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P26807 (GAG_MLVF5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. 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
  2. RNA-binding phosphoprotein p12
    Alternative name(s):
    pp12
  3. Capsid protein p30
  4. Nucleocapsid protein p10
Gene names
Name:gag
OrganismFriend murine leukemia virus (isolate 57) (FrMLV) [Complete proteome]
Taxonomic identifier11796 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length539 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. Note: These locations are probably linked to virus assembly sites. Ref.2

Matrix protein p15: Virion Potential Ref.2.

Capsid protein p30: Virion Potential Ref.2.

Nucleocapsid protein p10: Virion Potential Ref.2.

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 – 539538Gag polyprotein By similarity
PRO_0000390811
Chain2 – 132131Matrix protein p15 Potential
PRO_0000040896
Chain133 – 21684RNA-binding phosphoprotein p12 Potential
PRO_0000040897
Chain217 – 479263Capsid protein p30 Potential
PRO_0000040898
Chain480 – 53960Nucleocapsid protein p10 Potential
PRO_0000040899

Regions

Zinc finger503 – 52018CCHC-type
Coiled coil439 – 47941 Potential
Motif112 – 1154PTAP/PSAP motif
Motif131 – 1355LYPX(n)L motif
Motif163 – 1664PPXY motif

Sites

Site132 – 1332Cleavage; by viral protease p14 By similarity
Site216 – 2172Cleavage; by viral protease p14 By similarity
Site479 – 4802Cleavage; by viral protease p14 By similarity

Amino acid modifications

Modified residue1931Phosphoserine; by host By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Sequences

Sequence LengthMass (Da)Tools
P26807 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F1565E8979CDE96A

FASTA53961,038
        10         20         30         40         50         60 
MGQTVTTPLS LTLDHWKDVE RTAHNQSVEI RKRRWVTLCS AEWPTFNVGW PRDGTFNPDI 

        70         80         90        100        110        120 
ITQVKIKVFS SGPHGHPDQV PYIVTWEALA ADPPPWVKPF VHPKPPPLLL PPSAPSLPPE 

       130        140        150        160        170        180 
PPFPTPPQSS LYPALTSPLN TKPRPQVLPD SGGPLIDLLT EDPPPYRDPG PSSSDGNGGS 

       190        200        210        220        230        240 
GEVAPTEGAP DSSPMVSRLR GRREPPVADS TTSQAFPLRQ GGNGQFQYWP FSSSDLYNWK 

       250        260        270        280        290        300 
NNNPSFSEDP AKLTALIESV LLTHQPTWDD CQQLLGTLLT GEEKQRVLLE ARKAVRGEDG 

       310        320        330        340        350        360 
RPTQLPNDIN DAFPLERPDW DYNTQRGRNH LVHYRQLLLA GLQNAGRSPT NLAKVKGITQ 

       370        380        390        400        410        420 
GPNESPSAFL ERLKEAYRRY TPYDPEDPGQ ETNVAMSFIW QSAPDIGRKL ERLEDLKSKT 

       430        440        450        460        470        480 
LGDLVREAEK IFNKRETPEE REERIRRETE EKEERRRAED EQREKERDRR RHREMSKLLA 

       490        500        510        520        530 
TVISGQRQDR QGGERRRPQL DHDQCAYCKE KGHWARDCPK KPRGPRGPRP QASLLTLDD 

« Hide

References

[1]Friedrich R.W., Koch W., von Maydell-Livonius U., Schrewe H., Zimmermann W.
Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Visualization of retroviral replication in living cells reveals budding into multivesicular bodies."
Sherer N.M., Lehmann M.J., Jimenez-Soto L.F., Ingmundson A., Horner S.M., Cicchetti G., Allen P.G., Pypaert M., Cunningham J.M., Mothes W.
Traffic 4:785-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02794 Genomic RNA. Translation: CAA26560.1.

3D structure databases

ProteinModelPortalP26807.
SMRP26807. Positions 2-98, 217-347, 353-383, 480-535.
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_MLVF5
AccessionPrimary (citable) accession number: P26807
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 97 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