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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: Annotation score: 3 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).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
Sitei204 – 2052Cleavage; by viral proteaseBy similarity
Sitei274 – 2752Cleavage; 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
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

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 polyproteinPRO_0000390800Add
BLAST
Propeptidei1 – 7777Leader peptideSequence AnalysisPRO_0000040843Add
BLAST
Chaini78 – 204127Matrix protein p15Sequence AnalysisPRO_0000040844Add
BLAST
Chaini205 – 27470RNA-binding phosphoprotein p12Sequence AnalysisPRO_0000040845Add
BLAST
Chaini275 – 425151Capsid protein p30Sequence AnalysisPRO_0000040846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi79 – 791N-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

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

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).By similarity

Family and domain databases

Gene3Di1.10.150.180. 1 hit.
1.10.375.10. 1 hit.
InterProiIPR000840. G_retro_matrix.
IPR002079. Gag_p12.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
[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

« Hide

        10         20         30         40         50
MSRASSGTAT GARLFGISSV LGEYRVLIGD EGAGPSRSPS EVSFSVWYRS
60 70 80 90 100
RAARLVIVCL VASFLVPCLT FLIAETVMGQ TITTPLSLTL DHWSEVRARA
110 120 130 140 150
HNQGVEVRKK KWITLCEAEW VMMNVGWPRE GTFSLDNISQ VEKKIFAPGP
160 170 180 190 200
YGHPDQVPYI TTWRSLATDP PSWVRPFLPP PKPPTSLPQP LSPQPSAPLT
210 220 230 240 250
SSLYPVLPKS DPPKPPVLPP DPSSPLIDLL TEEPPPYPGG HGPPPSGPRT
260 270 280 290 300
PTASPIASRL RERRENPAEE SQALPLREGP NNRPQYWPFS ASDLYNWKSH
310 320 330 340 350
NPPFSQDPVA LTNLIESILV THQPTWDDCQ QLLQALLTGE ERQRVLLEAR
360 370 380 390 400
KQVPGEDGRP TQLPNVIDET FPLTRPNWDF ATPAGREHLR LYRQLLLAGL
410 420
RGAARRPTNL AQVKQVVQGK EETPA
Length:425
Mass (Da):47,009
Last modified:July 21, 1986 - v1
Checksum:i973A137FE537B1A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02086 Genomic RNA. No translation available.
J02087 Genomic RNA. Translation: AAA43041.1.
PIRiA03934. FOMVGC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02086 Genomic RNA. No translation available.
J02087 Genomic RNA. Translation: AAA43041.1.
PIRiA03934. FOMVGC.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.150.180. 1 hit.
1.10.375.10. 1 hit.
InterProiIPR000840. G_retro_matrix.
IPR002079. Gag_p12.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
[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.
ProtoNetiSearch...

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(1982) [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(1981) [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: January 7, 2015
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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.