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P29167 (GAG_MLVBM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 4 chains:

  1. Matrix protein p15
    Short name=MA
  2. RNA-binding phosphoprotein p12
    Alternative name(s):
    pp12
  3. Capsid protein p30
    Short name=CA
  4. Nucleocapsid protein p10
    Short name=NC-gag
Gene names
Name:gag
OrganismMurine leukemia virus (strain BM5 eco)
Taxonomic identifier31687 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length537 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 UCUG 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. Host late endosome membrane; Lipid-anchor Potential. Host endosomehost multivesicular body By similarity. Note: These locations are probably linked to virus assembly sites By similarity.

Matrix protein p15: Virion Potential.

Capsid protein p30: Virion Potential.

Nucleocapsid protein p10: 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 motif 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.

RNA-binding phosphoprotein p12 is phosphorylated on serine residues By similarity.

Sequence similarities

Contains 1 CCHC-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 537536Gag polyprotein By similarity
PRO_0000390807
Chain2 – 129128Matrix protein p15 Potential
PRO_0000040880
Chain130 – 21485RNA-binding phosphoprotein p12 Potential
PRO_0000040881
Chain215 – 477263Capsid protein p30 Potential
PRO_0000040882
Chain478 – 53760Nucleocapsid protein p10 Potential
PRO_0000040883

Regions

Zinc finger501 – 51818CCHC-type
Coiled coil448 – 47023 Potential
Motif109 – 1124PTAP/PSAP motif
Motif128 – 1325LYPX(n)L motif
Motif161 – 1644PPXY motif

Sites

Site129 – 1302Cleavage; by viral protease p14 By similarity
Site214 – 2152Cleavage; by viral protease p14 By similarity
Site477 – 4782Cleavage; by viral protease p14 By similarity

Amino acid modifications

Modified residue1911Phosphoserine; by host By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P29167 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: ABD2E70299BFFD64

FASTA53760,423
        10         20         30         40         50         60 
MGQTVTTPLS LTLEHWGDVQ RIASNQSVGV KKRRWVTFCS AEWPTFGVGW PQDGTFNLDI 

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

       130        140        150        160        170        180 
QPPPRSALYP AFTPSIKPRP SKPQVLSDDG GPLIDLLTED PPPYGEQGPS SPDGDGDREE 

       190        200        210        220        230        240 
ATSTSEIPAP SPMVSRLRGK RDPPAADSTT SRAFPLRLGG NGQLQYWPFS SSDLYNWKNN 

       250        260        270        280        290        300 
NPSFSEDPGK LTALIESVLT THQPTWDDCQ QLLGTLLTGE EKQRVLLEAR KAVRGNDGRP 

       310        320        330        340        350        360 
TQLPNEVNSA FPLERPDWDY TTPEGRNHLV LYRQLLLAGL QNAGRSPTNL AKVKGITQGP 

       370        380        390        400        410        420 
NESPSAFLER LKEAYRRYTP YDPEDPGQET NVSMSFIWQS APAIGRKLER LEDLKSKTLG 

       430        440        450        460        470        480 
DLVREAEKIF NKRETPEERE ERIRRETEEK EERRRAGDEQ REKERDRRRQ REMSKLLATV 

       490        500        510        520        530 
VTGQRQDRQG GERRRPQLDK DQCAYCKEKG HWAKDCPKKP RGPRGPRPQT SLLTLDD 

« Hide

References

[1]"Characteristics and contributions of defective, ecotropic, and mink cell focus-inducing viruses involved in a retrovirus-induced immunodeficiency syndrome of mice."
Chattopadhyay S.K., Sengupta D.N., Fredrickson T.N., Morse H.C. III, Hartley J.W.
J. Virol. 65:4232-4241(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64095 Genomic DNA. Translation: AAA46510.1.
PIRFOMVMB. A40416.

3D structure databases

ProteinModelPortalP29167.
SMRP29167. Positions 2-98, 215-346, 351-381, 478-533.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.150.180. 1 hit.
1.10.375.10. 1 hit.
4.10.60.10. 1 hit.
InterProIPR000840. G_retro_matrix_N.
IPR002079. Gag_p12.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF01140. Gag_MA. 1 hit.
PF01141. Gag_p12. 1 hit.
PF02093. Gag_p30. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTSM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMSSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEPS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGAG_MLVBM
AccessionPrimary (citable) accession number: P29167
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families