IED Industry Enzyme Database

Detail Information for IndEnz0002019203
IED ID IndEnz0002019203
Enzyme Type ID protease019203
Protein Name Calpain-2 catalytic subunit
EC 3.4.22.53
Calcium-activated neutral proteinase 2
CANP 2
Calpain M-type
Calpain large polypeptide L2
Calpain-2 large subunit
Millimolar-calpain
M-calpain
Gene Name CAPN2 CANPL2
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 MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL
Enzyme Length 700
Uniprot Accession Number P17655
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 CA_BIND 585..596; /note=1; CA_BIND 615..626; /note=2
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' (PubMed:17650508). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs (By similarity). {ECO:0000250|UniProtKB:O08529, ECO:0000269|PubMed:17650508}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (2); Beta strand (42); Calcium binding (2); Chain (1); Domain (4); Helix (27); Initiator methionine (1); Metal binding (25); Modified residue (1); Natural variant (6); Propeptide (1); Region (3); Sequence caution (2); Sequence conflict (5); Turn (7)
Keywords 3D-structure;Acetylation;Alternative splicing;Calcium;Cell membrane;Cytoplasm;Direct protein sequencing;Hydrolase;Membrane;Metal-binding;Protease;Reference proteome;Repeat;Thiol protease
Interact With P04632; P55212; P13473-2; O60356; P07237; P60201-2; O75400-2; P62826; Q9P1I4; Q8IUH5
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:22814378
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 1KFU; 1KFX; 2NQA;
Mapped Pubmed ID 10830966; 11023826; 11483505; 11853546; 11909964; 12000759; 12070670; 12150984; 12783889; 12843408; 14688278; 14976200; 14980313; 14993287; 15302874; 15471877; 15817486; 15950654; 16310784; 16361262; 16436382; 16530191; 16598790; 16652152; 16816119; 17192410; 17261541; 17359359; 17596297; 17608959; 18032503; 18340456; 18519038; 18568448; 19074885; 19422794; 19720936; 19752040; 19756344; 19861418; 19913121; 19946123; 20041182; 20070945; 20150423; 20193680; 20379614; 20453000; 20618160; 20628086; 20729206; 20730561; 20924799; 21030783; 21086148; 21117903; 21152086; 21185840; 21374734; 21670566; 21839844; 21864727; 21994455; 22064597; 22435971; 22623320; 22629380; 22711986; 22745213; 23035980; 23140395; 23389291; 23395904; 23466492; 23538341; 23606334; 23733271; 23889979; 23940116; 24705354; 25944670; 26248159; 26358320; 26496610; 26974350; 27077802; 27099352; 27121057; 27123462; 27277673; 27456359; 28112201; 28235949; 28280729; 29099266; 29115452; 29425806; 29909039; 30106446; 30177525; 30177812; 30417356; 30448882; 31634637; 31680308; 33078830; 34191270; 34381117; 7698360; 9228946; 9407132;
Motif
Gene Encoded By
Mass 79,995
Kinetics
Metal Binding METAL 89; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; 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:0000250; METAL 587; /note=Calcium 6; /evidence=ECO:0000250; METAL 589; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250; METAL 591; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250; METAL 596; /note=Calcium 6; /evidence=ECO:0000250; METAL 615; /note=Calcium 7; /evidence=ECO:0000250; METAL 617; /note=Calcium 7; /evidence=ECO:0000250; METAL 619; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250; METAL 621; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250; METAL 626; /note=Calcium 7; /evidence=ECO:0000250; METAL 658; /note=Calcium 1; /evidence=ECO:0000250; METAL 661; /note=Calcium 1; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda 3.4.22.53;