Detail Information for IndEnz0002016407
IED ID IndEnz0002016407
Enzyme Type ID protease016407
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
Gene Name Capn3
Organism Mus musculus (Mouse)
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 Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MPTVISPTVAPRTGAEPRSPGPVPHPAQGKTTEAGGGHPSGIYSAIISRNFPIIGVKEKTFEQLRRKCLEKKVLYLDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIGGANRTDICQGDLGDCWFLAAIACLTLNERLLFRVIPHDQSFTENYAGIFHFQFWRYGDWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFFEIKDAPSDMYKIMRKAIERGSLMGCSIDDGTNMTYGTSPSGLNMGELIARMVRNMDNSLLRDSDLDPRGSDDRPSRTIVPVQYETRMACGLVKGHAYSVTGLEEALFKGEKVKLVRLRNPWGQVEWNGSWSDGWKDWSFVDKDEKARLQHQVTEDGEFWMSYDDFVYHFTKLEICNLTADALESDKLQTWTVSVNEGRWVRGCSAGGCRNFPDTFWTNPQYRLKLLEEDDDPEDSEVICSFLVALMQKNRRKDRKLGANLFTIGFAIYEVPKEMHGNKQHLQKDFFLYNASKARSKTYINMREVSQRFRLPPSEYVIVPSTYEPHQEGEFILRVFSEKRNLSEEAENTISVDRPVKKKKNKPIIFVSDRANSNKELGVDQEAEEGKDKAGPEKRGETPQPRPGHTDQESEEQQQFRNIFRQIAGDDMEICADELKNVLNTVVNKHKDLKTQGFTLESCRSMIALMDTDGSGRLNLQEFHHLWKKIKAWQKIFKHYDTDHSGTINSYEMRNAVNDAGFHLNSQLYDIITMRYADKHMNIDFDSFICCFVRLEGMFRAFNAFDKDGDGIIKLNVLEWLQLTMYA
Enzyme Length 821
Uniprot Accession Number Q64691
Absorption
Active Site ACT_SITE 129; /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 at 'His-410'. 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); Alternative sequence (2); Calcium binding (4); Chain (1); Compositional bias (1); Domain (5); Region (5); Sequence conflict (2)
Keywords Alternative splicing;Calcium;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Repeat;Thiol protease
Interact With Q9ES46
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 10330145; 10607827; 10814721; 11134085; 11952156; 12084932; 12105198; 12466851; 12634108; 12672459; 12707983; 14594950; 14610273; 14645524; 14741210; 15138196; 15687484; 15961411; 16115818; 16140986; 16453164; 16602821; 16627476; 16705022; 16717059; 16982691; 17051641; 17371879; 17525200; 17594342; 18073330; 18310072; 18385073; 18676612; 19143834; 19269960; 19295178; 19483197; 19924298; 19926129; 20139084; 20405035; 20460380; 20592470; 20855473; 20860623; 21267068; 21624972; 2209092; 22505582; 22820870; 23300487; 23662692; 24096375; 25389288; 25877298; 26060189; 27005420; 27055500; 29241457; 29528394; 30333037; 31776291; 31890729; 32448375; 32982660; 33308300; 8738748; 8806430; 8997499; 9396712; 9473662; 9670959; 9846490;
Motif
Gene Encoded By
Mass 94,242
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.54;