P11269 (GAG_MLVRD) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 99. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Radiation murine leukemia virus [Complete proteome]|
|Taxonomic identifier||11787 [NCBI]|
|Taxonomic lineage||Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › Murine leukemia virus ›|
|Virus host||Mus musculus (Mouse) [TaxID: 10090]|
|Sequence length||537 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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.
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.
Gag polyprotein: Virion By similarity. Host cell membrane; Lipid-anchor Potential. Host late endosome membrane; Lipid-anchor Potential. Host endosome › host multivesicular body By similarity. Note: These locations are probably linked to virus assembly sites By similarity.
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.
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.
Contains 1 CCHC-type zinc finger.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed; by host By similarity|
|Chain||2 – 537||536||Gag polyprotein By similarity||PRO_0000390816|
|Chain||2 – 129||128||Matrix protein p15 Potential||PRO_0000040916|
|Chain||130 – 214||85||RNA-binding phosphoprotein p12 Potential||PRO_0000040917|
|Chain||215 – 477||263||Capsid protein p30 Potential||PRO_0000040918|
|Chain||478 – 537||60||Nucleocapsid protein p10 Potential||PRO_0000040919|
|Zinc finger||501 – 518||18||CCHC-type|
|Coiled coil||437 – 477||41||Potential|
|Motif||109 – 112||4||PTAP/PSAP motif|
|Motif||128 – 132||5||LYPX(n)L motif|
|Motif||161 – 164||4||PPXY motif|
|Site||129 – 130||2||Cleavage; by viral protease p14 By similarity|
|Site||214 – 215||2||Cleavage; by viral protease p14 By similarity|
|Site||477 – 478||2||Cleavage; by viral protease p14 By similarity|
Amino acid modifications
|Modified residue||191||1||Phosphoserine; by host By similarity|
|Lipidation||2||1||N-myristoyl glycine; by host By similarity|
|Sequence conflict||479||1||T → S AA sequence Ref.2|
|Sequence conflict||482||1||T → S AA sequence Ref.2|
|||"Nucleotide sequence of a radiation leukemia virus genome."|
Merregaert J., Janowski M., Reddy E.P.
Virology 158:88-102(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"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 478-505.
|K03363 Genomic RNA. Translation: AAA46518.1.|
|PIR||FOMVRV. A26183. |
3D structure databases
|SMR||P11269. Positions 2-98, 215-346, 351-381, 478-533. |
Protocols and materials databases
Family and domain databases
|Gene3D||184.108.40.206. 1 hit. |
1.10.375.10. 1 hit.
220.127.116.11. 1 hit.
|InterPro||IPR000840. G_retro_matrix_N. |
|Pfam||PF01140. Gag_MA. 1 hit. |
PF01141. Gag_p12. 1 hit.
PF02093. Gag_p30. 1 hit.
PF00098. zf-CCHC. 1 hit.
|SMART||SM00343. ZnF_C2HC. 1 hit. |
|SUPFAM||SSF47836. SSF47836. 1 hit. |
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
|PROSITE||PS50158. ZF_CCHC. 1 hit. |
|Accession||Primary (citable) accession number: P11269|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families