IED ID | IndEnz0002005877 |
Enzyme Type ID | protease005877 |
Protein Name |
Caspase-3 CASP-3 EC 3.4.22.56 Apopain Cysteine protease CPP32 xCPP32 Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12 |
Gene Name | casp3 |
Organism | Xenopus laevis (African clawed frog) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
Enzyme Sequence | MEESQNGVKYGGDATDAKEYFTIQPRSLQNCDLKDIERKTKFAHLQNYRTNYPEMGMCLIINNKNFHSSNMAVRNGTDVDALKLHETFTGLGYEVMVCNDQKSSDIIGRLKKISEEDHSKRSSFVCAILSHGEEDGSICGVDVPIHIKNLTDLFRGDRCKTLVGKPKIFFIQACRGTELDSGIETDSCSEPREEIQRIPVEADFLYAYSTVPGYCSWRDKMDGSWFIQSLCKMIKLYGSHLELIQILTCVNHMVALDFETFHAKKQIPCVVSMLTKSFYFFK |
Enzyme Length | 282 |
Uniprot Accession Number | P55866 |
Absorption | |
Active Site | ACT_SITE 131; /evidence=ECO:0000250; ACT_SITE 174; /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: Important mediator of apoptosis. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond (By similarity). {ECO:0000250|UniProtKB:P42574}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (2); Propeptide (1) |
Keywords | Apoptosis;Cytoplasm;Hydrolase;Protease;Thiol protease;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 32,125 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.22.56; |