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P32594 (GAG_MSVMT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. 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
OrganismMoloney murine sarcoma virus (strain ts110) (MoMSV)
Taxonomic identifier31691 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length468 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.

Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization 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 probably translated as a Gag-Mos polyprotein.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 468467Gag polyprotein
PRO_0000390819
Chain2 – 131130Matrix protein p15 Potential
PRO_0000040953
Chain132 – 21584RNA-binding phosphoprotein p12 Potential
PRO_0000040954
Chain216 – 468253Capsid protein p30 Potential
PRO_0000040955

Regions

Motif111 – 1144PTAP/PSAP motif
Motif130 – 1345LYPX(n)L motif
Motif162 – 1654PPXY motif

Sites

Site131 – 1322Cleavage; by viral protease By similarity
Site215 – 2162Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P32594 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AF4F795F5D69824F

FASTA46852,681
        10         20         30         40         50         60 
MGQTVTTPLS LTLDHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL 

        70         80         90        100        110        120 
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLL PSAPSLPLEP 

       130        140        150        160        170        180 
PLSTPPQSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGDSG 

       190        200        210        220        230        240 
EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRTG GNGQLQYWPF SSSDLYNWKS 

       250        260        270        280        290        300 
NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR 

       310        320        330        340        350        360 
PTQLPNEVDA AFPLERPDWE YTTQAGRNHL VHYRQLLIAG LQNAGRSPTN LAKVKGITQG 

       370        380        390        400        410        420 
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLRNKTL 

       430        440        450        460 
GDLVREAERI FNKRETPEER EERIRREREE KEERHAPKLP WLFLIISP 

« Hide

References

[1]"Moloney murine sarcoma virus MuSVts110 DNA: cloning, nucleotide sequence, and gene expression."
Huai L., Chiocca S.M., Gilbreth M.A., Ainsworth J.R., Bishop L.A., Murphy E.C. Jr.
J. Virol. 66:5329-5337(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96854 Genomic DNA. No translation available.
PIRFOMVMU. A42745.

3D structure databases

ProteinModelPortalP32594.
SMRP32594. Positions 2-98, 216-346, 352-382.
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_MSVMT
AccessionPrimary (citable) accession number: P32594
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program