Detail Information for IndEnz0002018764
IED ID IndEnz0002018764
Enzyme Type ID protease018764
Protein Name Calpain-1 catalytic subunit
EC 3.4.22.52
Calcium-activated neutral proteinase 1
CANP 1
Calpain mu-type
Calpain-1 large subunit
Micromolar-calpain
muCANP
Gene Name CAPN1 CANPL1 QccE-12457
Organism Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
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 Primates Haplorrhini Simiiformes Catarrhini Cercopithecoidea Cercopithecidae (Old World monkeys) Cercopithecinae Macaca (macaques) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Enzyme Sequence MAEEIITPVYCTGVSAQVQKQRAKELGLGRHENAIKYLGQDYEQLRARCLQSGTLFRDEAFPPVPQSLGFKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYESLSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQMVNLIRMRNPWGEVEWTGAWSDSSSEWNSVDPYEREQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPALHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTAELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA
Enzyme Length 714
Uniprot Accession Number Q9GLG2
Absorption
Active Site ACT_SITE 115; /evidence=ECO:0000250; ACT_SITE 272; /evidence=ECO:0000250; ACT_SITE 296; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Activated by micromolar concentrations of calcium and inhibited by calpastatin. {ECO:0000250}.
Binding Site
Calcium Binding CA_BIND 99..106; /note=1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; CA_BIND 302..333; /note=2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; CA_BIND 598..609; /note=3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; CA_BIND 628..639; /note=4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448
catalytic Activity CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52;
DNA Binding
EC Number 3.4.22.52
Enzyme Function FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1. {ECO:0000250|UniProtKB:P07384}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Calcium binding (4); Chain (1); Domain (5); Modified residue (1); Region (3); Site (2)
Keywords Autocatalytic cleavage;Calcium;Cell membrane;Cytoplasm;Hydrolase;Membrane;Metal-binding;Phosphoprotein;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 354; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P07384
Post Translational Modification PTM: Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 81,850
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.52;