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Q9UQF0 (ENW1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
HERV-W_7q21.2 provirus ancestral Env polyprotein
Alternative name(s):
Endogenous retrovirus group W member 1
Env-W
Envelope polyprotein gPr73
Enverin
HERV-7q Envelope protein
HERV-W envelope protein
Syncytin
Syncytin-1

Cleaved into the following 2 chains:

  1. Surface protein
    Short name=SU
    Alternative name(s):
    gp50
  2. Transmembrane protein
    Short name=TM
    Alternative name(s):
    gp24
Gene names
Name:ERVW-1
Synonyms:ERVWE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has retained its original fusogenic properties and participates in trophoblast fusion during placenta morphogenesis. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17

SU mediates receptor recognition. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide By similarity. Seems to recognize the type D mammalian retrovirus receptors SLC1A4 and SLC1A5, as it induces fusion of cells expressing these receptors in vitro. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17

The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has 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 By similarity. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17

Subunit structure

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. Ref.19

Subcellular location

Transmembrane protein: Cell membrane; Single-pass type I membrane protein By similarity.

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.

HERV-W_7q21.2 provirus ancestral Env polyprotein: Virion By similarity.

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. Ref.2 Ref.9 Ref.15 Ref.18

Developmental stage

In placenta, detected at higher level during early pregnancy and at lower level during late pregnancy. Ref.16

Domain

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.

Post-translational modification

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.

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.

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.

Sequence similarities

Belongs to the gamma type-C retroviral envelope protein family. HERV class-I W env subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 538518HERV-W_7q21.2 provirus ancestral Env polyprotein
PRO_0000008485
Chain21 – 317297Surface protein
PRO_0000008486
Chain318 – 538221Transmembrane protein
PRO_0000008487

Regions

Topological domain21 – 443423Extracellular Potential
Transmembrane444 – 46421Helical; Potential
Topological domain465 – 53874Cytoplasmic Potential
Region320 – 34021Fusion peptide Potential
Region380 – 39617Immunosuppression By similarity
Region465 – 48420Essential for the fusiogenic function
Motif186 – 1894CXXC By similarity
Motif397 – 4059CX6CC By similarity

Sites

Site317 – 3182Cleavage

Amino acid modifications

Glycosylation1691N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation2141N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation2811N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Disulfide bond186 ↔ 405Interchain (between SU and TM chains, or C-189 with C-405); alternate By similarity
Disulfide bond186 ↔ 189Alternate By similarity
Disulfide bond397 ↔ 404 By similarity

Natural variations

Natural variant1291V → A. Ref.4
Corresponds to variant rs142852059 [ dbSNP | Ensembl ].
VAR_018638
Natural variant1381R → Q. Ref.4
Corresponds to variant rs55903518 [ dbSNP | Ensembl ].
VAR_018639
Natural variant3071S → N. Ref.2 Ref.4 Ref.7
Corresponds to variant rs10266695 [ dbSNP | Ensembl ].
VAR_018640
Natural variant4771S → F. Ref.4
Corresponds to variant rs141340741 [ dbSNP | Ensembl ].
VAR_018641

Experimental info

Mutagenesis314 – 3163RNK → AAA: Complete loss of cleavage between SU and TM. Loss of fusiogenic function. Ref.19
Mutagenesis3171R → T: Complete loss of cleavage between SU and TM. Loss of fusiogenic function. Ref.19
Mutagenesis4051C → A: Loss of fusiogenic function. No effect on cleavage between SU and TM. Ref.19
Sequence conflict13 – 142LL → VS in AAD14545. Ref.1
Sequence conflict561S → C in AAD14545. Ref.1
Sequence conflict2981T → A in AAD14545. Ref.1
Sequence conflict2981T → A in AAD14548. Ref.1
Sequence conflict3811Q → R in AAF74215. Ref.3
Sequence conflict3881L → S in AAD14548. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UQF0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C54648A3C7043870

FASTA53859,866
        10         20         30         40         50         60 
MALPYHIFLF TVLLPSFTLT APPPCRCMTS SSPYQEFLWR MQRPGNIDAP SYRSLSKGTP 

        70         80         90        100        110        120 
TFTAHTHMPR NCYHSATLCM HANTHYWTGK MINPSCPGGL GVTVCWTYFT QTGMSDGGGV 

       130        140        150        160        170        180 
QDQAREKHVK EVISQLTRVH GTSSPYKGLD LSKLHETLRT HTRLVSLFNT TLTGLHEVSA 

       190        200        210        220        230        240 
QNPTNCWICL PLNFRPYVSI PVPEQWNNFS TEINTTSVLV GPLVSNLEIT HTSNLTCVKF 

       250        260        270        280        290        300 
SNTTYTTNSQ CIRWVTPPTQ IVCLPSGIFF VCGTSAYRCL NGSSESMCFL SFLVPPMTIY 

       310        320        330        340        350        360 
TEQDLYSYVI SKPRNKRVPI LPFVIGAGVL GALGTGIGGI TTSTQFYYKL SQELNGDMER 

       370        380        390        400        410        420 
VADSLVTLQD QLNSLAAVVL QNRRALDLLT AERGGTCLFL GEECCYYVNQ SGIVTEKVKE 

       430        440        450        460        470        480 
IRDRIQRRAE ELRNTGPWGL LSQWMPWILP FLGPLAAIIL LLLFGPCIFN LLVNFVSSRI 

       490        500        510        520        530 
EAVKLQMEPK MQSKTKIYRR PLDRPASPRS DVNDIKGTPP EEISAAQPLL RPNSAGSS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Endogenous retroviruses and multiple sclerosis. II. HERV-7q."
Alliel P.M., Perin J.-P., Pierig R., Nussbaum J.-L., Menard A., Rieger F.
C. R. Acad. Sci. III, Sci. Vie 321:857-863(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001124397.1. NM_001130925.1.
NP_055405.3. NM_014590.3.

3D structure databases

ProteinModelPortalQ9UQF0.
SMRQ9UQF0. Positions 357-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119040. 2 interactions.
STRING9606.ENSP00000419945.

Protein family/group databases

TCDB1.G.9.1.1. the syncytin (syncytin) family.

PTM databases

PhosphoSiteQ9UQF0.

Polymorphism databases

DMDM47605755.

Proteomic databases

PaxDbQ9UQF0.
PRIDEQ9UQF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000493463; ENSP00000419945; ENSG00000242950.
ENST00000603053; ENSP00000474984; ENSG00000242950.
GeneID30816.
KEGGhsa:30816.
UCSCuc022ahe.1. human.

Organism-specific databases

CTD30816.
GeneCardsGC07M092098.
HGNCHGNC:13525. ERVW-1.
MIM604659. gene.
neXtProtNX_Q9UQF0.
PharmGKBPA27878.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG131568.
HOVERGENHBG051487.
InParanoidQ9UQF0.
OMAHANTHYW.
OrthoDBEOG70ZZQM.
PhylomeDBQ9UQF0.
TreeFamTF332233.

Gene expression databases

ArrayExpressQ9UQF0.
BgeeQ9UQF0.
GenevestigatorQ9UQF0.

Family and domain databases

InterProIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERPTHR10424. PTHR10424. 1 hit.
PfamPF00429. TLV_coat. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSERVW-1. human.
GeneWikiERVWE1.
GenomeRNAi30816.
NextBio52878.
PROQ9UQF0.
SOURCESearch...

Entry information

Entry nameENW1_HUMAN
AccessionPrimary (citable) accession number: Q9UQF0
Secondary accession number(s): B2RPD4 expand/collapse secondary AC list , O95244, O95245, Q8NHY7, Q9NRZ2, Q9NZG3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM