Detail Information for IndEnz0002019145
IED ID IndEnz0002019145
Enzyme Type ID protease019145
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
Cell proliferation-inducing gene 30 protein
Micromolar-calpain
muCANP
Gene Name CAPN1 CANPL1 PIG30
Organism Homo sapiens (Human)
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 Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKSRTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFVLALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINLREVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSEEEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA
Enzyme Length 714
Uniprot Accession Number P07384
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:0000269|PubMed:8954105, ECO:0000269|PubMed:9271093}.
Binding Site
Calcium Binding CA_BIND 99..106; /note=1; CA_BIND 302..333; /note=2; CA_BIND 598..609; /note=3; CA_BIND 628..639; /note=4
catalytic Activity CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52; Evidence={ECO:0000269|PubMed:16411745, ECO:0000269|PubMed:21531719};
DNA Binding
EC Number 3.4.22.52
Enzyme Function FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (PubMed:21531719, PubMed:2400579). Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409' (PubMed:23707407). {ECO:0000269|PubMed:21531719, ECO:0000269|PubMed:23707407, ECO:0000269|PubMed:2400579}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (15); Calcium binding (4); Chain (1); Domain (5); Helix (16); Initiator methionine (1); Modified residue (2); Natural variant (5); Region (3); Sequence conflict (1); Site (2)
Keywords 3D-structure;Acetylation;Autocatalytic cleavage;Calcium;Cell membrane;Cytoplasm;Disease variant;Hereditary spastic paraplegia;Hydrolase;Membrane;Metal-binding;Neurodegeneration;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease
Interact With P05067; Q92934; P13569; P30085-3; P15311; Q96CV9; P18031; P40763
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21531719, ECO:0000269|PubMed:8769305}. Cell membrane {ECO:0000269|PubMed:8769305}. Note=Translocates to the plasma membrane upon Ca(2+) binding. In granular keratinocytes and in lower corneocytes, colocalizes with FLG and FLG2 (PubMed:21531719). {ECO:0000269|PubMed:21531719}.
Modified Residue MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"; MOD_RES 354; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:23186163"
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. {ECO:0000269|PubMed:8769305, ECO:0000269|PubMed:8954105}.
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1ZCM; 2ARY;
Mapped Pubmed ID 10639123; 10830966; 11076937; 11853546; 11861304; 12000759; 12121992; 12200134; 12393869; 12843408; 14612448; 14980313; 15131115; 15302874; 15471877; 15488707; 15590628; 15663601; 15809056; 15935327; 15948206; 15950654; 15975558; 16107503; 16150694; 16361262; 16598790; 16697376; 16740134; 16908521; 17121855; 17157313; 17359359; 17515931; 17608959; 17620599; 17690304; 17716656; 17765980; 17908236; 17977825; 18032503; 18070881; 18071073; 18085799; 18165173; 18468730; 18498295; 18624398; 18624772; 18726991; 18793761; 18806756; 18823990; 19457105; 19617626; 19712109; 19901552; 19946330; 20034566; 20041182; 20179351; 20398180; 20514436; 20518497; 20557290; 20659425; 20933204; 21030783; 21209906; 21268016; 21305563; 21315622; 21374734; 21442128; 21494752; 21516125; 21555338; 21670566; 21808066; 21825064; 21839844; 21864727; 21876002; 21880013; 21988832; 21997417; 22190034; 22335024; 22449977; 22477191; 22480599; 22623428; 22805611; 23023391; 23035980; 23289183; 23400779; 23408424; 23515028; 23629652; 23650620; 23707532; 23733271; 23919677; 24413738; 24416790; 24670325; 24691096; 25086406; 25241761; 25309925; 25336645; 25476568; 25918155; 26063807; 26172506; 26284543; 26317226; 26496610; 26496999; 26638075; 26974309; 26974350; 27036949; 27320912; 27349634; 27456359; 27742573; 28192161; 28498452; 28536704; 28686728; 29047085; 29572388; 29614685; 29993134; 30177525; 30177812; 30425303; 30572172; 30796192; 30959065; 31023339; 31262726; 31395734; 31878359; 31982778; 32332747; 32395869; 32544313; 32852077; 32860341; 33078830; 33258989; 33486633; 33729106; 34148878; 34440793; 34728688; 7592818; 7698360; 8993318; 9228946; 9407132; 9989581;
Motif
Gene Encoded By
Mass 81,890
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.22.52;3.4.22.53;