Detail Information for IndEnz0002019321
IED ID IndEnz0002019321
Enzyme Type ID protease019321
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 2 subtype A (isolate ROD) (HIV-2)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Human immunodeficiency virus 2 HIV-2 subtype A Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2)
Enzyme Sequence MGARNSVLRGKKADELERIRLRPGGKKKYRLKHIVWAANKLDRFGLAESLLESKEGCQKILTVLDPMVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVRRHLVAETGTAEKMPSTSRPTAPSSEKGGNYPVQHVGGNYTHIPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAAEWDVQHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLVQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMAEALKEVIGPAPIPFAAAQQRKAFKCWNCGKEGHSARQCRAPRRQGCWKCGKPGHIMTNCPDRQAGFLGLGPWGKKPRNFPVAQVPQGLTPTAPPVDPAVDLLEKYMQQGKRQREQRERPYKEVTEDLLHLEQGETPYREPPTEDLLHLNSLFGKDQ
Enzyme Length 522
Uniprot Accession Number P04590
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 (By similarity). Most core are conical, with only 7% tubular (By similarity). The core is constituted by capsid protein hexamer subunits (By similarity). The core is disassembled soon after virion entry (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 (By similarity). Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). The capsid interacts with high affinity with human NONO, promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation (By similarity). {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493, ECO:0000250|UniProtKB:P18095}.; 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 Beta strand (3); Chain (5); Compositional bias (2); Helix (7); Initiator methionine (1); Lipidation (1); Modified residue (1); Motif (3); Peptide (2); Region (10); Site (5); Turn (2); Zinc finger (2)
Keywords 3D-structure;AIDS;Capsid protein;Host cell membrane;Host cytoplasm;Host endosome;Host membrane;Host nucleus;Host-virus interaction;Lipoprotein;Membrane;Metal-binding;Myristate;Phosphoprotein;RNA-binding;Reference proteome;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 Q13523
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 150; /note=Phosphoserine; by host MAPK1; /evidence=ECO:0000250|UniProtKB:P12493
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 X-ray crystallography (2)
Cross Reference PDB 2WLV; 4DGB;
Mapped Pubmed ID 15452250; 19767750; 22407016;
Motif MOTIF 16..22; /note=Nuclear export signal; /evidence=ECO:0000250; MOTIF 26..32; /note=Nuclear localization signal; /evidence=ECO:0000250; MOTIF 456..459; /note=PTAP/PSAP motif
Gene Encoded By
Mass 58,374
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda