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P03388

- ENV_MCFF3

UniProt

P03388 - ENV_MCFF3

Protein

Envelope glycoprotein

Gene

env

Organism
Mink cell focus-forming murine leukemia virus (isolate CI-3)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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
    Sitei441 – 4422Cleavage; by hostBy similarity
    Sitei621 – 6222Cleavage; 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:
    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
    OrganismiMink cell focus-forming murine leukemia virus (isolate CI-3)
    Taxonomic identifieri11936 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]

    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 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 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 640608Envelope glycoproteinPRO_0000239578Add
    BLAST
    Chaini33 – 441409Surface proteinBy similarityPRO_0000040742Add
    BLAST
    Chaini442 – 621180Transmembrane proteinBy similarityPRO_0000040743Add
    BLAST
    Peptidei622 – 64019R-peptideBy similarityPRO_0000040744Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431N-linked (GlcNAc...); by hostBy similarity
    Glycosylationi58 – 581N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi109 ↔ 126By similarity
    Disulfide bondi118 ↔ 131By similarity
    Glycosylationi297 – 2971N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi307 ↔ 535Interchain (between SU and TM chains, or C-310 with C-535); in linked formBy similarity
    Disulfide bondi307 ↔ 310By similarity
    Glycosylationi329 – 3291N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi336 – 3361N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi337 ↔ 391By similarity
    Disulfide bondi356 ↔ 368By similarity
    Glycosylationi369 – 3691N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi398 ↔ 411By similarity
    Disulfide bondi527 ↔ 534By 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 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

    ProteinModelPortaliP03388.
    SMRiP03388. Positions 38-230, 487-539.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 582550ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini604 – 64037CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei583 – 60321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni444 – 46421Fusion peptideBy similarityAdd
    BLAST
    Regioni510 – 52617ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili473 – 50937Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi307 – 3104CXXC
    Motifi527 – 5359CX6CC
    Motifi627 – 6304YXXL motif; contains endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi255 – 2639Poly-Pro

    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

    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.

    P03388-1 [UniParc]FASTAAdd to Basket

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    MEGPAFSKPL KDKINPWGPL IILGILIRAG VSVQHDSPHQ VFNVTWRVTN    50
    LMTGQTANAT SLLGTMTDAF PKLYFDLCDL VGDDWDETGL GCRTPGGRKR 100
    ARTFDFYVCP GHTVPTGCGG PREGYCGKWG CETTGQAYWK PSSSWDLISL 150
    KRGNTPRNQG PCYDSSAVSS DIKGATPGGR CNPLVLEFTD AGKKASWDGP 200
    KVWGLRLYRS TGTDPVTRFS LTRQVLNIGP RVPIGPNPVI TDQLPPSRPV 250
    QIMLPRPPQP PPPGAASIVP ETAPPSQQLG TGDRLLNLVN GAYQALNLTS 300
    PDKTQECWLC LVAGPPYYEG VAVLGTYSNH TSAPANCSVA SQHKLTLSGV 350
    AGRGLCIAAF PKTHQALCNT TQKTSDGSYH LAAPAGTIWA CNTGLTPCLS 400
    TTVLDLTTDY CVLVELWPKV TYHSPSYVYG QFEKKKTKYK REPVSLTLAL 450
    LLGGLTMGGI AAGVGTGTTA LVATQQFQQL QAAMHDDLKE VEKSITNLEK 500
    SLTSLSEVVL QNRRGLDLLF LKEGGLCAAL KEECCFYADH TGLVRDSMAK 550
    LRERLSQRQK LFESQQGWFE GLFNKSPWFT TLISTIMGPL IILLLILLFG 600
    PWILNRLVQF IKDRISVVQA LVLTQQYHQL KTIGDCKSRE 640
    Length:640
    Mass (Da):69,726
    Last modified:July 21, 1986 - v1
    Checksum:iC2C71A6749128CF5
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti315 – 542228Missing in strain: Isolate CI-4.
    Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02725 Genomic RNA. Translation: AAA46375.1.
    K02726 Genomic RNA. Translation: AAA46376.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02725 Genomic RNA. Translation: AAA46375.1 .
    K02726 Genomic RNA. Translation: AAA46376.1 .

    3D structure databases

    ProteinModelPortali P03388.
    SMRi P03388. Positions 38-230, 487-539.
    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. "Envelope gene sequence of two in vitro-generated mink cell focus-forming murine leukemia viruses which contain the entire gp70 sequence of the endogenous nonecotropic parent."
      Mark G.E., Rapp U.R.
      J. Virol. 49:530-539(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate CI-3 and Isolate CI-4.

    Entry informationi

    Entry nameiENV_MCFF3
    AccessioniPrimary (citable) accession number: P03388
    Secondary accession number(s): Q85501
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The sequence shown is that of isolate CI-3.

    External Data

    Dasty 3