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P08360

- ENV_MLVCB

UniProt

P08360 - ENV_MLVCB

Protein

Envelope glycoprotein

Gene

env

Organism
Cas-Br-E murine leukemia virus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Aug 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
    Metal bindingi86 – 861ZincBy similarity
    Metal bindingi117 – 1171ZincBy similarity
    Sitei465 – 4662Cleavage; by hostBy similarity
    Sitei645 – 6462Cleavage; by viral protease p14

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. 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

    Keywords - Ligandi

    Metal-binding, Zinc

    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
    OrganismiCas-Br-E murine leukemia virus
    Taxonomic identifieri11792 [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 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 661628Envelope glycoproteinPRO_0000239580Add
    BLAST
    Chaini34 – 465432Surface proteinBy similarityPRO_0000040748Add
    BLAST
    Chaini466 – 645180Transmembrane proteinBy similarityPRO_0000040749Add
    BLAST
    Peptidei646 – 66116R-peptidePRO_0000040750Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi77 ↔ 129By similarity
    Disulfide bondi103 ↔ 118By similarity
    Disulfide bondi104 ↔ 114By similarity
    Disulfide bondi152 ↔ 172By similarity
    Disulfide bondi164 ↔ 177By similarity
    Glycosylationi199 – 1991N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi209 ↔ 215By similarity
    Glycosylationi322 – 3221N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi332 ↔ 559Interchain (between SU and TM chains, or C-335 with C-559); in linked form
    Disulfide bondi332 ↔ 335
    Glycosylationi361 – 3611N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi362 ↔ 416By similarity
    Disulfide bondi381 ↔ 393By similarity
    Glycosylationi394 – 3941N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi423 ↔ 436By similarity
    Glycosylationi430 – 4301N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi551 ↔ 558By similarity
    Lipidationi626 – 6261S-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

    ProteinModelPortaliP08360.
    SMRiP08360. Positions 40-266, 511-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 606573ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini628 – 66134CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei607 – 62721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 267236Receptor-binding domain (RBD)Sequence AnalysisAdd
    BLAST
    Regioni468 – 48821Fusion peptideBy similarityAdd
    BLAST
    Regioni534 – 55017ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili497 – 53337Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi332 – 3354CXXC
    Motifi551 – 5599CX6CC
    Motifi651 – 6544YXXL motif; contains endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi264 – 30239Pro-richAdd
    BLAST

    Domaini

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

    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.

    P08360-1 [UniParc]FASTAAdd to Basket

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    MEGPAFSKSP KDKTIERAFL GVLGILFVTG GLASRDNPHQ VYNITWEVTN    50
    GEQDTVWAVT GNHPLWTWWP DLTPDLCMLA LHGPTHWGLD NHPPYSSPPG 100
    PPCCSGDAGA VSGCARDCDE PLTSYSPRCN TAWNRLKLAR VTHAPKEGFY 150
    ICPGSHRPRW ARSCGGLDAY YCASWGCETT GRAAWNPTSS WDYITVSNNL 200
    TSSQATKACK NNGWCNPLVI RFTGPGKRAT SWTTGHFWGL RLYISGHDPG 250
    LTFGIRLKVT DLGPRVPIGP NPVLSDQRPP SRPVPARPPP PSASPSTPTI 300
    PPQQGTGDRL LNLVQGAYLT LNMTDPTRTQ ECWLCLVSEP PYYEGVAVLR 350
    EYTSHETAPA NCSSGSQHKL TLSEVTGQGR CLGTVPKTHQ ALCNRTEPTV 400
    SGSNYLVAPE GTLWACSTGL TPCLSTTVLN LTTDYCVLVE LWPKVTYHSP 450
    DYVYTQFEPG ARFRREPVSL TLALLPEGLT MGGIAAGVGT GTTALVATQQ 500
    FQQLQAAMHN DLKEVEKSIT NLEKSLTSLS EVVLQNRRGL DLLFLKEGGL 550
    CAALKEECCF YADHTGLVRD SMAKLRERLN QRQKLFESGQ GWFEGLFNRS 600
    PWFTTLISTI MGPLIVLLLI LLFGPCILNR LVQFVKDRIS VVQALVLTQQ 650
    YHQLKPIEYE P 661
    Length:661
    Mass (Da):72,625
    Last modified:August 1, 1988 - v1
    Checksum:i255BEE3AF62FB9FF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti476 – 4772PE → LG(PubMed:1840655)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14702 Genomic DNA. Translation: AAA46512.1.
    X57540 Genomic DNA. No translation available.
    PIRiB26103. VCMVCB.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14702 Genomic DNA. Translation: AAA46512.1 .
    X57540 Genomic DNA. No translation available.
    PIRi B26103. VCMVCB.

    3D structure databases

    ProteinModelPortali P08360.
    SMRi P08360. Positions 40-266, 511-563.
    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. "Cas-Br-E murine leukemia virus: sequencing of the paralytogenic region of its genome and derivation of specific probes to study its origin and the structure of its recombinant genomes in leukemic tissues."
      Rassart E., Nelbach L., Jolicoeur P.
      J. Virol. 60:910-919(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete nucleotide sequence of the neurotropic murine retrovirus CAS-BR-E."
      Perryman S.M., McAtee F.J., Portis J.L.
      Nucleic Acids Res. 19:1707-1707(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Identification of R-peptides in envelope proteins of C-type retroviruses."
      Bobkova M., Stitz J., Engelstadter M., Cichutek K., Buchholz C.J.
      J. Gen. Virol. 83:2241-2246(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF R-PEPTIDE.

    Entry informationi

    Entry nameiENV_MLVCB
    AccessioniPrimary (citable) accession number: P08360
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program