| IED ID | IndEnz0002018982 |
| Enzyme Type ID | protease018982 |
| Protein Name |
Calpain-3 EC 3.4.22.54 Calcium-activated neutral proteinase 3 CANP 3 Calpain L3 Calpain p94 Muscle-specific calcium-activated neutral protease 3 New calpain 1 nCL-1 |
| Gene Name | CAPN3 NCL1 |
| 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 | MPTVISASMAPRTGASQVPRTMPQAAQGKGTEAGVGNPGGKYSAIISRNFPIIGVKEKTFEQLHKKCLEKKVLYLDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIGGANRTDICQGDLGDCWFLAAIACLTLNKRLLFRVIPHDQSFTENYAGIFHFQFWRYGDWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFFEIKDAPRDMYKIMKKAIERGSLMGCSIDDGTNMTYGTSPSGLKMGDLIARMVRNMDESRLRDSDLIPEGCSDDRPTRTIVPVQFETRMACGLVKGHAYSVTGLEEALFKGEKVKLVRLRNPWGQVEWNGSWSDSWKDWSFVDKDEKARLQHQVTEDGEFWMSYDDFIYHFTKLEICNLTADALESDKLQTWTVSVNEGRWVRGCSAGGCRNFPDTFWTNPQYRLKLLEEDDDPDDSEVICSFLVALMQKNRRKDRKLGANLFTIGFAIYEVPKEMHGNKQHLQKDFFLYNASKARSRTYINMREVSERFRLPPSEYVIVPSTYEPHQEGEFILRVFSEKRNLSEEVENTISVDRPVRKKKTKPIIFVSDRANSNKELGVDQESEEGQDKTSPDKQEKSPKPEPSNTDQESEEQQQFRNIFRQIAGDDMEICADELKNVLNRVVNKHKDLKTEGFTLESCRSMIALMDTDGSGRLNLQEFHHLWKKIKSWQKIFKHYDTDQSGTINSYEMRNAVNDAGFHLNNQLYDIITMRYADKYMNIDFDSFICCFVRLEGMFRAFNAFDKDGDGIIKLNVLEWLQLTMYA |
| Enzyme Length | 821 |
| Uniprot Accession Number | P43368 |
| Absorption | |
| Active Site | ACT_SITE 128; /evidence=ECO:0000255|PROSITE-ProRule:PRU00239; ACT_SITE 334; /evidence=ECO:0000255|PROSITE-ProRule:PRU00239; ACT_SITE 358; /evidence=ECO:0000255|PROSITE-ProRule:PRU00239 |
| Activity Regulation | ACTIVITY REGULATION: Activated by micromolar concentrations of calcium and inhibited by calpastatin. |
| Binding Site | |
| Calcium Binding | CA_BIND 662..672; /note="1"; /evidence="ECO:0000250|UniProtKB:P20807"; CA_BIND 705..716; /note="2"; /evidence="ECO:0000250|UniProtKB:P20807, ECO:0000255|PROSITE-ProRule:PRU00448"; CA_BIND 735..741; /note="3"; /evidence="ECO:0000250|UniProtKB:P20807, ECO:0000255|PROSITE-ProRule:PRU00448"; CA_BIND 800..806; /note="4"; /evidence="ECO:0000250|UniProtKB:P20807" |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase activity.; EC=3.4.22.54; |
| DNA Binding | |
| EC Number | 3.4.22.54 |
| Enzyme Function | FUNCTION: Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53. {ECO:0000250|UniProtKB:P20807}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Calcium binding (4); Chain (1); Compositional bias (2); Domain (5); Region (5); Sequence conflict (7) |
| Keywords | Calcium;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Repeat;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20807}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P20807}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21450414; |
| Motif | |
| Gene Encoded By | |
| Mass | 94,551 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.54; |