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P29175 (GAG_MSVFR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 77. 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
OrganismFBR murine osteosarcoma virus (FBR-MSV) (Finkel-Biskis-Reilly murine osteosarcoma virus)
Taxonomic identifier11806 [NCBI]
Taxonomic lineageViruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › unclassified Gammaretrovirus ›
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length310 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-Fos-Fox polyprotein.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 310309Gag polyprotein
PRO_0000390817
Chain2 – 129128Matrix protein p15 Potential
PRO_0000040946
Chain130 – 21485RNA-binding phosphoprotein p12 Potential
PRO_0000040947
Chain215 – 31096Capsid protein p30 Potential
PRO_0000040948

Regions

Motif109 – 1124PTAP/PSAP motif
Motif128 – 1325LYPX(n)L motif
Motif161 – 1644PPXY motif

Sites

Site129 – 1302Cleavage; by viral protease By similarity
Site214 – 2152Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P29175 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F5713E16959C5F8C

FASTA31033,849
        10         20         30         40         50         60 
MGQTVTTPLS LTLEHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFDVGW PQDGTFNLDI 

        70         80         90        100        110        120 
ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF VSPKLSPSPT APILPSGPST 

       130        140        150        160        170        180 
QPPPRSALYP ALTPSIKPRP SKPQVLSDDG GPLIDLLTED PPPYGEQGPS SSDGDGDREE 

       190        200        210        220        230        240 
ATSTSEIPAP SPMVSRLRGK RDPPAADSTT SRAFPLRLGG NGQKNNNPSF SEDPGKLTAL 

       250        260        270        280        290        300 
IESVLTTHQP TWDDCQQLLG TLLTGEEKQR VLLEARKAVR GNDGRPTQMP NEVNAAFPLE 

       310 
RPDWDYTTPE

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References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		K02712 Genomic DNA. Translation: AAA46573.1. Different termination.
PIRFOMVFB. A23244.

3D structure databases

ProteinModelPortalP29175.
SMRP29175. Positions 2-98, 215-310.
ModBaseSearch...

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]
SUPFAMSSF47943. Retrov_capsid_N. 1 hit.
SSF47836. Retrovir_matrix. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGAG_MSVFR
AccessionPrimary (citable) accession number: P29175
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program
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