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P11269

- GAG_MLVRD

UniProt

P11269 - GAG_MLVRD

Protein

Gag polyprotein

Gene

gag

Organism
Radiation murine leukemia virus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Gag polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release By similarity.By similarity
    Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex By similarity.By similarity
    Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.By similarity
    Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei129 – 1302Cleavage; by viral protease p14By similarity
    Sitei214 – 2152Cleavage; by viral protease p14By similarity
    Sitei477 – 4782Cleavage; by viral protease p14By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri501 – 51818CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW
    2. structural constituent of virion Source: UniProtKB-KW
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. viral budding via host ESCRT complex Source: UniProtKB-KW
    2. viral release from host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Virus exit from host cell

    Keywords - Ligandi

    Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gag polyprotein
    Alternative name(s):
    Core polyprotein
    Cleaved into the following 4 chains:
    Matrix protein p15
    Short name:
    MA
    Alternative name(s):
    pp12
    Capsid protein p30
    Short name:
    CA
    Nucleocapsid protein p10
    Short name:
    NC-gag
    Gene namesi
    Name:gag
    OrganismiRadiation murine leukemia virus
    Taxonomic identifieri11787 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000007778: Genome

    Subcellular locationi

    Chain Gag polyprotein : Virion By similarity. Host cell membrane Curated; Lipid-anchor Curated. Host late endosome membrane Curated; Lipid-anchor Curated. Host endosomehost multivesicular body By similarity
    Note: These locations are probably linked to virus assembly sites.By similarity

    GO - Cellular componenti

    1. host cell late endosome membrane Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. host multivesicular body Source: UniProtKB-SubCell
    4. membrane Source: UniProtKB-KW
    5. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cell membrane, Host endosome, Host membrane, Membrane, Viral matrix protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 537536Gag polyproteinBy similarityPRO_0000390816Add
    BLAST
    Chaini2 – 129128Matrix protein p15Sequence AnalysisPRO_0000040916Add
    BLAST
    Chaini130 – 21485RNA-binding phosphoprotein p12Sequence AnalysisPRO_0000040917Add
    BLAST
    Chaini215 – 477263Capsid protein p30Sequence AnalysisPRO_0000040918Add
    BLAST
    Chaini478 – 53760Nucleocapsid protein p10Sequence AnalysisPRO_0000040919Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei191 – 1911Phosphoserine; by hostBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation By similarity.By similarity
    RNA-binding phosphoprotein p12 is phosphorylated on serine residues.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Interactioni

    Subunit structurei

    Capsid protein p30 is a homohexamer, that further associates as homomultimer. The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP11269.
    SMRiP11269. Positions 2-98, 215-346, 351-381, 478-533.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili437 – 47741Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi109 – 1124PTAP/PSAP motif
    Motifi128 – 1325LYPX(n)L motif
    Motifi161 – 1644PPXY motif

    Domaini

    Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which potentially interacts with PDCD6IP By similarity.By similarity

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri501 – 51818CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Family and domain databases

    Gene3Di1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    4.10.60.10. 1 hit.
    InterProiIPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view]
    SMARTiSM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF57756. SSF57756. 1 hit.
    PROSITEiPS50158. ZF_CCHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11269-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGQTVTTPLS LTLEHWGDVQ RIASNQSVEV KKRRRVTFCP AEWPTFDVGW    50
    PQDGTFNLDI ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPSWVKPF 100
    VSPKLSLSPT APILPSGPST QPPPRSALYP ALTPSIKPRP SKPQVLSDNG 150
    GPLIDLLTED PPPYGEQGPS SPDGDGDREE ATYTSEIPAP SPMVSRLRGK 200
    RDPPAADSTT SRAFPLRLGG NGQLQYWPFS SSDLYNWKNN NPSFSEDPGK 250
    LTALIESVLT THQPTWDDCQ QLLGTLLTGE EKQRVLLEAR KAVRGNDGRP 300
    TQLPNEVNSA FPLERPDWDY TTPEGRNHLV LYRQLLLAGL QNAGRSPTNL 350
    AKVKGITQGP NESPSAFLER LKEAYRRYTP YDPEDHGQET SVSMSFIWQS 400
    APDIGRKLER LEDLKSKTLR DLVREAEKIF NKRETPEERE ERFRRETEEN 450
    EERRRAEDEQ REKERDRRRQ REMSKLLATV VTGQRQDRQG GERKRPQLDK 500
    DQCAYCKEKG HWAKDCPKKP RGPRGPRPQT SLLTLDD 537
    Length:537
    Mass (Da):60,784
    Last modified:January 23, 2007 - v3
    Checksum:i312AF7B2BBB4B7FB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti479 – 4791T → S AA sequence (PubMed:6267042)Curated
    Sequence conflicti482 – 4821T → S AA sequence (PubMed:6267042)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03363 Genomic RNA. Translation: AAA46518.1.
    PIRiA26183. FOMVRV.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03363 Genomic RNA. Translation: AAA46518.1 .
    PIRi A26183. FOMVRV.

    3D structure databases

    ProteinModelPortali P11269.
    SMRi P11269. Positions 2-98, 215-346, 351-381, 478-533.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    4.10.60.10. 1 hit.
    InterProi IPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view ]
    SMARTi SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF57756. SSF57756. 1 hit.
    PROSITEi PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    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].
    2. "Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses."
      Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W., Oroszlan S.
      J. Biol. Chem. 256:8400-8406(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 478-505.

    Entry informationi

    Entry nameiGAG_MLVRD
    AccessioniPrimary (citable) accession number: P11269
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3