| IED ID | IndEnz0002005188 |
| Enzyme Type ID | protease005188 |
| 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 |
| Gene Name | CAPN2 |
| Organism | Bos taurus (Bovine) |
| 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 Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MAGIAAKLAKDREAAEGLGSHERAVKYLNQDYAALRDECLEAGALFQDPSFPALPSSLGFKELGPYSSKTRGIEWKRPTEICDNPQFITGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKAPPNLFRIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESRGSLQKLIRIRNPWGEVEWTGQWNDNCPNWNTVDPEVRETLTRQHEDGEFWMSFNDFLRHYSRLEICNLTPDTLTSDSYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDQEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLSKKFFLTTRARERSDTFINLREVLNRFKLPPGEYIVVPSTFEPNKDGDFCIRVFSEKKADYQVVDDEIEANIDEIDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDDLIIDFDNFVRCLIRLETLFRIFKQLDPENTGMIQLDLISWLSFSVL |
| Enzyme Length | 700 |
| Uniprot Accession Number | Q27971 |
| Absorption | |
| Active Site | ACT_SITE 105; /evidence=ECO:0000250; ACT_SITE 262; /evidence=ECO:0000250; ACT_SITE 286; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin. |
| Binding Site | |
| Calcium Binding | |
| 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 | Active site (3); Chain (1); Domain (4); Frameshift (1); Initiator methionine (1); Metal binding (24); Modified residue (1); Propeptide (1); Region (3); Sequence conflict (2) |
| Keywords | Acetylation;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 | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:P17655 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 8223493; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,935 |
| Kinetics | |
| Metal Binding | METAL 91; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 96; /note=Calcium 3; /evidence=ECO:0000250; METAL 175; /note=Calcium 3; /evidence=ECO:0000250; METAL 229; /note=Calcium 2; /evidence=ECO:0000250; METAL 230; /note=Calcium 2; /evidence=ECO:0000250; METAL 292; /note=Calcium 4; /evidence=ECO:0000250; METAL 299; /note=Calcium 4; /evidence=ECO:0000250; METAL 323; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 542; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 545; /note=Calcium 5; /evidence=ECO:0000250; METAL 547; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 552; /note=Calcium 5; /evidence=ECO:0000250; METAL 585; /note=Calcium 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 587; /note=Calcium 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 589; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 591; /note=Calcium 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 596; /note=Calcium 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 615; /note=Calcium 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 617; /note=Calcium 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 619; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 621; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 626; /note=Calcium 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 658; /note=Calcium 1; /evidence=ECO:0000250; METAL 661; /note=Calcium 1; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |