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P03337

- GAG_FSVGA

UniProt

P03337 - GAG_FSVGA

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Protein
Gag polyprotein
Gene
gag
Organism
Feline sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein feline leukemia oncovirus B)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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.
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.
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
Sitei204 – 2052Cleavage; by viral protease By similarity
Sitei274 – 2752Cleavage; by viral protease By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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 Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein feline leukemia oncovirus B)
Taxonomic identifieri11774 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiFelidae (cat family) [TaxID: 9681]

Subcellular locationi

Chain Gag polyprotein : Virion By similarity. Host cell membrane; Lipid-anchor Reviewed prediction
Chain Matrix protein p15 : Virion Reviewed prediction
Chain Capsid protein p30 : Virion Reviewed prediction

GO - Cellular componenti

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

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 – 425425Gag polyprotein
PRO_0000390800Add
BLAST
Propeptidei1 – 7777Leader peptide Reviewed prediction
PRO_0000040843Add
BLAST
Chaini78 – 204127Matrix protein p15 Reviewed prediction
PRO_0000040844Add
BLAST
Chaini205 – 27470RNA-binding phosphoprotein p12 Reviewed prediction
PRO_0000040845Add
BLAST
Chaini275 – 425151Capsid protein p30 Reviewed prediction
PRO_0000040846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi79 – 791N-myristoyl glycine; by host By 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.

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.

Structurei

3D structure databases

ProteinModelPortaliP03337.
SMRiP03337. Positions 79-175, 275-405.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi195 – 1984PTAP/PSAP motif
Motifi234 – 2374PPXY 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. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. Interacts with PDCD6IP 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.

P03337-1 [UniParc]FASTAAdd to Basket

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MSRASSGTAT GARLFGISSV LGEYRVLIGD EGAGPSRSPS EVSFSVWYRS    50
RAARLVIVCL VASFLVPCLT FLIAETVMGQ TITTPLSLTL DHWSEVRARA 100
HNQGVEVRKK KWITLCEAEW VMMNVGWPRE GTFSLDNISQ VEKKIFAPGP 150
YGHPDQVPYI TTWRSLATDP PSWVRPFLPP PKPPTSLPQP LSPQPSAPLT 200
SSLYPVLPKS DPPKPPVLPP DPSSPLIDLL TEEPPPYPGG HGPPPSGPRT 250
PTASPIASRL RERRENPAEE SQALPLREGP NNRPQYWPFS ASDLYNWKSH 300
NPPFSQDPVA LTNLIESILV THQPTWDDCQ QLLQALLTGE ERQRVLLEAR 350
KQVPGEDGRP TQLPNVIDET FPLTRPNWDF ATPAGREHLR LYRQLLLAGL 400
RGAARRPTNL AQVKQVVQGK EETPA 425
Length:425
Mass (Da):47,009
Last modified:July 21, 1986 - v1
Checksum:i973A137FE537B1A7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02086 Genomic RNA. No translation available.
J02087 Genomic RNA. Translation: AAA43041.1.
PIRiA03934. FOMVGC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02086 Genomic RNA. No translation available.
J02087 Genomic RNA. Translation: AAA43041.1 .
PIRi A03934. FOMVGC.

3D structure databases

ProteinModelPortali P03337.
SMRi P03337. Positions 79-175, 275-405.
ModBasei 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 1-78.
  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 78-425.

Entry informationi

Entry nameiGAG_FSVGA
AccessioniPrimary (citable) accession number: P03337
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 79 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

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