| IED ID | IndEnz0002003051 |
| Enzyme Type ID | protease003051 |
| Protein Name |
Gag polyprotein Pr55Gag Cleaved into: Matrix protein p17 MA ; Capsid protein p24 CA ; Spacer peptide 1 SP1 p2 ; Nucleocapsid protein p7 NC ; Spacer peptide 2 SP2 p1 ; p6-gag |
| Gene Name | gag |
| Organism | Human immunodeficiency virus type 1 group M subtype B (isolate OYI) (HIV-1) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Human immunodeficiency virus 1 HIV-1 unknown group Human immunodeficiency virus type 1 group M subtype B (isolate OYI) (HIV-1) |
| Enzyme Sequence | MGARASVLSGGELDKWEKIRLRPGGKKKYQLKHIVWASRELERFAINPGLLETSEGCRQILGQLQPSLKTGSEEIRSLYNTVATLYCVHQKIEVKDTKEALDKIEEEQNKSKKKAQQTAADTGNSSQVSQNYPIVQNLQGQMVHQPISPRTLNAWVKVVEEKAFSPEVIPMFSALAEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVNSVTVMMQKGNFKNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWKCGREGHQMKDCTERQANFLGKIWPSHKGRPGNFLQNRPEPTAPPAESFGFGEETTTPPQKQEPIDKGLYPLTSLRSLFGNDPSSQ |
| Enzyme Length | 499 |
| Uniprot Accession Number | P20889 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry (By similarity). The capsid promotes immune invasion by cloaking viral DNA from CGAS detection (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription. Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species. Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.; FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. {ECO:0000250|UniProtKB:P04591}.; FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (5); Initiator methionine (1); Lipidation (1); Modified residue (3); Motif (4); Peptide (2); Region (10); Site (5); Zinc finger (2) |
| Keywords | AIDS;Capsid protein;Host cell membrane;Host cytoplasm;Host endosome;Host membrane;Host nucleus;Host-virus interaction;Lipoprotein;Membrane;Metal-binding;Methylation;Myristate;Phosphoprotein;RNA-binding;Repeat;Ribosomal frameshifting;Viral budding;Viral budding via the host ESCRT complexes;Viral nucleoprotein;Viral release from host cell;Virion;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}. |
| Modified Residue | MOD_RES 148; /note=Phosphoserine; by host MAPK1; /evidence=ECO:0000250|UniProtKB:P12493; MOD_RES 386; /note=Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6; /evidence=ECO:0000250; MOD_RES 408; /note=Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniProtKB:P04591}.; PTM: Capsid protein p24 is phosphorylated possibly by host MAPK1; this phosphorylation is necessary for Pin1-mediated virion uncoating. {ECO:0000250|UniProtKB:P12493}.; PTM: Nucleocapsid protein p7 is methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription. {ECO:0000250|UniProtKB:P03347}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 16..22; /note=Nuclear export signal; /evidence=ECO:0000250; MOTIF 26..32; /note=Nuclear localization signal; /evidence=ECO:0000250; MOTIF 454..457; /note=PTAP/PSAP motif; MOTIF 482..491; /note=LYPX(n)L motif |
| Gene Encoded By | |
| Mass | 55,583 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |