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P03338

- GAG_FSVST

UniProt

P03338 - GAG_FSVST

Protein

Gag polyprotein

Gene

gag

Organism
Feline sarcoma virus (strain Snyder-Theilen)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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
    Sitei201 – 2022Cleavage; by viral proteaseBy similarity
    Sitei271 – 2722Cleavage; 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
    OrganismiFeline sarcoma virus (strain Snyder-Theilen)
    Taxonomic identifieri11780 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
    Virus hostiFelidae (cat family) [TaxID: 9681]

    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
    Chaini1 – 371371Gag polyproteinPRO_0000390803Add
    BLAST
    Propeptidei1 – 7474Leader peptideSequence AnalysisPRO_0000040856Add
    BLAST
    Chaini75 – 201127Matrix protein p15Sequence AnalysisPRO_0000040857Add
    BLAST
    Chaini202 – 27170RNA-binding phosphoprotein p12Sequence AnalysisPRO_0000040858Add
    BLAST
    Chaini272 – 371100Capsid protein p30Sequence AnalysisPRO_0000040859Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi76 – 761N-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

    ProteinModelPortaliP03338.
    SMRiP03338. Positions 76-172, 272-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi192 – 1954PTAP/PSAP motif
    Motifi200 – 2045LYPX(n)L motif
    Motifi231 – 2344PPXY 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.

    P03338-1 [UniParc]FASTAAdd to Basket

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    MSGASSGTAI GAHLFGVSPE YRVLIGDEGA GPSKSLSEVS FSVWYRSRAA    50
    RLVILCLVAS FLVPCLTFLI AEAVMGQTVT TPLSLTLDHW SEVRARAHNQ 100
    GVEVRKKKWI TLCKAEWVMM NVGWPREGTF SLDNISQVKK KIFAPGPHGH 150
    PDQVPYITTW RSLATDPPSW VRPFLPPPKP PTPLPQPLSP QPSAPLTSSL 200
    YPVVPKPDPP KPPVLPPDPS SPLIDLLTEE PPPYPGGHGP PPSGPRTPAA 250
    SPIVSRLRER RENPAEESQA LPLREGPNNR PQYWPFSASD LYNWKSHNPP 300
    FSQDPVALTN LIESILVTHQ PTWDDCQQLL QALLTGEERQ RVLLEARKQV 350
    PGEDGRPTQL PNVIDETFPL T 371
    Length:371
    Mass (Da):40,830
    Last modified:July 21, 1986 - v1
    Checksum:i5842DCC63483F420
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02088 Genomic RNA. Translation: AAA43046.2. Different termination.
    PIRiA03935. FOMVCS.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02088 Genomic RNA. Translation: AAA43046.2 . Different termination.
    PIRi A03935. FOMVCS.

    3D structure databases

    ProteinModelPortali P03338.
    SMRi P03338. Positions 76-172, 272-370.
    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. "Nucleotide sequences of feline sarcoma virus long terminal repeats and 5' leaders show extensive homology to those of other mammalian retroviruses."
      Hampe A., Gobet M., Even J., Sherr C.J., Galibert F.
      J. Virol. 45:466-472(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-75.
    2. "Nucleotide sequences of feline retroviral oncogenes (v-fes) provide evidence for a family of tyrosine-specific protein kinase genes."
      Hampe A., Laprevotte I., Galibert F., Fedele L.A., Sherr C.J.
      Cell 30:775-785(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 75-371.

    Entry informationi

    Entry nameiGAG_FSVST
    AccessioniPrimary (citable) accession number: P03338
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein is synthesized as a Gag-Fes polyprotein.

    External Data

    Dasty 3