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P21415

- ENV_GALV

UniProt

P21415 - ENV_GALV

Protein

Envelope glycoprotein

Gene

env

Organism
Gibbon ape leukemia virus (GALV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (13 Jun 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 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
    Sitei489 – 4902Cleavage; by hostBy similarity
    Sitei669 – 6702Cleavage; by viral proteaseBy 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:
    Surface protein
    Short name:
    SU
    Alternative name(s):
    Glycoprotein 70
    Short name:
    gp70
    Transmembrane protein
    Short name:
    TM
    Alternative name(s):
    Envelope protein p15E
    Alternative name(s):
    p2E
    Gene namesi
    Name:env
    OrganismiGibbon ape leukemia virus (GALV)
    Taxonomic identifieri11840 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
    Virus hostiHylobatidae (gibbons) [TaxID: 9577]
    ProteomesiUP000008231: 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 extravirion 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 By similarity; Peripheral membrane protein By similarity
    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 – 4141Sequence AnalysisAdd
    BLAST
    Chaini42 – 685644Envelope glycoproteinPRO_0000239575Add
    BLAST
    Chaini42 – 489448Surface proteinBy similarityPRO_0000040731Add
    BLAST
    Chaini490 – 670181Transmembrane proteinBy similarityPRO_0000040732Add
    BLAST
    Peptidei671 – 68515R-peptideBy similarityPRO_0000239576Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi148 ↔ 169By similarity
    Disulfide bondi161 ↔ 174By similarity
    Glycosylationi301 – 3011N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi344 – 3441N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi354 ↔ 584Interchain (between SU and TM chains, or C-357 with C-584); in linked formBy similarity
    Disulfide bondi354 ↔ 357By similarity
    Glycosylationi415 – 4151N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi421 – 4211N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi433 – 4331N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi453 – 4531N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi576 ↔ 583By similarity
    Lipidationi651 – 6511S-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.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

    ProteinModelPortaliP21415.
    SMRiP21415. Positions 536-588.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 632591ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini654 – 68532CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei633 – 65321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni492 – 51221Fusion peptideBy similarityAdd
    BLAST
    Regioni559 – 57517ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili520 – 57051Sequence AnalysisAdd
    BLAST
    Coiled coili580 – 61637Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi354 – 3574CXXC
    Motifi576 – 5849CX6CC
    Motifi676 – 6794YXXL 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.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.

    P21415-1 [UniParc]FASTAAdd to Basket

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    MVLLPGSMLL TSNLHHLRHQ MSPGSWKRLI ILLSCVFGGG GTSLQNKNPH    50
    QPMTLTWQVL SQTGDVVWDT KAVQPPWTWW PTLKPDVCAL AASLESWDIP 100
    GTDVSSSKRV RPPDSDYTAA YKQITWGAIG CSYPRARTRM ASSTFYVCPR 150
    DGRTLSEARR CGGLESLYCK EWDCETTGTG YWLSKSSKDL ITVKWDQNSE 200
    WTQKFQQCHQ TGWCNPLKID FTDKGKLSKD WITGKTWGLR FYVSGHPGVQ 250
    FTIRLKITNM PAVAVGPDLV LVEQGPPRTS LALPPPLPPR EAPPPSLPDS 300
    NSTALATSAQ TPTVRKTIVT LNTPPPTTGD RLFDLVQGAF LTLNATNPGA 350
    TESCWLCLAM GPPYYEAIAS SGEVAYSTDL DRCRWGTQGK LTLTEVSGHG 400
    LCIGKVPFTH QHLCNQTLSI NSSGDHQYLL PSNHSWWACS TGLTPCLSTS 450
    VFNQTRDFCI QVQLIPRIYY YPEEVLLQAY DNSHPRTKRE AVSLTLAVLL 500
    GLGITAGIGT GSTALIKGPI DLQQGLTSLQ IAIDADLRAL QDSVSKLEDS 550
    LTSLSEVVLQ NRRGLDLLFL KEGGLCAALK EECCFYIDHS GAVRDSMKKL 600
    KEKLDKRQLE RQKSQNWYEG WFNNSPWFTT LLSTIAGPLL LLLLLLILGP 650
    CIINKLVQFI NDRISAVKIL VLRQKYQALE NEGNL 685
    Length:685
    Mass (Da):75,837
    Last modified:June 13, 2006 - v2
    Checksum:iD13AB40C5F3A1721
    GO

    Sequence cautioni

    The sequence AAA46811.1 differs from that shown. Reason: Frameshift at positions 667 and 674.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26927 Genomic RNA. Translation: AAA46811.1. Frameshift.
    AF055060 mRNA. Translation: AAC96083.1.
    PIRiC32595. VCLJGL.
    RefSeqiNP_056791.2. NC_001885.2.

    Genome annotation databases

    GeneIDi1491895.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26927 Genomic RNA. Translation: AAA46811.1 . Frameshift.
    AF055060 mRNA. Translation: AAC96083.1 .
    PIRi C32595. VCLJGL.
    RefSeqi NP_056791.2. NC_001885.2.

    3D structure databases

    ProteinModelPortali P21415.
    SMRi P21415. Positions 536-588.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1491895.

    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. "Genetic organization of gibbon ape leukemia virus."
      Delassus S., Sonigo P., Wain-Hobson S.
      Virology 173:205-213(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Simian sarcoma-associated virus fails to infect Chinese hamster cells despite the presence of functional gibbon ape leukemia virus receptors."
      Ting Y.T., Wilson C.A., Farrell K.B., Chaudry G.J., Eiden M.V.
      J. Virol. 72:9453-9458(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: SEATO.

    Entry informationi

    Entry nameiENV_GALV
    AccessioniPrimary (citable) accession number: P21415
    Secondary accession number(s): Q9YWM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 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