubMed:9882319)Curated
    Sequence conflicti298 – 2981T → A in AAD14548. (PubMed:9882319)Curated
    Sequence conflicti381 – 3811Q → R in AAF74215. (PubMed:10826480)Curated
    Sequence conflicti388 – 3881L → S in AAD14548. (PubMed:9882319)Curated

    Polymorphismi

    All variants have fusogenic properties.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291V → A.1 Publication
    Corresponds to variant rs142852059 [ dbSNP | Ensembl ].
    VAR_018638
    Natural varianti138 – 1381R → Q.1 Publication
    Corresponds to variant rs55903518 [ dbSNP | Ensembl ].
    VAR_018639
    Natural varianti307 – 3071S → N.3 Publications
    Corresponds to variant rs10266695 [ dbSNP | Ensembl ].
    VAR_018640
    Natural varianti477 – 4771S → F.1 Publication
    Corresponds to variant rs141340741 [ dbSNP | Ensembl ].
    VAR_018641

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072503 mRNA. No translation available.
    AF072505 mRNA. Translation: AAD14545.1.
    AF072506 mRNA. Translation: AAD14546.2.
    AF072508 mRNA. Translation: AAD14548.1.
    AF208161 mRNA. Translation: AAF28334.1.
    AF513360 mRNA. Translation: AAM47599.1.
    AF156963 Genomic DNA. Translation: AAF74215.1.
    AC007566 Genomic DNA. No translation available.
    AY101582 Genomic DNA. Translation: AAM68161.1.
    AY101583 Genomic DNA. Translation: AAM68162.1.
    AY101584 Genomic DNA. Translation: AAM68163.1.
    AY101585 Genomic DNA. Translation: AAM68164.1.
    AF520478 Genomic DNA. Translation: AAQ17561.1.
    AF520480 Genomic DNA. Translation: AAQ17562.1.
    AF520482 Genomic DNA. Translation: AAQ17563.1.
    AF520484 Genomic DNA. Translation: AAQ17564.1.
    AF520486 Genomic DNA. Translation: AAQ17565.1.
    AF520488 Genomic DNA. Translation: AAQ17566.1.
    AF520490 Genomic DNA. Translation: AAQ17567.1.
    AF520492 Genomic DNA. Translation: AAQ17568.1.
    AF520494 Genomic DNA. Translation: AAQ17569.1.
    AF520496 Genomic DNA. Translation: AAQ17570.1.
    AF520498 Genomic DNA. Translation: AAQ17571.1.
    AF520500 Genomic DNA. Translation: AAQ17572.1.
    AF520502 Genomic DNA. Translation: AAQ17573.1.
    AF520504 Genomic DNA. Translation: AAQ17574.1.
    AF520506 Genomic DNA. Translation: AAQ17575.1.
    AF520508 Genomic DNA. Translation: AAQ17576.1.
    AF520510 Genomic DNA. Translation: AAQ17577.1.
    AF520512 Genomic DNA. Translation: AAQ17578.1.
    AF520514 Genomic DNA. Translation: AAQ17579.1.
    AF520516 Genomic DNA. Translation: AAQ17580.1.
    AF520518 Genomic DNA. Translation: AAQ17581.1.
    AF520520 Genomic DNA. Translation: AAQ17582.1.
    AF520522 Genomic DNA. Translation: AAQ17583.1.
    AF520524 Genomic DNA. Translation: AAQ17584.1.
    AF520526 Genomic DNA. Translation: AAQ17585.1.
    AF520528 Genomic DNA. Translation: AAQ17586.1.
    AF520530 Genomic DNA. Translation: AAQ17587.1.
    AF520532 Genomic DNA. Translation: AAQ17588.1.
    AF520534 Genomic DNA. Translation: AAQ17589.1.
    AF520536 Genomic DNA. Translation: AAQ17590.1.
    AF520538 Genomic DNA. Translation: AAQ17591.1.
    AF520540 Genomic DNA. Translation: AAQ17592.1.
    AF520542 Genomic DNA. Translation: AAQ17593.1.
    AF520544 Genomic DNA. Translation: AAQ17594.1.
    AF520546 Genomic DNA. Translation: AAQ17595.1.
    AF520548 Genomic DNA. Translation: AAQ17596.1.
    AF520550 Genomic DNA. Translation: AAQ17597.1.
    AF520552 Genomic DNA. Translation: AAQ17598.1.
    AF520554 Genomic DNA. Translation: AAQ17599.1.
    AF520556 Genomic DNA. Translation: AAQ17600.1.
    AF520558 Genomic DNA. Translation: AAQ17601.1.
    AF520560 Genomic DNA. Translation: AAQ17602.1.
    AF520562 Genomic DNA. Translation: AAQ17603.1.
    AF520564 Genomic DNA. Translation: AAQ17604.1.
    BC137381 mRNA. Translation: AAI37382.1.
    AF506835 mRNA. Translation: AAM33413.1.
    CCDSiCCDS5626.1.
    RefSeqiNP_001124397.1. NM_001130925.1.
    NP_055405.3. NM_014590.3.

    Genome annotation databases

    EnsembliENST00000493463; ENSP00000419945; ENSG00000242950.
    ENST00000603053; ENSP00000474984; ENSG00000242950.
    GeneIDi30816.
    KEGGihsa:30816.
    UCSCiuc022ahe.1. human.

    Polymorphism databases

    DMDMi47605755.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Protein Spotlight

    A virus for life - Issue 50 of September 2004

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072503 mRNA. No translation available.
    AF072505 mRNA. Translation: AAD14545.1 .
    AF072506 mRNA. Translation: AAD14546.2 .
    AF072508 mRNA. Translation: AAD14548.1 .
    AF208161 mRNA. Translation: AAF28334.1 .
    AF513360 mRNA. Translation: AAM47599.1 .
    AF156963 Genomic DNA. Translation: AAF74215.1 .
    AC007566 Genomic DNA. No translation available.
    AY101582 Genomic DNA. Translation: AAM68161.1 .
    AY101583 Genomic DNA. Translation: AAM68162.1 .
    AY101584 Genomic DNA. Translation: AAM68163.1 .
    AY101585 Genomic DNA. Translation: AAM68164.1 .
    AF520478 Genomic DNA. Translation: AAQ17561.1 .
    AF520480 Genomic DNA. Translation: AAQ17562.1 .
    AF520482 Genomic DNA. Translation: AAQ17563.1 .
    AF520484 Genomic DNA. Translation: AAQ17564.1 .
    AF520486 Genomic DNA. Translation: AAQ17565.1 .
    AF520488 Genomic DNA. Translation: AAQ17566.1 .
    AF520490 Genomic DNA. Translation: AAQ17567.1 .
    AF520492 Genomic DNA. Translation: AAQ17568.1 .
    AF520494 Genomic DNA. Translation: AAQ17569.1 .
    AF520496 Genomic DNA. Translation: AAQ17570.1 .
    AF520498 Genomic DNA. Translation: AAQ17571.1 .
    AF520500 Genomic DNA. Translation: AAQ17572.1 .
    AF520502 Genomic DNA. Translation: AAQ17573.1 .
    AF520504 Genomic DNA. Translation: AAQ17574.1 .
    AF520506 Genomic DNA. Translation: AAQ17575.1 .
    AF520508 Genomic DNA. Translation: AAQ17576.1 .
    AF520510 Genomic DNA. Translation: AAQ17577.1 .
    AF520512 Genomic DNA. Translation: AAQ17578.1 .
    AF520514 Genomic DNA. Translation: AAQ17579.1 .
    AF520516 Genomic DNA. Translation: AAQ17580.1 .
    AF520518 Genomic DNA. Translation: AAQ17581.1 .
    AF520520 Genomic DNA. Translation: AAQ17582.1 .
    AF520522 Genomic DNA. Translation: AAQ17583.1 .
    AF520524 Genomic DNA. Translation: AAQ17584.1 .
    AF520526 Genomic DNA. Translation: AAQ17585.1 .
    AF520528 Genomic DNA. Translation: AAQ17586.1 .
    AF520530 Genomic DNA. Translation: AAQ17587.1 .
    AF520532 Genomic DNA. Translation: AAQ17588.1 .
    AF520534 Genomic DNA. Translation: AAQ17589.1 .
    AF520536 Genomic DNA. Translation: AAQ17590.1 .
    AF520538 Genomic DNA. Translation: AAQ17591.1 .
    AF520540 Genomic DNA. Translation: AAQ17592.1 .
    AF520542 Genomic DNA. Translation: AAQ17593.1 .
    AF520544 Genomic DNA. Translation: AAQ17594.1 .
    AF520546 Genomic DNA. Translation: AAQ17595.1 .
    AF520548 Genomic DNA. Translation: AAQ17596.1 .
    AF520550 Genomic DNA. Translation: AAQ17597.1 .
    AF520552 Genomic DNA. Translation: AAQ17598.1 .
    AF520554 Genomic DNA. Translation: AAQ17599.1 .
    AF520556 Genomic DNA. Translation: AAQ17600.1 .
    AF520558 Genomic DNA. Translation: AAQ17601.1 .
    AF520560 Genomic DNA. Translation: AAQ17602.1 .
    AF520562 Genomic DNA. Translation: AAQ17603.1 .
    AF520564 Genomic DNA. Translation: AAQ17604.1 .
    BC137381 mRNA. Translation: AAI37382.1 .
    AF506835 mRNA. Translation: AAM33413.1 .
    CCDSi CCDS5626.1.
    RefSeqi NP_001124397.1. NM_001130925.1.
    NP_055405.3. NM_014590.3.

    3D structure databases

    ProteinModelPortali Q9UQF0.
    SMRi Q9UQF0. Positions 357-409.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119040. 2 interactions.
    STRINGi 9606.ENSP00000419945.

    Protein family/group databases

    TCDBi 1.G.9.1.1. the syncytin (syncytin) family.

    PTM databases

    PhosphoSitei Q9UQF0.

    Polymorphism databases

    DMDMi 47605755.

    Proteomic databases

    PaxDbi Q9UQF0.
    PRIDEi Q9UQF0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000493463 ; ENSP00000419945 ; ENSG00000242950 .
    ENST00000603053 ; ENSP00000474984 ; ENSG00000242950 .
    GeneIDi 30816.
    KEGGi hsa:30816.
    UCSCi uc022ahe.1. human.

    Organism-specific databases

    CTDi 30816.
    GeneCardsi GC07M092098.
    HGNCi HGNC:13525. ERVW-1.
    MIMi 604659. gene.
    neXtProti NX_Q9UQF0.
    PharmGKBi PA27878.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG131568.
    HOVERGENi HBG051487.
    InParanoidi Q9UQF0.
    OMAi HANTHYW.
    OrthoDBi EOG70ZZQM.
    PhylomeDBi Q9UQF0.
    TreeFami TF332233.

    Miscellaneous databases

    ChiTaRSi ERVW-1. human.
    GeneWikii ERVWE1.
    GenomeRNAii 30816.
    NextBioi 52878.
    PROi Q9UQF0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UQF0.
    Bgeei Q9UQF0.
    Genevestigatori Q9UQF0.

    Family and domain databases

    InterProi IPR018154. TLV/ENV_coat_polyprotein.
    [Graphical view ]
    PANTHERi PTHR10424. PTHR10424. 1 hit.
    Pfami PF00429. TLV_coat. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization and placental expression of HERV-W, a new human endogenous retrovirus family."
      Blond J.-L., Beseme F., Duret L., Bouton O., Bedin F., Perron H., Mandrand B., Mallet F.
      J. Virol. 73:1175-1185(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "Syncytin is captive retroviral envelope protein involved in human placental morphogenesis."
      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.
      Nature 403:785-789(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, VARIANT ASN-307.
      Tissue: Testis.
    3. "Chromosomal distribution and coding capacity of the human endogenous retrovirus HERV-W family."
      Voisset C., Bouton O., Bedin F., Duret L., Mandrand B., Mallet F., Paranhos-Baccala G.
      AIDS Res. Hum. Retroviruses 16:731-740(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The endogenous retroviral locus ERVWE1 is a bona fide gene involved in hominoid placental physiology."
      Mallet F., Bouton O., Prudhomme S., Cheynet V., Oriol G., Bonnaud B., Lucotte G., Duret L., Mandrand B.
      Proc. Natl. Acad. Sci. U.S.A. 101:1731-1736(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-129; GLN-138; ASN-307 AND PHE-477.
    5. "The DNA sequence of human chromosome 7."
      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.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The HERV-W/7q family in the human genome. Potential for protein expression and gene regulation."
      Alliel P.M., Perin J.-P., Goudou D., Bitoun M., Robert B., Rieger F.
      Cell. Mol. Biol. 48:213-217(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-533, VARIANT ASN-307.
      Tissue: Placenta.
    8. Cited for: IDENTIFICATION.
    9. "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."
      Blond J.-L., Lavillette D., Cheynet V., Bouton O., Oriol G., Chapel-Fernandes S., Mandrand B., Mallet F., Cosset F.-L.
      J. Virol. 74:3321-3329(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "Envelope gene of the human endogenous retrovirus HERV-W encodes a functional retrovirus envelope."
      An D.S., Xie Y.-M., Chen I.S.Y.
      J. Virol. 75:3488-3489(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Multiple sclerosis retrovirus particles and recombinant envelope trigger an abnormal immune response in vitro, by inducing polyclonal Vbeta16 T-lymphocyte activation."
      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.
      Virology 287:321-332(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The envelope glycoprotein of human endogenous retrovirus type W uses a divergent family of amino acid transporters/cell surface receptors."
      Lavillette D., Marin M., Ruggieri A., Mallet F., Cosset F.-L., Kabat D.
      J. Virol. 76:6442-6452(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Genomewide screening for fusogenic human endogenous retrovirus envelopes identifies syncytin 2, a gene conserved on primate evolution."
      Blaise S., de Parseval N., Benit L., Heidmann T.
      Proc. Natl. Acad. Sci. U.S.A. 100:13013-13018(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "The envelope glycoprotein of human endogenous retrovirus HERV-W induces cellular resistance to spleen necrosis virus."
      Ponferrada V.G., Mauck B.S., Wooley D.P.
      Arch. Virol. 148:659-675(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Survey of human genes of retroviral origin: identification and transcriptome of the genes with coding capacity for complete envelope proteins."
      de Parseval N., Lazar V., Casella J.-F., Benit L., Heidmann T.
      J. Virol. 77:10414-10422(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    16. "Temporal regulation of the expression of syncytin (HERV-W), maternally imprinted PEG10, and SGCE in human placenta."
      Smallwood A., Papageorghiou A., Nicolaides K., Alley M.K.R., Jim A., Nargund G., Ojha K., Campbell S., Banerjee S.
      Biol. Reprod. 69:286-293(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    17. "Evidence of selection on the domesticated ERVWE1 env retroviral element involved in placentation."
      Bonnaud B., Bouton O., Oriol G., Cheynet V., Duret L., Mallet F.
      Mol. Biol. Evol. 21:1895-1901(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Human endogenous retrovirus glycoprotein-mediated induction of redox reactants causes oligodendrocyte death and demyelination."
      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.
      Nat. Neurosci. 7:1088-1095(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MULTIPLE SCLEROSIS, TISSUE SPECIFICITY.
    19. "Synthesis, assembly, and processing of the Env ERVWE1/syncytin human endogenous retroviral envelope."
      Cheynet V., Ruggieri A., Oriol G., Blond J.-L., Boson B., Vachot L., Verrier B., Cosset F.-L., Mallet F.
      J. Virol. 79:5585-5593(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, SUBUNIT, INTERACTION WITH CD209/DC-SIGN, MUTAGENESIS OF 314-ARG--LYS-316; ARG-317 AND CYS-405.
    20. "A novel human endogenous retroviral protein inhibits cell-cell fusion."
      Sugimoto J., Sugimoto M., Bernstein H., Jinno Y., Schust D.
      Sci. Rep. 3:1462-1462(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiSYCY1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQF0
    Secondary accession number(s): B2RPD4
    , O95244, O95245, Q8NHY7, Q9NRZ2, Q9NZG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.
    Orthologs in Pan troglodytes, Gorilla gorilla, Pongo pygmaeus and Hylobates moloch.
    It can make pseudotypes with HIV-1 virions and confer infectivity. Can also induce cellular resistance to spleen necrosis virus in vitro.
    HERV-W family subgenomic RNAs have been observed.
    This provirus is intergenic, the closest flanking genes being ODAG and PEX1.
    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.

    Keywords - Technical termi

    Complete proteome, ERV, Reference proteome, Transposable element

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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