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P26806 (GAG_MLVFF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 106. 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
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 FB29) (FrMLV) [Complete proteome]
Taxonomic identifier11797 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 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 – 538537Gag polyprotein By similarity
PRO_0000390812
Chain2 – 131130Matrix protein p15 Potential
PRO_0000040900
Chain132 – 21584RNA-binding phosphoprotein p12 Potential
PRO_0000040901
Chain216 – 478263Capsid protein p30 Potential
PRO_0000040902
Chain479 – 53860Nucleocapsid protein p10 Potential
PRO_0000040903

Regions

Zinc finger502 – 51918CCHC-type
Coiled coil438 – 47841 Potential
Motif111 – 1144PTAP/PSAP motif
Motif130 – 1345LYPX(n)L motif
Motif162 – 1654PPXY motif

Sites

Site131 – 1322Cleavage; by viral protease p14 By similarity
Site215 – 2162Cleavage; by viral protease p14 By similarity
Site478 – 4792Cleavage; by viral protease p14 By similarity

Amino acid modifications

Modified residue1921Phosphoserine; by host By similarity
Lipidation21N-myristoyl glycine; by host By similarity

Experimental info

Sequence conflict5011H → R AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P26806 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2E652DDB9E0D4A3C

FASTA53860,929
        10         20         30         40         50         60 
MGQAVTTPLS LTLDHWKDVE RTAHNLSVEV RKRRWVTFCS AEWPTFNVGW PRDGTFNPDI 

        70         80         90        100        110        120 
ITQVKIKVFS PGPHGHPDQV PYIVTWEAIA VDPPPWVRPF VHPKPPLSLP PSAPSLPPEP 

       130        140        150        160        170        180 
PLSTPPQSSL YPALTSPLNT KPRPQVLPDS GGPLIDLLTE DPPPYRDPGP PSPDGNGDSG 

       190        200        210        220        230        240 
EVAPTEGAPD PSPMVSRLRG RKEPPVADST TSQAFPLRLG GNGQYQYWPF SSSDLYNWKN 

       250        260        270        280        290        300 
NNPSFSEDPA KLTALIESVL LTHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGEDGR 

       310        320        330        340        350        360 
PTQLPNDIND AFPLERPDWD YNTQRGRNHL VHYRQLLLAG LQNAGRSPTN LAKVKGITQG 

       370        380        390        400        410        420 
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVAMSFIWQ SAPDIGRKLE RLEDLKSKTL 

       430        440        450        460        470        480 
GDLVREAEKI FNKRETPEER EERIRRETEE KEERRRAEDV QREKERDRRR HREMSKLLAT 

       490        500        510        520        530 
VVSGQRQDRQ GGERRRPQLD HDQCAYCKEK GHWARDCPKK PRGPRGPRPQ ASLLTLDD 

« Hide

References

[1]"Complete nucleotide sequence of Friend murine leukemia virus, strain FB29."
Perryman S., Nishio J., Chesebro B.
Nucleic Acids Res. 19:6950-6950(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses."
Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W., Oroszlan S.
J. Biol. Chem. 256:8400-8406(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 479-512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z11128 Genomic DNA. Translation: CAA77478.1.
PIRS70394.
RefSeqNP_040332.1. NC_001362.1.

3D structure databases

ProteinModelPortalP26806.
SMRP26806. Positions 2-98, 216-346, 352-382, 479-534.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1491876.

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_MLVFF
AccessionPrimary (citable) accession number: P26806
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 106 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