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Q9UQF0

- SYCY1_HUMAN

UniProt

Q9UQF0 - SYCY1_HUMAN

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Protein

Syncytin-1

Gene
ERVW-1, ERVWE1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 (1 Publication, 1 Publication, 1 Publication).
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: ProtInc
Complete GO annotation...

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; 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 443423Extracellular Reviewed predictionAdd
BLAST
Transmembranei444 – 46421Helical; Reviewed predictionAdd
BLAST
Topological domaini465 – 53874Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

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. 1 Publication
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 – 2020 Reviewed predictionAdd
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...) Reviewed prediction
Disulfide bondi186 ↔ 405Interchain (between SU and TM chains, or C-189 with C-405); in linked form By similarity
Disulfide bondi186 ↔ 189 By similarity
Glycosylationi208 – 2081N-linked (GlcNAc...) Reviewed prediction
Glycosylationi214 – 2141N-linked (GlcNAc...) Reviewed prediction
Glycosylationi234 – 2341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi242 – 2421N-linked (GlcNAc...) Reviewed prediction
Glycosylationi281 – 2811N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi397 ↔ 404 By similarity
Glycosylationi409 – 4091N-linked (GlcNAc...) Reviewed prediction

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.
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.

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni320 – 34021Fusion peptide Reviewed predictionAdd
BLAST
Regioni380 – 39617Immunosuppression By similarityAdd
BLAST
Regioni465 – 48420Essential for the fusiogenic functionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi186 – 1894CXXC By similarity
Motifi397 – 4059CX6CC By 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.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 142LL → VS in AAD14545. 1 Publication
Sequence conflicti56 – 561S → C in AAD14545. 1 Publication
Sequence conflicti298 – 2981T → A in AAD14545. 1 Publication
Sequence conflicti298 – 2981T → A in AAD14548. 1 Publication
Sequence conflicti381 – 3811Q → R in AAF74215. 1 Publication
Sequence conflicti388 – 3881L → S in AAD14548. 1 Publication

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
Human Endogenous Retrovirus Database (HERVd)
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 112 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

Dasty 3

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