P26805 · GAG_MLVFP
- ProteinGag polyprotein
- Genegag
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids538 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
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 links the viral protein to the host ESCRT pathway and facilitates release.
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 pre-integration complex.
RNA-binding phosphoprotein p12
Constituent of the pre-integration complex (PIC) which tethers the latter to mitotic chromosomes.
Capsid protein p30
Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.
Nucleocapsid protein p10-Gag
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.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 131-132 | Cleavage; by viral protease | ||||
Sequence: YP | ||||||
Site | 215-216 | Cleavage; by viral protease | ||||
Sequence: FP | ||||||
Site | 478-479 | Cleavage; by viral protease | ||||
Sequence: LA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell plasma membrane | |
Cellular Component | host multivesicular body | |
Cellular Component | membrane | |
Cellular Component | viral nucleocapsid | |
Molecular Function | RNA binding | |
Molecular Function | structural constituent of virion | |
Molecular Function | zinc ion binding | |
Biological Process | viral budding via host ESCRT complex |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGag polyprotein
- Alternative names
- Cleaved into 4 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Pararnavirae > Artverviricota > Revtraviricetes > Ortervirales > Retroviridae > Orthoretrovirinae > Gammaretrovirus > Murine leukemia virus
- Virus hosts
Accessions
- Primary accessionP26805
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Gag polyprotein
Host cell membrane ; Lipid-anchor
Matrix protein p15
Capsid protein p30
Nucleocapsid protein p10-Gag
RNA-binding phosphoprotein p12
Note: Localizes to the host cytoplasm early in infection and binds to the mitotic chromosomes later on.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; by host | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine; by host | ||||
Sequence: G | ||||||
Chain | PRO_0000040904 | 2-131 | Matrix protein p15 | |||
Sequence: GQTATTPLSLTLDHWKDVERTAHNQSVEVRKRRWVTFCSAEWPTFNVGWPRDGTFNPDIITQVKIKVFSPGPHGHPDQVPYIVTWEALAVDPPPWVKPFVHPKPPLLLPPSAPSLPPEPPLSTPPQSSLY | ||||||
Chain | PRO_0000390813 | 2-538 | Gag polyprotein | |||
Sequence: GQTATTPLSLTLDHWKDVERTAHNQSVEVRKRRWVTFCSAEWPTFNVGWPRDGTFNPDIITQVKIKVFSPGPHGHPDQVPYIVTWEALAVDPPPWVKPFVHPKPPLLLPPSAPSLPPEPPLSTPPQSSLYPALTSPLNTKPRPQVLPDSGGPLIDLLTEDPPPYRDPGPPSPDGKGDSGEVAPTEGAPDSSPMVSRLRGRREPPVADSTTSQAFPLRLGGNGQFQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLLTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGEDGRPTQLPNDINDAFPLERPDWDYNTQRGRNHLVHYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKNKTLGDLVREAEKIFNKRETPEEREERVRRETEEKEERRRAEDERREKERDRRRHREMSKLLATVVSGQRQDRQGGERRRPQLDHDQCAYCKEKGHWARDCPKKPRGPRGPRPQASLLTLDD | ||||||
Chain | PRO_0000040905 | 132-215 | RNA-binding phosphoprotein p12 | |||
Sequence: PALTSPLNTKPRPQVLPDSGGPLIDLLTEDPPPYRDPGPPSPDGKGDSGEVAPTEGAPDSSPMVSRLRGRREPPVADSTTSQAF | ||||||
Modified residue | 192 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Chain | PRO_0000040906 | 216-478 | Capsid protein p30 | |||
Sequence: PLRLGGNGQFQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLLTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGEDGRPTQLPNDINDAFPLERPDWDYNTQRGRNHLVHYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKNKTLGDLVREAEKIFNKRETPEEREERVRRETEEKEERRRAEDERREKERDRRRHREMSKLL | ||||||
Chain | PRO_0000040907 | 479-538 | Nucleocapsid protein p10-Gag | |||
Sequence: ATVVSGQRQDRQGGERRRPQLDHDQCAYCKEKGHWARDCPKKPRGPRGPRPQASLLTLDD |
Post-translational modification
Gag polyprotein
Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination.
Gag polyprotein
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.
Capsid protein p30
Sumoylated; required for virus replication.
RNA-binding phosphoprotein p12 is phosphorylated on serine residues.
Keywords
- PTM
Interaction
Subunit
Capsid protein p30
Homohexamer; further associates as homomultimer (By similarity).
The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers. Interacts with mouse UBE2I and mouse PIAS4
The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers. Interacts with mouse UBE2I and mouse PIAS4
Gag polyprotein
Interacts (via PPXY motif) with host NEDD4. Interacts (via PSAP motif) with host TSG101. Interacts (via LYPX(n)L motif) with host PDCD6IP.
Family & Domains
Features
Showing features for motif, compositional bias, region, coiled coil, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 111-114 | PTAP/PSAP motif | ||||
Sequence: PSAP | ||||||
Compositional bias | 111-127 | Pro residues | ||||
Sequence: PSAPSLPPEPPLSTPPQ | ||||||
Region | 111-218 | Disordered | ||||
Sequence: PSAPSLPPEPPLSTPPQSSLYPALTSPLNTKPRPQVLPDSGGPLIDLLTEDPPPYRDPGPPSPDGKGDSGEVAPTEGAPDSSPMVSRLRGRREPPVADSTTSQAFPLR | ||||||
Compositional bias | 128-143 | Polar residues | ||||
Sequence: SSLYPALTSPLNTKPR | ||||||
Motif | 130-134 | LYPX(n)L motif | ||||
Sequence: LYPAL | ||||||
Motif | 162-165 | PPXY motif | ||||
Sequence: PPPY | ||||||
Region | 345-393 | Interaction with host PIAS4 | ||||
Sequence: GRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPEDPGQETNV | ||||||
Region | 430-435 | Interaction with host UBE2I | ||||
Sequence: IFNKRE | ||||||
Compositional bias | 434-476 | Basic and acidic residues | ||||
Sequence: RETPEEREERVRRETEEKEERRRAEDERREKERDRRRHREMSK | ||||||
Region | 434-538 | Disordered | ||||
Sequence: RETPEEREERVRRETEEKEERRRAEDERREKERDRRRHREMSKLLATVVSGQRQDRQGGERRRPQLDHDQCAYCKEKGHWARDCPKKPRGPRGPRPQASLLTLDD | ||||||
Coiled coil | 438-478 | |||||
Sequence: EEREERVRRETEEKEERRRAEDERREKERDRRRHREMSKLL | ||||||
Compositional bias | 488-523 | Basic and acidic residues | ||||
Sequence: DRQGGERRRPQLDHDQCAYCKEKGHWARDCPKKPRG | ||||||
Zinc finger | 502-519 | CCHC-type | ||||
Sequence: DQCAYCKEKGHWARDCPK |
Domain
Gag polyprotein
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 interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which 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 interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release.
Keywords
- Domain
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative initiation.
P26805-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameGag polyprotein
- Length538
- Mass (Da)61,033
- Last updated2007-01-23 v3
- Checksum2FF9F97D2C79DEBE
P0DOH6-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameGlyco-Gag protein
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 111-127 | Pro residues | ||||
Sequence: PSAPSLPPEPPLSTPPQ | ||||||
Compositional bias | 128-143 | Polar residues | ||||
Sequence: SSLYPALTSPLNTKPR | ||||||
Compositional bias | 434-476 | Basic and acidic residues | ||||
Sequence: RETPEEREERVRRETEEKEERRRAEDERREKERDRRRHREMSK | ||||||
Compositional bias | 488-523 | Basic and acidic residues | ||||
Sequence: DRQGGERRRPQLDHDQCAYCKEKGHWARDCPKKPRG |
Keywords
- Coding sequence diversity