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P03338 (GAG_FSVST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gag polyprotein
Alternative name(s):
Core polyprotein

Cleaved into the following 3 chains:

  1. Matrix protein p15
    Short name=MA
  2. RNA-binding phosphoprotein p12
    Alternative name(s):
    pp12
  3. Capsid protein p30
    Short name=CA
Gene names
Name:gag
OrganismFeline sarcoma virus (strain Snyder-Theilen)
Taxonomic identifier11780 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostFelidae (cat family) [TaxID: 9681]

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Gag polyprotein: Virion By similarity. Host cell membrane; Lipid-anchor Potential.

Matrix protein p15: Virion Potential.

Capsid protein p30: Virion Potential.

Domain

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.

Post-translational modification

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.

Miscellaneous

This protein is synthesized as a Gag-Fes polyprotein.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371Gag polyprotein
PRO_0000390803
Propeptide1 – 7474Leader peptide Potential
PRO_0000040856
Chain75 – 201127Matrix protein p15 Potential
PRO_0000040857
Chain202 – 27170RNA-binding phosphoprotein p12 Potential
PRO_0000040858
Chain272 – 371100Capsid protein p30 Potential
PRO_0000040859

Regions

Motif192 – 1954PTAP/PSAP motif
Motif200 – 2045LYPX(n)L motif
Motif231 – 2344PPXY motif

Sites

Site201 – 2022Cleavage; by viral protease By similarity
Site271 – 2722Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation761N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P03338 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 5842DCC63483F420

FASTA37140,830
        10         20         30         40         50         60 
MSGASSGTAI GAHLFGVSPE YRVLIGDEGA GPSKSLSEVS FSVWYRSRAA RLVILCLVAS 

        70         80         90        100        110        120 
FLVPCLTFLI AEAVMGQTVT TPLSLTLDHW SEVRARAHNQ GVEVRKKKWI TLCKAEWVMM 

       130        140        150        160        170        180 
NVGWPREGTF SLDNISQVKK KIFAPGPHGH PDQVPYITTW RSLATDPPSW VRPFLPPPKP 

       190        200        210        220        230        240 
PTPLPQPLSP QPSAPLTSSL YPVVPKPDPP KPPVLPPDPS SPLIDLLTEE PPPYPGGHGP 

       250        260        270        280        290        300 
PPSGPRTPAA SPIVSRLRER RENPAEESQA LPLREGPNNR PQYWPFSASD LYNWKSHNPP 

       310        320        330        340        350        360 
FSQDPVALTN LIESILVTHQ PTWDDCQQLL QALLTGEERQ RVLLEARKQV PGEDGRPTQL 

       370 
PNVIDETFPL T 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02088 Genomic RNA. Translation: AAA43046.2. Different termination.
PIRFOMVCS. A03935.

3D structure databases

ProteinModelPortalP03338.
SMRP03338. Positions 76-172, 272-370.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.150.180. 1 hit.
1.10.375.10. 1 hit.
InterProIPR000840. G_retro_matrix_N.
IPR002079. Gag_p12.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
[Graphical view]
PfamPF01140. Gag_MA. 1 hit.
PF01141. Gag_p12. 1 hit.
PF02093. Gag_p30. 1 hit.
[Graphical view]
SUPFAMSSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGAG_FSVST
AccessionPrimary (citable) accession number: P03338
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program