P03322 · GAG_RSVP
- ProteinGag polyprotein
- Genegag
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids701 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Gag polyprotein
Capsid protein p27, alternate cleaved 1
Binds to inositol hexakisphosphate (IP6), which allows the assembly of the polyhedral capsid (PubMed:34050170).
Capsid protein p27, alternate cleaved 2
Binds to inositol hexakisphosphate (IP6), which allows the assembly of the polyhedral capsid (PubMed:34050170).
Nucleocapsid protein p12
Plays a role in the maturation-stabilization of the viral dimeric RNA via highly structured zinc-binding motifs (By similarity).
Spacer peptide
Essential layering element during tube assembly that is progressively removed as capsid assembly proceeds (PubMed:28588198).
Allows the cooperative binging of Gag to the host plasma membrane (PubMed:26676779).
Protease p15
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 155-156 | Cleavage; by viral protease p15 | ||||
Sequence: YH | ||||||
Site | 166-167 | Cleavage; by viral protease p15 | ||||
Sequence: AT | ||||||
Site | 177-178 | Cleavage; by viral protease p15 | ||||
Sequence: GS | ||||||
Site | 239-240 | Cleavage; by viral protease p15 | ||||
Sequence: MP | ||||||
Site | 418 | Involved in capsid protein dimerization upon acidification | ||||
Sequence: D | ||||||
Site | 430 | Involved in capsid protein dimerization upon acidification | ||||
Sequence: D | ||||||
Site | 476-477 | Cleavage; by viral protease p15 | ||||
Sequence: AA | ||||||
Site | 479-480 | Cleavage; by viral protease p15 | ||||
Sequence: MS | ||||||
Site | 488-489 | Cleavage; by viral protease p15 | ||||
Sequence: MA | ||||||
Site | 577-578 | Cleavage; by viral protease p15 | ||||
Sequence: SL | ||||||
Active site | 614 | For protease activity; shared with dimeric partner | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell nucleolus | |
Cellular Component | host cell nucleoplasm | |
Cellular Component | host cell plasma membrane | |
Cellular Component | membrane | |
Cellular Component | viral capsid | |
Molecular Function | aspartic-type endopeptidase activity | |
Molecular Function | nucleic acid binding | |
Molecular Function | structural constituent of virion | |
Molecular Function | zinc ion binding | |
Biological Process | proteolysis | |
Biological Process | viral procapsid maturation | |
Biological Process | viral translational frameshifting |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGag polyprotein
- Cleaved into 9 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Pararnavirae > Artverviricota > Revtraviricetes > Ortervirales > Retroviridae > Orthoretrovirinae > Alpharetrovirus > Rous sarcoma virus
- Virus hosts
Accessions
- Primary accessionP03322
- Secondary accessions
Proteomes
Subcellular Location
Matrix protein p19
Capsid protein p27, alternate cleaved 1
Capsid protein p27, alternate cleaved 2
Nucleocapsid protein p12
Gag polyprotein
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 172 | 75% loss of budding. | ||||
Sequence: P → A | ||||||
Mutagenesis | 180-184 | 40% loss of budding. | ||||
Sequence: LYPSL → AAASA | ||||||
Mutagenesis | 219 | Reduced nucleolar localization of Gag polyprotein. | ||||
Sequence: L → A | ||||||
Mutagenesis | 524-527 | Complete loss of nuclear and nucleolar localization. | ||||
Sequence: KKRK → AAAA | ||||||
Mutagenesis | 549-551 | Reduced localization in nucleolus; no effect on nuclear localization. | ||||
Sequence: RKR → AAA |
PTM/Processing
Features
Showing features for chain, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000026113 | 1-155 | Matrix protein p19 | |||
Sequence: MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMILGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCY | ||||||
Chain | PRO_0000442114 | 1-701 | Gag polyprotein | |||
Sequence: MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMILGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGPALTDWARVREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLNRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADIMQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRTAPSTLTTPGEIIKYVLDRQKTAPLTDQGIAAAMSSAIQPLIMAVVNRERDGQTGSGGRARGLCYTCGSPGHYQAQCPKKRKSGNSRERCQLCNGMGHNAKQCRKRDGNQGQRPGKGLSSGPWPGPEPPAVSLAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVMEAANPQIHGIGGGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNL | ||||||
Chain | PRO_0000026114 | 156-166 | p2A | |||
Sequence: HCGTAIGCNCA | ||||||
Chain | PRO_0000026115 | 167-177 | p2B | |||
Sequence: TASAPPPPYVG | ||||||
Chain | PRO_0000026116 | 178-239 | p10 | |||
Sequence: SGLYPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGPALTDWARVREELASTGPPVVAM | ||||||
Chain | PRO_0000442115 | 240-476 | Capsid protein p27, alternate cleaved 1 | |||
Sequence: PVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLNRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADIMQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRTAPSTLTTPGEIIKYVLDRQKTAPLTDQGIA | ||||||
Chain | PRO_0000026117 | 240-479 | Capsid protein p27, alternate cleaved 2 | |||
Sequence: PVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLNRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADIMQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRTAPSTLTTPGEIIKYVLDRQKTAPLTDQGIAAAM | ||||||
Peptide | PRO_0000026118 | 477-488 | Spacer peptide | |||
Sequence: AAMSSAIQPLIM | ||||||
Chain | PRO_0000026119 | 489-577 | Nucleocapsid protein p12 | |||
Sequence: AVVNRERDGQTGSGGRARGLCYTCGSPGHYQAQCPKKRKSGNSRERCQLCNGMGHNAKQCRKRDGNQGQRPGKGLSSGPWPGPEPPAVS | ||||||
Chain | PRO_0000026120 | 578-701 | Protease p15 | |||
Sequence: LAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVMEAANPQIHGIGGGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNL |
Post-translational modification
Gag polyprotein
The cleavage at the C-terminus of the Capsid protein p27 is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 amino acids in a ratio of 2:1 (PubMed:7666544).
Interaction
Subunit
Protease p15
Capsid protein p27, alternate cleaved 1
Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062).
Homohexamer (PubMed:28588198).
Capsid protein p27, alternate cleaved 2
Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062).
Homohexamer (PubMed:28588198).
Gag polyprotein
Interacts (via p2B domain) with host PACSIN2; this interaction probably allows PACSIN2 recruitment to viral assembly sites (By similarity).
Protein-protein interaction databases
Family & Domains
Features
Showing features for region, motif, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 128-150 | Disordered | ||||
Sequence: VGETTVQRDAKMAPEETATPKTV | ||||||
Motif | 172-175 | PPXY motif | ||||
Sequence: PPPY | ||||||
Motif | 180-184 | LYPX(n)L motif | ||||
Sequence: LYPSL | ||||||
Region | 181-217 | Disordered | ||||
Sequence: YPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGP | ||||||
Region | 217-259 | Involved in capsid protein dimerization | ||||
Sequence: PALTDWARVREELASTGPPVVAMPVVIKTEGPAWTPLEPKLIT | ||||||
Motif | 219-229 | Nuclear export signal | ||||
Sequence: LTDWARVREEL | ||||||
Region | 290-298 | Involved in capsid protein dimerization | ||||
Sequence: HDVTNLMRV | ||||||
Region | 351-362 | Involved in capsid protein dimerization | ||||
Sequence: GMVGNPQGQAAL | ||||||
Zinc finger | 507-524 | CCHC-type 1 | ||||
Sequence: GLCYTCGSPGHYQAQCPK | ||||||
Motif | 524-527 | Nuclear/nucleolar localization signal | ||||
Sequence: KKRK | ||||||
Zinc finger | 533-550 | CCHC-type 2 | ||||
Sequence: ERCQLCNGMGHNAKQCRK | ||||||
Region | 543-575 | Disordered | ||||
Sequence: HNAKQCRKRDGNQGQRPGKGLSSGPWPGPEPPA | ||||||
Domain | 609-690 | Peptidase A2 | ||||
Sequence: ITALLDSGADITIISEEDWPTDWPVMEAANPQIHGIGGGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDC |
Domain
Gag polyprotein
Gag polyprotein
Keywords
- Domain
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Ribosomal frameshifting. Translation results in the formation of the Gag polyprotein. Ribosomal frameshifting at the gag/pol genes boundary produces the Gag-Pol polyprotein.
P03322-1
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
- NoteProduced by conventional translation.
- Length701
- Mass (Da)74,527
- Last updated1986-07-21 v1
- Checksum5FD365D9CFEF37F1
P03354-1
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- NameGag-Pol polyprotein
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 505 | in Ref. 2; AA sequence | ||||
Sequence: A → S | ||||||
Sequence conflict | 536 | in Ref. 2; AA sequence | ||||
Sequence: Q → E |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF033808 EMBL· GenBank· DDBJ | AAC82560.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
J02342 EMBL· GenBank· DDBJ | AAB59932.1 EMBL· GenBank· DDBJ | Genomic RNA | ||
V01197 EMBL· GenBank· DDBJ | CAA24512.1 EMBL· GenBank· DDBJ | Genomic DNA |