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P21416 (GAG_GALV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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
OrganismGibbon ape leukemia virus (GALV) [Complete proteome]
Taxonomic identifier11840 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostHylobatidae (gibbons) [TaxID: 9577]

Protein attributes

Sequence length520 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.

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 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.

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 – 520519Gag polyprotein
PRO_0000390804
Chain2 – 125124Matrix protein p15 Potential
PRO_0000040863
Chain126 – 19570RNA-binding phosphoprotein p12 Potential
PRO_0000040864
Chain196 – 454259Capsid protein p30 Potential
PRO_0000040865
Chain455 – 52066Nucleocapsid protein p10 Potential
PRO_0000040866

Regions

Zinc finger489 – 50618CCHC-type
Motif116 – 1194PTAP/PSAP motif
Motif139 – 1424PPXY motif

Sites

Site125 – 1262Cleavage; by viral protease By similarity
Site195 – 1962Cleavage; by viral protease By similarity
Site454 – 4552Cleavage; by viral protease By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P21416 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 77FE4760E61D1E2D

FASTA52058,110
        10         20         30         40         50         60 
MGQDNSTPIS LTLNHWRDVR TRAHNLSVEI KKGKWQTFCS SEWPTFGVGW PPEGTFNLSV 

        70         80         90        100        110        120 
IFAVKKIVFQ ENGGHPDQVP YIVVWQDLAQ NPPPWVPASA KVAVVSDTRR PVAGRPSAPP 

       130        140        150        160        170        180 
RPPIYPATDD LLLLSEPTPP PYPAALPPPL APQAIGPPSG QMPDSSDPEG PAAGTRSRRA 

       190        200        210        220        230        240 
RSPADNSGPD STVILPLRAI GPPAEPNGLV PLQYWPFSSA DLYNWKSNHP SFSENPAGLT 

       250        260        270        280        290        300 
GLLESLMFSH QPTWDDCQQL LQILFTTEER ERILLEARKN VLGDNGAPTQ LENLINEAFP 

       310        320        330        340        350        360 
LNRPHWDYNT AAGRERLLVY RRTLVAGLKG AARRPTNLAK VREVLQGPAE PPSVFLERLM 

       370        380        390        400        410        420 
EAYRRYTPFD PSSEGQQAAV AMAFIGQSAP DIKKKLQRLE GLQDYSLQDL VKEAEKVYHK 

       430        440        450        460        470        480 
RETEEERQER EKKEAEEKER RRDRPKKKNL TKILAAVVSR EGSTGRQTGN LSNQAKKTPR 

       490        500        510        520 
DGRPPLDKDQ CAYCKEKGHW ARECPRKKHV REAKVLALDN 

« Hide

References

[1]"Genetic organization of gibbon ape leukemia virus."
Delassus S., Sonigo P., Wain-Hobson S.
Virology 173:205-213(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26927 Genomic RNA. Translation: AAA46809.1.
PIRFOLJGL. A32595.
RefSeqNP_056789.1. NC_001885.2.

3D structure databases

ProteinModelPortalP21416.
SMRP21416. Positions 5-98, 212-333, 338-369, 481-508.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1491894.

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.
IPR003036. Gag_P30.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF01140. Gag_MA. 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_GALV
AccessionPrimary (citable) accession number: P21416
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 88 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