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P10269

- ENV_BAEVM

UniProt

P10269 - ENV_BAEVM

Protein

Envelope glycoprotein

Gene

env

Organism
Baboon endogenous virus (strain M7)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      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 triggers the refolding of the transmembrane protein (TM) 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
    Sitei376 – 3772Cleavage; by hostBy similarity
    Sitei546 – 5472Cleavage; by viral proteaseBy similarity

    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:
    Surface protein
    Short name:
    SU
    Alternative name(s):
    Glycoprotein 70
    Short name:
    gp70
    Transmembrane protein
    Short name:
    TM
    Alternative name(s):
    Glycoprotein p20E
    Alternative name(s):
    p2E
    Gene namesi
    Name:env
    OrganismiBaboon endogenous virus (strain M7)
    Taxonomic identifieri11764 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
    Virus hostiPapio (baboons) [TaxID: 9554]
    Theropithecus gelada (Gelada baboon) [TaxID: 9565]
    ProteomesiUP000007443: Genome

    Subcellular locationi

    Chain Transmembrane protein : Virion membrane By similarity; Single-pass type I membrane protein By similarity. Host cell membrane By similarity; Single-pass type I membrane protein By similarity
    Note: It is probably 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
    Chain Surface protein : Virion membrane By similarity; Peripheral membrane protein By similarity. 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 extravirion surface through its binding to TM. It is probably 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 envelope Source: UniProtKB-KW
    4. 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 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 563545Envelope glycoproteinPRO_0000239549Add
    BLAST
    Chaini19 – 376358Surface proteinBy similarityPRO_0000040687Add
    BLAST
    Chaini377 – 546170Transmembrane proteinBy similarityPRO_0000040688Add
    BLAST
    Peptidei547 – 56317R-peptideBy similarityPRO_0000239550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi113 – 1131N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi219 – 2191N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi229 – 2291N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi236 ↔ 465Interchain (between SU and TM chains, or C-239 with C-465); in linked formBy similarity
    Disulfide bondi236 ↔ 239By similarity
    Glycosylationi264 – 2641N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi282 – 2821N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi292 – 2921N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi306 – 3061N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi312 – 3121N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi321 – 3211N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi339 – 3391N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi457 ↔ 464By similarity
    Glycosylationi469 – 4691N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi527 – 5271S-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

    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.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP10269.
    SMRiP10269. Positions 417-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 503485ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini525 – 56339CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei504 – 52421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni380 – 40021Fusion peptideSequence AnalysisAdd
    BLAST
    Regioni440 – 45617ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili401 – 45151Sequence AnalysisAdd
    BLAST
    Coiled coili461 – 49737Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi236 – 2394CXXC
    Motifi457 – 4659CX6CC
    Motifi552 – 5554YXXL motif; contains endocytosis signalBy similarity

    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.

    Keywords - Domaini

    Coiled coil, Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    InterProiIPR018154. TLV/ENV_coat_polyprotein.
    [Graphical view]
    PANTHERiPTHR10424. PTHR10424. 1 hit.
    PfamiPF00429. TLV_coat. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10269-1 [UniParc]FASTAAdd to Basket

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    MGFTTKIIFL YNLVLVYAGF DDPRKAIELV QKRYGRPCDC SGGQVSEPPS    50
    DRVSQVTCSG KTAYLMPDQR WKCKSIPKDT SPSGPLQECP CNSYQSSVHS 100
    SCYTSYQQCR SGNKTYYTAT LLKTQTGGTS DVQVLGSTNK LIQSPCNGIK 150
    GQSICWSTTA PIHVSDGGGP LDTTRIKSVQ RKLEEIHKAL YPELQYHPLA 200
    IPKVRDNLMV DAQTLNILNA TYNLLLMSNT SLVDDCWLCL KLGPPTPLAI 250
    PNFLLSYVTR SSDNISCLII PPLLVQPMQF SNSSCLFSPS YNSTEEIDLG 300
    HVAFSNCTSI TNVTGPICAV NGSVFLCGNN MAYTYLPTNW TGLCVLATLL 350
    PDIDIIPGDE PVPIPAIDHF IYRPKRAIQF IPLLAGLGIT AAFTTGATGL 400
    GVSVTQYTKL SNQLISDVQI LSSTIQDLQD QVDSLAEVVL QNRRGLDLLT 450
    AEQGGICLAL QEKCCFYVNK SGIVRDKIKT LQEELERRRK DLASNPLWTG 500
    LQGLLPYLLP FLGPLLTLLL LLTIGPCIFN RLTAFINDKL NIIHAMVLTQ 550
    QYQVLRTDEE AQD 563
    Length:563
    Mass (Da):61,879
    Last modified:July 1, 1989 - v1
    Checksum:i9573137DC4620BB7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10032 Genomic DNA. Translation: BAA00924.1.
    X05470 Genomic DNA. Translation: CAA29028.1.
    PIRiJT0262. VCMVM7.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10032 Genomic DNA. Translation: BAA00924.1 .
    X05470 Genomic DNA. Translation: CAA29028.1 .
    PIRi JT0262. VCMVM7.

    3D structure databases

    ProteinModelPortali P10269.
    SMRi P10269. Positions 417-469.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR018154. TLV/ENV_coat_polyprotein.
    [Graphical view ]
    PANTHERi PTHR10424. PTHR10424. 1 hit.
    Pfami PF00429. TLV_coat. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The entire nucleotide sequence of baboon endogenous virus DNA: a chimeric genome structure of murine type C and simian type D retroviruses."
      Kato S., Matsuo K., Nishimura N., Takahashi N., Takano T.
      Jpn. J. Genet. 62:127-137(1987)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiENV_BAEVM
    AccessioniPrimary (citable) accession number: P10269
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 89 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

    External Data

    Dasty 3