| IED ID | IndEnz0002014073 |
| Enzyme Type ID | protease014073 |
| Protein Name |
Caspase-3 CASP-3 EC 3.4.22.56 Apopain Cysteine protease CPP32 CPP-32 Protein Yama SREBP cleavage activity 1 SCA-1 Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12 |
| Gene Name | CASP3 CPP32 |
| Organism | Mesocricetus auratus (Golden hamster) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Cricetidae Cricetinae (hamsters) Mesocricetus Mesocricetus auratus (Golden hamster) |
| Enzyme Sequence | MENNETSVDSKSIKNFEVKTIHGSKSMDSGIYLDSSYKMDYPEMGVCIIINNKNFHKSTGMTPRSGTDVDAAKLRETFMALKYEVRNKNDLTREEIVELMKNASKEDHSKRSSFVCVILSHGDEGVIFGTDGPIDLKKLTSYFRGDYCRSLIGKPKLFIIQACRGTELDCGIETDSGTEDDMTCQKIPVEADFLYAYSTAPGYYSWRNPKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESFSLDSTFHAKKQIPCIVSMLTKELYFYH |
| Enzyme Length | 277 |
| Uniprot Accession Number | Q60431 |
| Absorption | |
| Active Site | ACT_SITE 121; /evidence=ECO:0000250; ACT_SITE 163; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.; EC=3.4.22.56; Evidence={ECO:0000250|UniProtKB:P42574}; |
| DNA Binding | |
| EC Number | 3.4.22.56 |
| Enzyme Function | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction. Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (By similarity). {ECO:0000250|UniProtKB:P42574, ECO:0000250|UniProtKB:P70677}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (2); Modified residue (4); Propeptide (2) |
| Keywords | Acetylation;Apoptosis;Cytoplasm;Hydrolase;Phosphoprotein;Protease;Reference proteome;S-nitrosylation;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P42574; MOD_RES 11; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P70677; MOD_RES 26; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P42574; MOD_RES 163; /note=S-nitrosocysteine; in inhibited form; /evidence=ECO:0000250|UniProtKB:P42574 |
| Post Translational Modification | PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa (By similarity). {ECO:0000250}.; PTM: S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,612 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |