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P11268

- ENV_MLVRD

UniProt

P11268 - ENV_MLVRD

Protein

Envelope glycoprotein

Gene

env

Organism
Radiation murine leukemia virus
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      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 bindingi117 – 1171ZincBy similarity
    Sitei467 – 4682Cleavage; by hostBy similarity
    Sitei644 – 6452Cleavage; by viral protease p14By similarity

    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 76
    Short name:
    gp76
    Transmembrane protein
    Short name:
    TM
    Alternative name(s):
    Envelope protein p15E
    Alternative name(s):
    p2E
    Gene namesi
    Name:env
    OrganismiRadiation murine leukemia virus
    Taxonomic identifieri11787 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000007778: 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 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 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 665634Envelope glycoproteinPRO_0000239590Add
    BLAST
    Chaini32 – 467436Surface proteinBy similarityPRO_0000040771Add
    BLAST
    Chaini468 – 644177Transmembrane proteinBy similarityPRO_0000040772Add
    BLAST
    Peptidei645 – 66521R-peptideBy similarityPRO_0000040773Add
    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
    Glycosylationi211 – 2111N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi334 ↔ 558Interchain (between SU and TM chains, or C-337 with C-558); in linked formBy similarity
    Disulfide bondi334 ↔ 337By similarity
    Glycosylationi356 – 3561N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi363 – 3631N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi364 ↔ 418By similarity
    Disulfide bondi383 ↔ 395By similarity
    Glycosylationi396 – 3961N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi400 – 4001N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi425 ↔ 438By similarity
    Glycosylationi432 – 4321N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi550 ↔ 557By similarity
    Lipidationi625 – 6251S-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

    ProteinModelPortaliP11268.
    SMRiP11268. Positions 40-266, 510-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 605574ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini627 – 66539CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei606 – 62621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 267236Receptor-binding domain (RBD)Sequence AnalysisAdd
    BLAST
    Regioni470 – 49021Fusion peptideBy similarityAdd
    BLAST
    Regioni533 – 54917ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili505 – 53228Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi334 – 3374CXXC
    Motifi550 – 5589CX6CC
    Motifi650 – 6534YXXL motif; contains endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi264 – 30542Pro-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.

    P11268-1 [UniParc]FASTAAdd to Basket

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    MESTTLSKPF KNQVNPWGPL IVLLILGRVN PVALGNSPHQ VFNLSWEVTN    50
    EDRETVWAIT GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YQAPFSPPPG 100
    PPCCSGSSGS TPGCSRDCEE PLTSYTPRCN TAWNRLKLSK VTHAHNEGFY 150
    VCPGPHRPRW ARSCGGPESF YCASWGCETT GRASWKPSSS WDYITVSNNL 200
    TSGQATPVCK NNTWCNSLTI RFTSLGKQAT SWVTGHWWGL RLYVSGHDPG 250
    LIFGIRLKIT DSGPRVPIGP NPVLSDQRPP SQPRSPPHSN STPTETPLTL 300
    PEPPPAGVEN RLLNLVKGAY QALNLTSPDR TQECWLCLVS GPPYYEGVAV 350
    LGTYSNHTSA PANCSVALQH KLTLSEVTGQ GLCVGAVPKT HQALCNTTQN 400
    TSGGSYYLAA PAGTIWACNT GLTPCLSTTV LNLTTDYCVL VELWPRVTYH 450
    SPSYVYHQFE RRGKYKREPV SLTLALLLGG LTMGGIAAGI GTGTTALVAT 500
    QQLQAAVHDD LKEVEKSITN LEKSLTSLSE VVLQNRRGLD LLFLKEGGLC 550
    AALKEECCFY ADHTGVVRDS MAKLRERLNQ RQKLFESGQG WFERLFNGSP 600
    WFTTLISTIM GPLIVLLLIL LLGPCILNRL VQFVKDRISV VQALVLTQQY 650
    HQLKSIDPEE MESRE 665
    Length:665
    Mass (Da):73,083
    Last modified:July 1, 1993 - v2
    Checksum:i93B2BFECC9E45984
    GO

    Sequence cautioni

    The sequence AAA46519.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03363 Genomic RNA. Translation: AAA46519.1. Different initiation.
    PIRiC26183. VCMVVR.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03363 Genomic RNA. Translation: AAA46519.1 . Different initiation.
    PIRi C26183. VCMVVR.

    3D structure databases

    ProteinModelPortali P11268.
    SMRi P11268. Positions 40-266, 510-562.
    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. "Nucleotide sequence of a radiation leukemia virus genome."
      Merregaert J., Janowski M., Reddy E.P.
      Virology 158:88-102(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiENV_MLVRD
    AccessioniPrimary (citable) accession number: P11268
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 96 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