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P29175

- GAG_MSVFR

UniProt

P29175 - GAG_MSVFR

Protein

Gag polyprotein

Gene

gag

Organism
FBR murine osteosarcoma virus (FBR-MSV) (Finkel-Biskis-Reilly murine osteosarcoma virus)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei129 – 1302Cleavage; by viral proteaseBy similarity
    Sitei214 – 2152Cleavage; by viral proteaseBy similarity

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW
    2. structural constituent of virion Source: UniProtKB-KW

    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

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gag polyprotein
    Alternative name(s):
    Core polyprotein
    Cleaved into the following 3 chains:
    Matrix protein p15
    Short name:
    MA
    Alternative name(s):
    pp12
    Capsid protein p30
    Short name:
    CA
    Gene namesi
    Name:gag
    OrganismiFBR murine osteosarcoma virus (FBR-MSV) (Finkel-Biskis-Reilly murine osteosarcoma virus)
    Taxonomic identifieri11806 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]

    Subcellular locationi

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-KW
    3. viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 310309Gag polyproteinPRO_0000390817Add
    BLAST
    Chaini2 – 129128Matrix protein p15Sequence AnalysisPRO_0000040946Add
    BLAST
    Chaini130 – 21485RNA-binding phosphoprotein p12Sequence AnalysisPRO_0000040947Add
    BLAST
    Chaini215 – 31096Capsid protein p30Sequence AnalysisPRO_0000040948Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; 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

    Keywords - PTMi

    Lipoprotein, Myristate

    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

    ProteinModelPortaliP29175.
    SMRiP29175. Positions 2-98, 215-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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 which potentially interacts with PDCD6IP By similarity.By similarity

    Family and domain databases

    Gene3Di1.10.150.180. 1 hit.
    1.10.375.10. 1 hit.
    InterProiIPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    [Graphical view]
    PfamiPF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    [Graphical view]
    SUPFAMiSSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P29175-1 [UniParc]FASTAAdd to Basket

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    MGQTVTTPLS LTLEHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFDVGW    50
    PQDGTFNLDI ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF 100
    VSPKLSPSPT APILPSGPST QPPPRSALYP ALTPSIKPRP SKPQVLSDDG 150
    GPLIDLLTED PPPYGEQGPS SSDGDGDREE ATSTSEIPAP SPMVSRLRGK 200
    RDPPAADSTT SRAFPLRLGG NGQKNNNPSF SEDPGKLTAL IESVLTTHQP 250
    TWDDCQQLLG TLLTGEEKQR VLLEARKAVR GNDGRPTQMP NEVNAAFPLE 300
    RPDWDYTTPE 310
    Length:310
    Mass (Da):33,849
    Last modified:January 23, 2007 - v3
    Checksum:iF5713E16959C5F8C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02712 Genomic DNA. Translation: AAA46573.1. Different termination.
    PIRiA23244. FOMVFB.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02712 Genomic DNA. Translation: AAA46573.1 . Different termination.
    PIRi A23244. FOMVFB.

    3D structure databases

    ProteinModelPortali P29175.
    SMRi P29175. Positions 2-98, 215-310.
    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.
    InterProi IPR000840. G_retro_matrix_N.
    IPR002079. Gag_p12.
    IPR003036. Gag_P30.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    [Graphical view ]
    Pfami PF01140. Gag_MA. 1 hit.
    PF01141. Gag_p12. 1 hit.
    PF02093. Gag_p30. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "FBR murine osteosarcoma virus. II. Nucleotide sequence of the provirus reveals that the genome contains sequences acquired from two cellular genes."
      van Beveren C., Enami S., Curran T., Verma I.M.
      Virology 135:229-243(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiGAG_MSVFR
    AccessioniPrimary (citable) accession number: P29175
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 81 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein is synthesized as a Gag-Fos-Fox polyprotein.

    External Data

    Dasty 3