| IED ID | IndEnz0002018769 |
| Enzyme Type ID | protease018769 |
| Protein Name |
Calpain-2 catalytic subunit EC 3.4.22.53 Calcium-activated neutral proteinase 2 CANP 2 Calpain M-type Calpain-2 large subunit Millimolar-calpain M-calpain Fragment |
| Gene Name | CAPN2 |
| Organism | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | YPNTFWMNPQYLIKLEEEDEDQEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLSKNFFLTHRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQVVDDEIEADLEENDASEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCRIMVDMLDSDGSAKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFRISKQLDSENTGTIELDLISWLCFSVL |
| Enzyme Length | 324 |
| Uniprot Accession Number | P43367 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin. |
| Binding Site | |
| Calcium Binding | CA_BIND 209..220; /note=1; CA_BIND 239..250; /note=2 |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.53; |
| DNA Binding | |
| EC Number | 3.4.22.53 |
| Enzyme Function | FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs. {ECO:0000250|UniProtKB:O08529, ECO:0000250|UniProtKB:P17655}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Calcium binding (2); Chain (1); Domain (2); Metal binding (16); Non-terminal residue (1); Region (3); Sequence conflict (1) |
| Keywords | Calcium;Cell membrane;Cytoplasm;Hydrolase;Membrane;Metal-binding;Protease;Reference proteome;Repeat;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,809 |
| Kinetics | |
| Metal Binding | METAL 166; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 169; /note=Calcium 5; /evidence=ECO:0000250; METAL 171; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 176; /note=Calcium 5; /evidence=ECO:0000250; METAL 209; /note=Calcium 6; /evidence=ECO:0000250; METAL 211; /note=Calcium 6; /evidence=ECO:0000250; METAL 213; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250; METAL 215; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250; METAL 220; /note=Calcium 6; /evidence=ECO:0000250; METAL 239; /note=Calcium 7; /evidence=ECO:0000250; METAL 241; /note=Calcium 7; /evidence=ECO:0000250; METAL 243; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250; METAL 245; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250; METAL 250; /note=Calcium 7; /evidence=ECO:0000250; METAL 282; /note=Calcium 1; /evidence=ECO:0000250; METAL 285; /note=Calcium 1; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.53; |