P04591 · GAG_HV1H2
- ProteinGag polyprotein
- Genegag
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids500 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Gag polyprotein
Matrix protein p17
Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity).
Capsid protein p24
The core is constituted by capsid protein hexamer subunits (PubMed:19914170, PubMed:8648689).
The core is disassembled soon after virion entry (PubMed:12660176).
The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (PubMed:30270045).
Host restriction factors such as host TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription (PubMed:23785198).
Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (PubMed:23785198).
Host PIN1 apparently facilitates the virion uncoating (By similarity).
On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (PubMed:24554657).
Nucleocapsid protein p7
p6-gag
Miscellaneous
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 132-133 | Cleavage; by viral protease | ||||
Sequence: YP | ||||||
Site | 363-364 | Cleavage; by viral protease | ||||
Sequence: LA | ||||||
Site | 377-378 | Cleavage; by viral protease | ||||
Sequence: MM | ||||||
Site | 432-433 | Cleavage; by viral protease | ||||
Sequence: NF | ||||||
Site | 448-449 | Cleavage; by viral protease | ||||
Sequence: FL |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell nuclear membrane | |
Cellular Component | host cell plasma membrane | |
Cellular Component | host cellular component | |
Cellular Component | host multivesicular body | |
Cellular Component | membrane | |
Cellular Component | viral nucleocapsid | |
Cellular Component | virion membrane | |
Molecular Function | RNA binding | |
Molecular Function | structural molecule activity | |
Molecular Function | zinc ion binding | |
Biological Process | viral budding via host ESCRT complex | |
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
- Alternative names
- Cleaved into 6 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Pararnavirae > Artverviricota > Revtraviricetes > Ortervirales > Retroviridae > Orthoretrovirinae > Lentivirus > Human immunodeficiency virus 1
- Virus hosts
Accessions
- Primary accessionP04591
Proteomes
Subcellular Location
Gag polyprotein
Matrix protein p17
Capsid protein p24
Nucleocapsid protein p7
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 6 | No influence on the PIP2- or concentration-dependent myristyl switch mechanism. | ||||
Sequence: S → D | ||||||
Mutagenesis | 9 | No influence on the PIP2- or concentration-dependent myristyl switch mechanism. | ||||
Sequence: S → D | ||||||
Mutagenesis | 18 | Replication-defective, induces nuclear mislocalization of matrix protein; when associated with G-22. | ||||
Sequence: K → A | ||||||
Mutagenesis | 22 | Replication-defective, induces nuclear mislocalization of matrix protein; when associated with A-18. | ||||
Sequence: R → G | ||||||
Mutagenesis | 27 | No effect on subcellular localization of matrix protein; when associated with A-18 and G-22. | ||||
Sequence: K → A | ||||||
Mutagenesis | 67 | No influence on the PIP2- or concentration-dependent myristyl switch mechanism. | ||||
Sequence: S → D | ||||||
Mutagenesis | 72 | No influence on the PIP2- or concentration-dependent myristyl switch mechanism. | ||||
Sequence: S → D | ||||||
Mutagenesis | 182 | Increased interaction with human NONO. | ||||
Sequence: Q → Y | ||||||
Mutagenesis | 217 | 3-fold decrease of PPIA-binding affinity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 218 | 2.7-fold decrease of PPIA-binding affinity. | ||||
Sequence: V → A | ||||||
Mutagenesis | 219 | 8-fold decrease of PPIA-binding affinity. | ||||
Sequence: H → A or Q | ||||||
Mutagenesis | 220 | 44-fold decrease of PPIA-binding affinity. | ||||
Sequence: A → G | ||||||
Mutagenesis | 220 | 3.4-fold decrease of PPIA-binding affinity. | ||||
Sequence: A → V | ||||||
Mutagenesis | 221 | 31-fold decrease of PPIA-binding affinity. | ||||
Sequence: G → A | ||||||
Mutagenesis | 221 | 154-fold decrease of PPIA-binding affinity. | ||||
Sequence: G → V | ||||||
Mutagenesis | 222 | 36-fold decrease of PPIA-binding affinity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 222 | More than 150-fold decrease of PPIA-binding affinity. | ||||
Sequence: P → V | ||||||
Mutagenesis | 223 | 1.2-fold decrease of PPIA-binding affinity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 223 | 1.0-fold decrease of PPIA-binding affinity. | ||||
Sequence: I → V | ||||||
Mutagenesis | 224 | 2.3-fold decrease of PPIA-binding affinity. | ||||
Sequence: A → G | ||||||
Mutagenesis | 224 | 1.7-fold decrease of PPIA-binding affinity. | ||||
Sequence: A → V | ||||||
Mutagenesis | 225 | 1.6-fold decrease of PPIA-binding affinity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 235-236 | Strongly decreased interaction with human NONO. | ||||
Sequence: DI → AA | ||||||
Mutagenesis | 394 | Decreases infectivity and replication. | ||||
Sequence: N → F or G | ||||||
Mutagenesis | 400 | Complete loss of infectivity and in vitro chaperone activity. | ||||
Sequence: H → C | ||||||
Mutagenesis | 405 | Complete loss of infectivity and DNA synthesis. | ||||
Sequence: C → H | ||||||
Mutagenesis | 421 | Partial loss of infectivity. Complete loss of in vitro chaperone activity. | ||||
Sequence: H → C | ||||||
Mutagenesis | 426 | Partial loss of infectivity. | ||||
Sequence: C → H |
Keywords
- Disease
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; by host | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine; by host | ||||
Sequence: G | ||||||
Chain | PRO_0000038593 | 2-132 | Matrix protein p17 | |||
Sequence: GARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNY | ||||||
Chain | PRO_0000261216 | 2-500 | Gag polyprotein | |||
Sequence: GARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ | ||||||
Chain | PRO_0000038594 | 133-363 | Capsid protein p24 | |||
Sequence: PIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVL | ||||||
Modified residue | 148 | Phosphoserine; by host MAPK1 | ||||
Sequence: S | ||||||
Peptide | PRO_0000038595 | 364-377 | Spacer peptide 1 | |||
Sequence: AEAMSQVTNSATIM | ||||||
Chain | PRO_0000038596 | 378-432 | Nucleocapsid protein p7 | |||
Sequence: MQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQAN | ||||||
Modified residue | 387 | Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 | ||||
Sequence: R | ||||||
Modified residue | 409 | Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 | ||||
Sequence: R | ||||||
Peptide | PRO_0000038597 | 433-448 | Spacer peptide 2 | |||
Sequence: FLGKIWPSYKGRPGNF | ||||||
Chain | PRO_0000038598 | 449-500 | p6-gag | |||
Sequence: LQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ |
Post-translational modification
Matrix protein p17
Capsid protein p24
Nucleocapsid protein p7
Keywords
- PTM
Interaction
Subunit
Gag polyprotein
Oligomerization possibly creates a central hole into which the cytoplasmic tail of the gp41 envelope protein may be inserted. Interacts with host TRIM22; this interaction seems to disrupt proper trafficking of Gag polyprotein and may interfere with budding (PubMed:18389079).
Interacts with host PDZD8 (PubMed:20573829).
When ubiquitinated, interacts (via p6-gag domain) with host PACSIN2; this interaction allows PACSIN2 recruitment to viral assembly sites and its subsequent incorporation into virions (By similarity).
Interacts with MOV10 (PubMed:20215113).
Matrix protein p17
Interacts with gp41 (via C-terminus) (By similarity).
Interacts with host CALM1; this interaction induces a conformational change in the Matrix protein, triggering exposure of the myristate group (PubMed:24500712).
Interacts with host AP3D1; this interaction allows the polyprotein trafficking to multivesicular bodies during virus assembly (By similarity).
Part of the pre-integration complex (PIC) which is composed of viral genome, matrix protein, Vpr and integrase (By similarity).
Capsid protein p24
Interacts with host NUP98 (By similarity).
Interacts with host PPIA/CYPA; this interaction stabilizes the capsid (PubMed:9223641).
Interacts with host NUP153 (By similarity).
Interacts with host PDZD8; this interaction stabilizes the capsid (PubMed:20573829).
Interacts with host TRIM5; this interaction destabilizes the capsid (PubMed:23785198).
Interacts with host CPSF6 (By similarity).
Interacts with host NONO; the interaction is weak (PubMed:30270045).
Nucleocapsid protein p7
p6-gag
Interacts with host TSG101 (By similarity).
Interacts with host PDCD6IP/AIP1 (By similarity).
Binary interactions
Protein-protein interaction databases
Family & Domains
Features
Showing features for region, motif, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 7-31 | Interaction with Gp41 | ||||
Sequence: VLSGGELDRWEKIRLRPGGKKKYKL | ||||||
Region | 8-43 | Interaction with host CALM1 | ||||
Sequence: LSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELER | ||||||
Region | 12-19 | Interaction with host AP3D1 | ||||
Sequence: ELDRWEKI | ||||||
Region | 14-33 | Interaction with membrane phosphatidylinositol 4,5-bisphosphate and RNA | ||||
Sequence: DRWEKIRLRPGGKKKYKLKH | ||||||
Motif | 16-22 | Nuclear export signal | ||||
Sequence: WEKIRLR | ||||||
Motif | 26-32 | Nuclear localization signal | ||||
Sequence: KKKYKLK | ||||||
Region | 73-77 | Interaction with membrane phosphatidylinositol 4,5-bisphosphate | ||||
Sequence: EELRS | ||||||
Region | 106-128 | Disordered | ||||
Sequence: EEQNKSKKKAQQAAADTGHSNQV | ||||||
Region | 189-227 | Interaction with host PPIA/CYPA and NUP153 | ||||
Sequence: NTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQ | ||||||
Region | 217-225 | PPIA/CYPA-binding loop | ||||
Sequence: PVHAGPIAP | ||||||
Region | 277-363 | Dimerization/Multimerization of capsid protein p24 | ||||
Sequence: YSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVL | ||||||
Zinc finger | 390-407 | CCHC-type 1 | ||||
Sequence: VKCFNCGKEGHTARNCRA | ||||||
Zinc finger | 411-428 | CCHC-type 2 | ||||
Sequence: KGCWKCGKEGHQMKDCTE | ||||||
Region | 444-500 | Disordered | ||||
Sequence: RPGNFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ | ||||||
Motif | 455-458 | PTAP/PSAP motif | ||||
Sequence: PTAP | ||||||
Motif | 483-492 | LYPX(n)L motif | ||||
Sequence: LYPLTSLRSL |
Domain
Sequence similarities
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 most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.
P04591-1
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.
- Length500
- Mass (Da)55,930
- Last updated2007-01-23 v3
- ChecksumB74C3858C20EF82C
P04585-1
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
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
K03455 EMBL· GenBank· DDBJ | AAB50258.1 EMBL· GenBank· DDBJ | Genomic RNA |