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P06445

- ENV_RMCFV

UniProt

P06445 - ENV_RMCFV

Protein

Envelope glycoprotein

Gene

env

Organism
Rauscher mink cell focus-inducing virus
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      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
    Sitei443 – 4442Cleavage; by hostBy similarity
    Sitei623 – 6242Cleavage; 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
    OrganismiRauscher mink cell focus-inducing virus
    Taxonomic identifieri11784 [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_0000239598Add
    BLAST
    Chaini33 – 443411Surface proteinBy similarityPRO_0000040792Add
    BLAST
    Chaini444 – 623180Transmembrane proteinBy similarityPRO_0000040793Add
    BLAST
    Peptidei624 – 64017R-peptideBy similarityPRO_0000040794Add
    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
    Glycosylationi300 – 3001N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi310 ↔ 537Interchain (between SU and TM chains, or C-310 with C-535); in linked formBy similarity
    Disulfide bondi310 ↔ 313By similarity
    Glycosylationi332 – 3321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi339 – 3391N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi372 – 3721N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi408 – 4081N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi529 ↔ 536By similarity
    Lipidationi604 – 6041S-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

    ProteinModelPortaliP06445.
    SMRiP06445. Positions 38-233, 489-541.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini33 – 584552ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini606 – 64035CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei585 – 60521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 236205Receptor-binding domain (RBD)Sequence AnalysisAdd
    BLAST
    Regioni446 – 46621Fusion peptideBy similarityAdd
    BLAST
    Regioni512 – 52817ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili477 – 51135Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi310 – 3134CXXC
    Motifi529 – 5379CX6CC
    Motifi629 – 6324YXXL motif; contains endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi233 – 28250Pro-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.

    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.

    P06445-1 [UniParc]FASTAAdd to Basket

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    MACSTFSKPL KDKINPWGPL IILGILIRAG VSVQHDSPHK VFNVTWRVTN    50
    LMTGQTANAT SLLGTMTDAF PKLYFDLCDL VGDYWDDPEP DIGDGCRTPG 100
    GRRRTRLYDF YVCPGHTVPI GCGGPGEGYC GKWGCETTGQ AYWKPSSSWD 150
    LISLKRGNTP KDQGPCYDSS VSSDIKGATP GGRCNPLVLE FTDAGKKASW 200
    DGPKVWGLRL YRSTGTDPVT RFSLTRRVLN IGPRVPIGPN PVIIDQLPPS 250
    RPVQIMLPRP PQPPPPGAAS IVPETAPPSQ QPGTGDRLLN LVDGAYQALN 300
    LTSPDKTQEC WLCLVAEPPY YEGVAVLGTY SNHTSAPTNC SVASQHKLTL 350
    SEVTGQGLCI GTVPKTHQAL CNTTLKTNKG SYYLVAPAGT TWACNTGLTP 400
    CLSATVLNRT TDYCVLVELW PRVTYHPPSY VYSQFEKSYR HKREPVSLTL 450
    ALLLGGLTMG GIAAGVGTGT TALVATQQFQ QLHAAVQDDL KEVEKSITNL 500
    EKSLTSLSEV VLQNRRGLDL LFLKEGGLCA ALKEECCFYA DHTGLVRDSM 550
    AKLRERLTQR QKLFESSQGW FEGLFNRSPW FTTLISTIMG PLIILLLILL 600
    FGPCILNRLV QFVKDRISVV QALVLTQQYH QLKPLEYEPQ 640
    Length:640
    Mass (Da):70,072
    Last modified:January 1, 1988 - v1
    Checksum:i1E4450343643D799
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10100 Genomic RNA. Translation: AAA46528.1.
    PIRiA03990. VCMVRV.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10100 Genomic RNA. Translation: AAA46528.1 .
    PIRi A03990. VCMVRV.

    3D structure databases

    ProteinModelPortali P06445.
    SMRi P06445. Positions 38-233, 489-541.
    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 and long terminal repeat determine the different biological properties of Rauscher, Friend, and Moloney mink cell focus-inducing viruses."
      Vogt M., Haggblom C., Swift S., Haas M.
      J. Virol. 55:184-192(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiENV_RMCFV
    AccessioniPrimary (citable) accession number: P06445
    Secondary accession number(s): Q85628, Q85629, Q89529
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program