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Q27ID8

- ENV_XMRV6

UniProt

Q27ID8 - ENV_XMRV6

Protein

Envelope glycoprotein

Gene

env

Organism
Xenotropic MuLV-related virus (isolate VP62) (XMRV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack the disulfide and cause its isomerization into a disulfide isomer within the motif. This leads to SU displacement and TM refolding, and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane By similarity.By similarity
    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 viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei444 – 4452Cleavage; by hostBy similarity
    Sitei624 – 6252Cleavage; by viral protease p14By similarity

    GO - Molecular functioni

    1. structural molecule activity Source: InterPro

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
    2. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Envelope glycoprotein
    Alternative name(s):
    Env polyprotein
    Cleaved into the following 3 chains:
    Gene namesi
    Name:env
    OrganismiXenotropic MuLV-related virus (isolate VP62) (XMRV)
    Taxonomic identifieri373193 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000002240: Genome

    Subcellular locationi

    Chain Surface protein : Virion membrane; Peripheral membrane protein. Host cell membrane By similarity; Peripheral membrane protein By similarity
    Note: The surface protein is not anchored to the viral envelope, but associates with the virion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag By similarity.By similarity
    R-peptide : Host cell membrane; Peripheral membrane protein
    Note: The R-peptide is membrane-associated through its palmitate.By similarity

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral capsid Source: InterPro
    4. viral envelope Source: UniProtKB-KW
    5. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 645612Envelope glycoproteinBy similarityPRO_0000390831Add
    BLAST
    Chaini34 – 444411Surface proteinBy similarityPRO_0000390832Add
    BLAST
    Chaini445 – 645201Transmembrane proteinBy similarityPRO_0000390833Add
    BLAST
    Peptidei625 – 64521R-peptideBy similarityPRO_0000390834Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi58 – 581N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi113 ↔ 130By similarity
    Disulfide bondi122 ↔ 135By similarity
    Glycosylationi301 – 3011N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi311 ↔ 538Interchain (between SU and TM chains, or C-314 with C-538); in linked formBy similarity
    Disulfide bondi311 ↔ 314By similarity
    Glycosylationi333 – 3331N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi340 – 3401N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi341 ↔ 395By similarity
    Disulfide bondi360 ↔ 372By similarity
    Glycosylationi373 – 3731N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi402 ↔ 415By similarity
    Glycosylationi409 – 4091N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi530 ↔ 537By similarity
    Lipidationi605 – 6051S-palmitoyl cysteine; by hostBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as a inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease 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 R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic By similarity.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
    The transmembrane protein is palmitoylated.By similarity
    The R-peptide is palmitoylated.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by a labile interchain disulfide bond. The activated Env consists of SU monomers and TM trimers By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ27ID8.
    SMRiQ27ID8. Positions 38-234, 490-542.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 585552ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini607 – 64034CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei586 – 60621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 237206Receptor-binding domain (RBD)Sequence AnalysisAdd
    BLAST
    Regioni447 – 46721Fusion peptideBy similarityAdd
    BLAST
    Regioni513 – 52917ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili490 – 51021Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi311 – 3144CXXCBy similarity
    Motifi530 – 5389CX6CCBy similarity
    Motifi630 – 6334YXXL motif; contains endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi234 – 28350Pro-richAdd
    BLAST

    Domaini

    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.By similarity
    The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.By similarity

    Keywords - Domaini

    Coiled coil, Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di3.90.310.10. 1 hit.
    InterProiIPR008981. FMuLV_rcpt-bd.
    IPR018154. TLV/ENV_coat_polyprotein.
    [Graphical view]
    PANTHERiPTHR10424. PTHR10424. 1 hit.
    PfamiPF00429. TLV_coat. 1 hit.
    [Graphical view]
    SUPFAMiSSF49830. SSF49830. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q27ID8-1 [UniParc]FASTAAdd to Basket

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    MESPAFSKPL KDKINPWGPL IIMGILVRAG ASVQRDSPHQ VFNVTWKITN    50
    LMTGQTANAT SLLGTMTDTF PKLYFDLCDL VGDNWDDPEP DIGDGCRSPG 100
    GRKRTRLYDF YVCPGHTVLT GCGGPREGYC GKWGCETTGQ AYWKPSSSWD 150
    LISLKRGNTP KGQGPCFDSS VGSGSIQGAT PGGRCNPLVL EFTDAGKRAS 200
    WDAPKTWGLR LYRSTGADPV TLFSLTRQVL NVGPRVPIGP NPVITEQLPP 250
    SQPVQIMLPR TPRPPPSGAA SMVPGAPPPS QQPGTGDRLL NLVEGAYLAL 300
    NLTSPDKTQE CWLCLVSGPP YYEGVAVLGT YSNHTSAPAN CSVTSQHKLT 350
    LSEVTGQGLC IGAVPKTHQA LCNTTQKTSD GSYYLASPAG TIWACSTGLT 400
    PCLSTTVLNL TTDYCVLVEL WPKVTYHSPN YVYGQFEKKT KYKREPVSLT 450
    LALLLGGLTM GGIAAGVGTG TTALVATKQF EQLQAAIHTD LGALEKSVSA 500
    LEKSLTSLSE VVLQNRRGLD LLFLKEGGLC AALKEECCFY ADHTGVVRDS 550
    MAKLRERLNQ RQKLFESGQG WFEGLFNRSP WFTTLISTIM GPLIVLLLIL 600
    LFGPCILNRL VQFVKDRISV VQALVLTQQY HQLKSIDPEE VESRE 645
    Length:645
    Mass (Da):69,876
    Last modified:April 4, 2006 - v1
    Checksum:i19ACC5E3EAF9AEC3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2611T → P in ABM47429. (PubMed:16609730)Curated
    Sequence conflicti298 – 2981L → Q in ABM47429. (PubMed:16609730)Curated
    Sequence conflicti568 – 5681G → R in ABM47429. (PubMed:16609730)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ399707 Genomic RNA. Translation: ABD49688.1.
    EF185282 Genomic RNA. Translation: ABM47429.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ399707 Genomic RNA. Translation: ABD49688.1 .
    EF185282 Genomic RNA. Translation: ABM47429.1 .

    3D structure databases

    ProteinModelPortali Q27ID8.
    SMRi Q27ID8. Positions 38-234, 490-542.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.90.310.10. 1 hit.
    InterProi IPR008981. FMuLV_rcpt-bd.
    IPR018154. TLV/ENV_coat_polyprotein.
    [Graphical view ]
    PANTHERi PTHR10424. PTHR10424. 1 hit.
    Pfami PF00429. TLV_coat. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49830. SSF49830. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel Gammaretrovirus in prostate tumors of patients homozygous for R462Q RNASEL variant."
      Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A., Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H., DeRisi J.L.
      PLoS Pathog. 2:E25-E25(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "An infectious retrovirus susceptible to an IFN antiviral pathway from human prostate tumors."
      Dong B., Kim S., Hong S., Das Gupta J., Malathi K., Klein E.A., Ganem D., Derisi J.L., Chow S.A., Silverman R.H.
      Proc. Natl. Acad. Sci. U.S.A. 104:1655-1660(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiENV_XMRV6
    AccessioniPrimary (citable) accession number: Q27ID8
    Secondary accession number(s): A1Z653
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 19, 2010
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 42 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    External Data

    Dasty 3