Detail Information for IndEnz0002003195
IED ID IndEnz0002003195
Enzyme Type ID protease003195
Protein Name Gag polyprotein
Core polyprotein

Cleaved into: Matrix protein p15
MA
; RNA-binding phosphoprotein p12
pp12
; Capsid protein p30
CA
; Nucleocapsid protein p10-Gag
NC-gag
Gene Name gag
Organism Gibbon ape leukemia virus (GALV)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Gammaretrovirus Gibbon ape leukemia virus (GALV)
Enzyme Sequence MGQDNSTPISLTLNHWRDVRTRAHNLSVEIKKGKWQTFCSSEWPTFGVGWPPEGTFNLSVIFAVKKIVFQENGGHPDQVPYIVVWQDLAQNPPPWVPASAKVAVVSDTRRPVAGRPSAPPRPPIYPATDDLLLLSEPTPPPYPAALPPPLAPQAIGPPSGQMPDSSDPEGPAAGTRSRRARSPADNSGPDSTVILPLRAIGPPAEPNGLVPLQYWPFSSADLYNWKSNHPSFSENPAGLTGLLESLMFSHQPTWDDCQQLLQILFTTEERERILLEARKNVLGDNGAPTQLENLINEAFPLNRPHWDYNTAAGRERLLVYRRTLVAGLKGAARRPTNLAKVREVLQGPAEPPSVFLERLMEAYRRYTPFDPSSEGQQAAVAMAFIGQSAPDIKKKLQRLEGLQDYSLQDLVKEAEKVYHKRETEEERQEREKKEAEEKERRRDRPKKKNLTKILAAVVSREGSTGRQTGNLSNQAKKTPRDGRPPLDKDQCAYCKEKGHWARECPRKKHVREAKVLALDN
Enzyme Length 520
Uniprot Accession Number P21416
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme 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. {ECO:0000250|UniProtKB:P03332}.; FUNCTION: [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. {ECO:0000250|UniProtKB:P03332}.; FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-integration complex (PIC) which tethers the latter to mitotic chromosomes. {ECO:0000250|UniProtKB:P03332}.; FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250|UniProtKB:P03336}.; FUNCTION: [Nucleocapsid protein p10-Gag]: Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization. {ECO:0000250|UniProtKB:P03332}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (5); Compositional bias (3); Initiator methionine (1); Lipidation (1); Motif (2); Region (2); Site (3); Zinc finger (1)
Keywords Capsid protein;Host cell membrane;Host cytoplasm;Host endosome;Host membrane;Host-virus interaction;Lipoprotein;Membrane;Metal-binding;Myristate;Phosphoprotein;RNA-binding;Viral budding;Viral budding via the host ESCRT complexes;Viral matrix protein;Viral nucleoprotein;Viral release from host cell;Virion;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P26807}. Note=These locations are probably linked to virus assembly sites. {ECO:0000305}.; SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000250|UniProtKB:P03332}.; SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000250|UniProtKB:P03332}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p10-Gag]: Virion {ECO:0000250|UniProtKB:P03332}.; SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm {ECO:0000250|UniProtKB:P03332}. Note=Localizes to the host cytoplasm early in infection and binds to the mitotic chromosomes later on. {ECO:0000250|UniProtKB:P03332}.
Modified Residue
Post Translational Modification PTM: [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. {ECO:0000250|UniProtKB:P03332}.; PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine residues. {ECO:0000250|UniProtKB:P03332}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 116..119; /note=PTAP/PSAP motif; /evidence=ECO:0000250|UniProtKB:P03332; MOTIF 139..142; /note=PPXY motif; /evidence=ECO:0000250|UniProtKB:P03332
Gene Encoded By
Mass 58,110
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda