Detail Information for IndEnz0002005877
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;