ERVW-1
Syncytin-1
Also known as: envW, ERVWE1, HERV-7q, HERV-W, HERV-W-ENV, HERVW, SYCY1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9UQF0
- Gene
- ERVW-1
- Ensembl
- ENSG00000242950
- Chromosome
- 7
- Canonical length
- 538 aa
- Protein class
- Predicted membrane proteins, Transporters
OverviewNCBI Gene
Many different human endogenous retrovirus (HERV) families are expressed in normal placental tissue at high levels, suggesting that HERVs are functionally important in reproduction. This gene is part of an HERV provirus on chromosome 7 that has inactivating mutations in the gag and pol genes. This gene is the envelope glycoprotein gene which appears to have been selectively preserved. The gene's protein product is expressed in the placental syncytiotrophoblast and is involved in fusion of the cytotrophoblast cells to form the syncytial layer of the placenta. The protein has the characteristics of a typical retroviral envelope protein, including a furin cleavage site that separates the surface (SU) and transmembrane (TM) proteins which form a heterodimer. Alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Mar 2010]
Canonical amino-acid sequenceUniProt
538 residues, UniProt reviewed canonical sequence.
>Q9UQF0|ERVW-1
1 MALPYHIFLF TVLLPSFTLT APPPCRCMTS SSPYQEFLWR MQRPGNIDAP SYRSLSKGTP
61 TFTAHTHMPR NCYHSATLCM HANTHYWTGK MINPSCPGGL GVTVCWTYFT QTGMSDGGGV
121 QDQAREKHVK EVISQLTRVH GTSSPYKGLD LSKLHETLRT HTRLVSLFNT TLTGLHEVSA
181 QNPTNCWICL PLNFRPYVSI PVPEQWNNFS TEINTTSVLV GPLVSNLEIT HTSNLTCVKF
241 SNTTYTTNSQ CIRWVTPPTQ IVCLPSGIFF VCGTSAYRCL NGSSESMCFL SFLVPPMTIY
301 TEQDLYSYVI SKPRNKRVPI LPFVIGAGVL GALGTGIGGI TTSTQFYYKL SQELNGDMER
361 VADSLVTLQD QLNSLAAVVL QNRRALDLLT AERGGTCLFL GEECCYYVNQ SGIVTEKVKE
421 IRDRIQRRAE ELRNTGPWGL LSQWMPWILP FLGPLAAIIL LLLFGPCIFN LLVNFVSSRI
481 EAVKLQMEPK MQSKTKIYRR PLDRPASPRS DVNDIKGTPP EEISAAQPLL RPNSAGSSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against ERVW-1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.45
- Highest tissue expression
- 51 nTPM
Expression across tissuesHPA
Tissue
- placenta: 51 nTPM
- retina: 6.4 nTPM
- testis: 5.8 nTPM
- epididymis: 3.3 nTPM
- choroid plexus: 2.3 nTPM
- stomach: 1.2 nTPM
Single-cell type
- syncytiotrophoblasts: 1,171 nCPM
- cytotrophoblasts: 307 nCPM
- migrating cytotrophoblasts: 175 nCPM
- extravillous trophoblasts: 80 nCPM
- early spermatids: 36 nCPM
- late primary spermatocytes: 34 nCPM
Immune cell
- eosinophil: 0.3 nTPM
- intermediate monocyte: 0.1 nTPM
- non-classical monocyte: 0.1 nTPM
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- gdT-cell: 0 nTPM
Brain region
- white matter: 24 nTPM
- cerebral cortex: 20 nTPM
- cerebellum: 20 nTPM
- hypothalamus: 19 nTPM
- pons: 19 nTPM
- medulla oblongata: 19 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about ERVW-1.
Disease | ImmuneIEDB
Conditions an epitope on ERVW-1 was assayed in.
- multiple sclerosis B cell
- myasthenia gravis B cell
ReferencesPubMed · IEDB
Publications for ERVW-1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.
Reference: AutoantibodyPubMed
2 publications
- Increased Presence of Antibodies against Type I Interferons and Human Endogenous Retrovirus W in Intensive Care Unit COVID-19 Patients.
2022 · Microbiol Spectr · RCR 2 · 31 citations - Anti-HERV-WEnv antibodies are correlated with seroreactivity against Mycobacterium avium subsp. paratuberculosis in children and youths at T1D risk.
2019 · Sci Rep · RCR 1 · 21 citations
Reference: B cellIEDB
2 publications
- Epitopes of HERV-Wenv induce antigen-specific humoral immunity in multiple sclerosis patients.
2015 · J Neuroimmunol · RCR 0.9 · 28 citations - Antibody Response to HERV-K and HERV-W Envelope Epitopes in Patients with Myasthenia Gravis.
2023 · Int J Mol Sci · RCR 0.3 · 4 citations
Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD missense Z
- 0.45
- DepMap mean gene effect
- -0.5
- DepMap dependency class
- selective
OntologyGO
Biological processes
- anatomical structure morphogenesis
- myoblast fusion
- syncytium formation
- syncytium formation by plasma membrane fusion
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads ERVW-1 as an antibody target. Whether an autoantibody or antibody against ERVW-1 could matter depends on whether native ERVW-1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
ERVW-1 is annotated at the cell surface, where native ERVW-1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label ERVW-1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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