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Q14264

- ENR1_HUMAN

UniProt

Q14264 - ENR1_HUMAN

Protein

Endogenous retrovirus group 3 member 1 Env polyprotein

Gene

ERV3-1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
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    Functioni

    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 lost its fusogenic properties. It can inhibit cell growth through decrease expression of cyclin B1 and increased expression of p21 in vitro.3 Publications
    SU mediates receptor recognition.By similarity
    TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei471 – 4722CleavageBy similarity

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endogenous retrovirus group 3 member 1 Env polyprotein
    Alternative name(s):
    ERV-3 envelope protein
    Short name:
    ERV3 envelope protein
    ERV3-1 envelope protein
    Envelope polyprotein
    HERV-R envelope protein
    Short name:
    ERV-R envelope protein
    HERV-R_7q21.2 provirus ancestral Env polyprotein
    Cleaved into the following 2 chains:
    Surface protein
    Short name:
    SU
    Transmembrane protein
    Short name:
    TM
    Gene namesi
    Name:ERV3-1
    Synonyms:ERV3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:3454. ERV3-1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. viral envelope Source: UniProtKB-KW

    Keywords - Cellular componenti

    Viral envelope protein, Virion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27866.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 604582Endogenous retrovirus group 3 member 1 Env polyproteinPRO_0000008477Add
    BLAST
    Chaini23 – 471449Surface proteinBy similarityPRO_0000008478Add
    BLAST
    Chaini472 – 604133Transmembrane proteinBy similarityPRO_0000008479Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi369 – 3691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi527 – 5271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield the mature SU and TM proteins By similarity. Has been mainly detected in vivo as an 65 kDa unprocessed polyprotein precursor.By similarity
    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

    PaxDbiQ14264.
    PeptideAtlasiQ14264.
    PRIDEiQ14264.

    PTM databases

    PhosphoSiteiQ14264.

    Expressioni

    Tissue specificityi

    Expressed at higher level in adrenal, sebaceous glands and placenta. Expressed at lower level in bone marrow, brain, breast, colon, heart, kidney, liver, lung, ovary, PBL, prostate, skin, spleen, testis, thymus, thyroid, trachea.1 Publication

    Developmental stagei

    Highly expressed in primitive adrenal cortex and placenta. Expressed at lower level in developing nervous tissues, tongue, heart, gut, kidney, columna vertebralis and liver.1 Publication

    Gene expression databases

    BgeeiQ14264.
    CleanExiHS_ERV3.
    GenevestigatoriQ14264.

    Organism-specific databases

    HPAiHPA017209.

    Interactioni

    Subunit structurei

    The surface (SU) and transmembrane (TM) proteins form a heterodimer. SU and TM are attached by non-covalent interactions or by a labile interchain disulfide bond By similarity.By similarity

    Protein-protein interaction databases

    BioGridi108395. 1 interaction.
    STRINGi9606.ENSP00000391594.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14264.
    SMRiQ14264. Positions 489-594.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi165 – 1684CXXCBy similarity
    Motifi548 – 56417CKS-17By similarityAdd
    BLAST
    Motifi565 – 57410CX6CCBy similarity

    Domaini

    Contains the CKS-17 immunosuppressive domain present in many retroviral envelope proteins. As a synthetic peptide, it inhibits immune function in vitro and in vivo (By similarity).By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG126753.
    HOGENOMiHOG000112377.
    HOVERGENiHBG048920.
    OMAiWEARELM.
    OrthoDBiEOG7W6WK7.
    PhylomeDBiQ14264.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    Q14264-1 [UniParc]FASTAAdd to Basket

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    MLGMNMLLIT LFLLLPLSML KGEPWEGCLH CTHTTWSGNI MTKTLLYHTY    50
    YECAGTCLGT CTHNQTTYSV CDPGRGQPYV CYDPKSSPGT WFEIHVGSKE 100
    GDLLNQTKVF PSGKDVVSLY FDVCQIVSMG SLFPVIFSSM EYYSSCHKNR 150
    YAHPACSTDS PVTTCWDCTT WSTNQQSLGP IMLTKIPLEP DCKTSTCNSV 200
    NLTILEPDQP IWTTGLKAPL GARVSGEEIG PGAYVYLYII KKTRTRSTQQ 250
    FRVFESFYEH VNQKLPEPPP LASNLFAQLA ENIASSLHVA SCYVCGGMNM 300
    GDQWPWEARE LMPQDNFTLT ASSLEPAPSS QSIWFLKTSI IGKFCIARWG 350
    KAFTDPVGEL TCLGQQYYNE TLGKTLWRGK SNNSESPHPS PFSRFPSLNH 400
    SWYQLEAPNT WQAPSGLYWI CGPQAYRQLP AKWSGACVLG TIRPSFFLMP 450
    LKQGEALGYP IYDETKRKSK RGITIGDWKD NEWPPERIIQ YYGPATWAED 500
    GMWGYRTPVY MLNRIIRLQA VLEIITNETA GALNLLAQQA TKMRNVIYQN 550
    RLALDYLLAQ EEGVCGKFNL TNCCLELDDE GKVIKEITAK IQKLAHIPVQ 600
    TWKG 604
    Length:604
    Mass (Da):67,942
    Last modified:March 1, 2004 - v2
    Checksum:iC426D9193857D4BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti218 – 2181A → T in AAA88027. (PubMed:3840930)Curated
    Sequence conflicti226 – 2261G → D in AAA88027. (PubMed:3840930)Curated
    Sequence conflicti251 – 2511F → L in AAA88027. (PubMed:3840930)Curated

    Polymorphismi

    This envelope gene is polymorphic with at least five different alleles. A mutation introducing a premature stop codon instead of amino acid 223 is present in approximately 1% of the Caucasian population.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901T → I.2 Publications
    Corresponds to variant rs6460219 [ dbSNP | Ensembl ].
    VAR_017801
    Natural varianti192 – 1921C → Y.2 Publications
    Corresponds to variant rs34639489 [ dbSNP | Ensembl ].
    VAR_017802
    Natural varianti236 – 2361Y → C.2 Publications
    Corresponds to variant rs71539632 [ dbSNP | Ensembl ].
    VAR_017803
    Natural varianti481 – 4811N → S.2 Publications
    Corresponds to variant rs4618579 [ dbSNP | Ensembl ].
    VAR_017804
    Natural varianti522 – 5221L → P.1 Publication
    VAR_017805
    Natural varianti569 – 5691N → S.3 Publications
    Corresponds to variant rs4717229 [ dbSNP | Ensembl ].
    VAR_017806

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC073210 Genomic DNA. No translation available.
    M12140 Genomic DNA. Translation: AAA88027.1.
    CCDSiCCDS47595.1.
    RefSeqiNP_001007254.2. NM_001007253.3.
    UniGeneiHs.250693.

    Genome annotation databases

    EnsembliENST00000394323; ENSP00000391594; ENSG00000213462.
    GeneIDi2086.
    KEGGihsa:2086.
    UCSCiuc011kdr.2. human.

    Polymorphism databases

    DMDMi44887883.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC073210 Genomic DNA. No translation available.
    M12140 Genomic DNA. Translation: AAA88027.1 .
    CCDSi CCDS47595.1.
    RefSeqi NP_001007254.2. NM_001007253.3.
    UniGenei Hs.250693.

    3D structure databases

    ProteinModelPortali Q14264.
    SMRi Q14264. Positions 489-594.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108395. 1 interaction.
    STRINGi 9606.ENSP00000391594.

    PTM databases

    PhosphoSitei Q14264.

    Polymorphism databases

    DMDMi 44887883.

    Proteomic databases

    PaxDbi Q14264.
    PeptideAtlasi Q14264.
    PRIDEi Q14264.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394323 ; ENSP00000391594 ; ENSG00000213462 .
    GeneIDi 2086.
    KEGGi hsa:2086.
    UCSCi uc011kdr.2. human.

    Organism-specific databases

    CTDi 2086.
    GeneCardsi GC07M064451.
    HGNCi HGNC:3454. ERV3-1.
    HPAi HPA017209.
    neXtProti NX_Q14264.
    PharmGKBi PA27866.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG126753.
    HOGENOMi HOG000112377.
    HOVERGENi HBG048920.
    OMAi WEARELM.
    OrthoDBi EOG7W6WK7.
    PhylomeDBi Q14264.

    Miscellaneous databases

    GeneWikii ERV3.
    NextBioi 8469.
    PROi Q14264.

    Gene expression databases

    Bgeei Q14264.
    CleanExi HS_ERV3.
    Genevestigatori Q14264.

    Family and domain databases

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

    Publicationsi

    1. "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].
    2. "The nucleotide sequence of the env gene from the human provirus ERV3 and isolation and characterization of an ERV3-specific cDNA."
      Cohen M., Powers M., O'Connell C., Kato N.
      Virology 147:449-458(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-604, VARIANTS ILE-90; SER-481 AND SER-569.
    3. "Abundance of an endogenous retroviral envelope protein in placental trophoblasts suggests a biological function."
      Venables P.J.W., Brookes S.M., Griffiths D., Weiss R.A., Boyd M.T.
      Virology 211:589-592(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "The cellular mechanism by which the human endogenous retrovirus ERV-3 env gene affects proliferation and differentiation in a human placental trophoblast model, BeWo."
      Lin L., Xu B., Rote N.S.
      Placenta 21:73-78(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "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.
    6. "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.
    7. "Developmental expression of HERV-R (ERV3) and HERV-K in human tissue."
      Andersson A.-C., Venables P.J.W., Toenjes R.R., Scherer J., Eriksson L., Larsson E.
      Virology 297:220-225(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    8. "Physiological knockout of the envelope gene of the single-copy ERV-3 human endogenous retrovirus in a fraction of the Caucasian population."
      de Parseval N., Heidmann T.
      J. Virol. 72:3442-3445(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TYR-192; CYS-236; PRO-522 AND SER-569.
    9. "Large number of polymorphic nucleotides and a termination codon in the env gene of the endogenous human retrovirus ERV3."
      Rasmussen H.B., Clausen J.
      Dis. Markers 14:127-133(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ILE-90; TYR-192; CYS-236; SER-481 AND SER-569.

    Entry informationi

    Entry nameiENR1_HUMAN
    AccessioniPrimary (citable) accession number: Q14264
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2004
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 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

    HERV-R_7q21.2 genomic and subgenomic RNAs have been observed.
    This provirus is intergenic, the closest flanking genes being ZNF117 and FLJ25037.

    Caution

    CKS-17 sequence does not match the minimal active consensus.Curated
    Truncated; premature stop codon upstream of the fusion peptide on TM.Curated

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3