Q9UQF0 (ENW1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	538 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Viral envelope protein Virion
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome ERV Reference proteome Transposable element
Gene Ontology (GO)
Biological_process	syncytium formation Traceable author statement Ref.2. Source: ProtInc
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell viral envelope Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 538	518	HERV-W_7q21.2 provirus ancestral Env polyprotein		PRO_0000008485
	Chain	21 – 317	297	Surface protein		PRO_0000008486
	Chain	318 – 538	221	Transmembrane protein		PRO_0000008487
Regions
	Topological domain	21 – 443	423	Extracellular Potential
	Transmembrane	444 – 464	21	Helical; Potential
	Topological domain	465 – 538	74	Cytoplasmic Potential
	Region	320 – 340	21	Fusion peptide Potential
	Region	380 – 396	17	Immunosuppression By similarity
	Region	465 – 484	20	Essential for the fusiogenic function
	Motif	186 – 189	4	CXXC By similarity
	Motif	397 – 405	9	CX6CC By similarity
Sites
	Site	317 – 318	2	Cleavage
Amino acid modifications
	Glycosylation	169	1	N-linked (GlcNAc...) Potential
	Glycosylation	208	1	N-linked (GlcNAc...) Potential
	Glycosylation	214	1	N-linked (GlcNAc...) Potential
	Glycosylation	234	1	N-linked (GlcNAc...) Potential
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
	Glycosylation	281	1	N-linked (GlcNAc...) Potential
	Glycosylation	409	1	N-linked (GlcNAc...) Potential
	Disulfide bond	186 ↔ 405		Interchain (between SU and TM chains, or C-189 with C-405); alternate By similarity
	Disulfide bond	186 ↔ 189		Alternate By similarity
	Disulfide bond	397 ↔ 404		By similarity
Natural variations
	Natural variant	129	1	V → A. Ref.4		VAR_018638
	Natural variant	138	1	R → Q. Ref.4 Corresponds to variant rs55903518 [ dbSNP | Ensembl ].		VAR_018639
	Natural variant	307	1	S → N. Ref.2 Ref.4 Ref.7 Corresponds to variant rs10266695 [ dbSNP | Ensembl ].		VAR_018640
	Natural variant	477	1	S → F. Ref.4		VAR_018641
Experimental info
	Mutagenesis	314 – 316	3	RNK → AAA: Complete loss of cleavage between SU and TM. Loss of fusiogenic function. Ref.19
	Mutagenesis	317	1	R → T: Complete loss of cleavage between SU and TM. Loss of fusiogenic function. Ref.19
	Mutagenesis	405	1	C → A: Loss of fusiogenic function. No effect on cleavage between SU and TM. Ref.19
	Sequence conflict	13 – 14	2	LL → VS in AAD14545. Ref.1
	Sequence conflict	56	1	S → C in AAD14545. Ref.1
	Sequence conflict	298	1	T → A in AAD14545. Ref.1
	Sequence conflict	298	1	T → A in AAD14548. Ref.1
	Sequence conflict	381	1	Q → R in AAF74215. Ref.3
	Sequence conflict	388	1	L → S in AAD14548. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UQF0 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C54648A3C7043870	FASTA	538	59,866
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Web resources

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

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.
IPI	IPI00329525.
RefSeq	NP_001124397.1. NM_001130925.1. NP_055405.3. NM_014590.3.
3D structure databases
ProteinModelPortal	Q9UQF0.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000419945.
PTM databases
PhosphoSite	Q9UQF0.
Polymorphism databases
DMDM	47605755.
Proteomic databases
PaxDb	Q9UQF0.
PRIDE	Q9UQF0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000493463; ENSP00000419945; ENSG00000242950.
GeneID	30816.
KEGG	hsa:30816.
UCSC	uc022ahe.1. human.
Organism-specific databases
CTD	30816.
GeneCards	GC07M092098.
HGNC	HGNC:13525. ERVW-1.
MIM	604659. gene.
neXtProt	NX_Q9UQF0.
PharmGKB	PA27878.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG131568.
HOVERGEN	HBG051487.
InParanoid	Q9UQF0.
OMA	HANTHYW.
OrthoDB	EOG4QJRN1.
PhylomeDB	Q9UQF0.
Gene expression databases
ArrayExpress	Q9UQF0.
Bgee	Q9UQF0.
Genevestigator	Q9UQF0.
GermOnline	ENSG00000197604. Homo sapiens.
Family and domain databases
InterPro	IPR018154. TLV/ENV_coat_polyprotein. [Graphical view]
PANTHER	PTHR10424. PTHR10424. 1 hit.
Pfam	PF00429. TLV_coat. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ERVW-1. human.
GenomeRNAi	30816.
NextBio	52878.
SOURCE	Search...

Entry information

Entry name

ENW1_HUMAN

Accession

Primary (citable) accession number: Q9UQF0
Secondary accession number(s): B2RPD4 , O95244, O95245, Q8NHY7, Q9NRZ2, Q9NZG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.