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Q27ID9 (GAG_XMRV6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gag polyprotein

Short name=Pr65gag
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
OrganismXenotropic MuLV-related virus (isolate VP62) (XMRV) [Reference proteome]
Taxonomic identifier373193 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length536 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. 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.

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 – 536535Gag polyprotein By similarity
PRO_0000390845
Chain2 – 129128Matrix protein p15 Potential
PRO_0000390846
Chain130 – 21384RNA-binding phosphoprotein p12 Potential
PRO_0000390847
Chain214 – 476263Capsid protein p30 Potential
PRO_0000390848
Chain477 – 53660Nucleocapsid protein p10 Potential
PRO_0000390849

Regions

Zinc finger500 – 51718CCHC-type
Coiled coil436 – 47641 Potential
Motif109 – 1124PTAP/PSAP motif
Motif128 – 1325LYPX(n)L motif
Motif161 – 1644PPXY motif

Sites

Site129 – 1302Cleavage; by viral protease p14 By similarity
Site213 – 2142Cleavage; by viral protease p14 By similarity
Site476 – 4772Cleavage; by viral protease p14 By similarity

Amino acid modifications

Modified residue1901Phosphoserine; by host By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
Q27ID9 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 63CD1FB1561E0836

FASTA53660,446
        10         20         30         40         50         60 
MGQTVTTPLS LTLQHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW PQDGTFNLGV 

        70         80         90        100        110        120 
ISQVKSRVFC PGPHGHPDQV PYIVTWEALA YDPPPWVKPF VSPKPPPLPT APVLPPGPSA 

       130        140        150        160        170        180 
QPPSRSALYP ALTPSIKSKP PKPQVLPDSG GPLIDLLTED PPPYGAQPSS SARENNEEEA 

       190        200        210        220        230        240 
ATTSEVSPPS PMVSRLRGRR DPPAADSTTS QAFPLRMGGD GQLQYWPFSS SDLYNWKNNN 

       250        260        270        280        290        300 
PSFSEDPGKL TALIESVLIT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGNDGRPT 

       310        320        330        340        350        360 
QLPNEVNAAF PLERPDWDYT TTEGRNHLVL YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN 

       370        380        390        400        410        420 
ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA PDIGRKLERL EDLKSKTLGD 

       430        440        450        460        470        480 
LVREAEKIFN KRETPEEREE RIRREIEEKE ERRRAEDEQR ERERDRRRHR EMSKLLATVV 

       490        500        510        520        530 
IGQRQDRQGG ERRRPQLDKD QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGD 

« Hide

References

[1]"Identification of a novel Gammaretrovirus in prostate tumors of patients homozygous for R462Q RNASEL variant."
Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A., Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H., DeRisi J.L.
PLoS Pathog. 2:E25-E25(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"An infectious retrovirus susceptible to an IFN antiviral pathway from human prostate tumors."
Dong B., Kim S., Hong S., Das Gupta J., Malathi K., Klein E.A., Ganem D., Derisi J.L., Chow S.A., Silverman R.H.
Proc. Natl. Acad. Sci. U.S.A. 104:1655-1660(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ399707 Genomic RNA. Translation: ABD49686.1.
EF185282 Genomic RNA. Translation: ABM47427.1.

3D structure databases

ProteinModelPortalQ27ID9.
SMRQ27ID9. Positions 2-98, 214-345, 350-380, 477-532.
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_XMRV6
AccessionPrimary (citable) accession number: Q27ID9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: April 4, 2006
Last modified: February 19, 2014
This is version 50 of the entry and version 1 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