Detail Information for IndEnz0002003940
IED ID IndEnz0002003940
Enzyme Type ID protease003940
Protein Name Calpain-2 catalytic subunit
EC 3.4.22.53
Calcium-activated neutral proteinase 2
CANP 2
Calpain M-type
Calpain-2 large subunit
Millimolar-calpain
M-calpain
Fragment
Gene Name CAPN2
Organism Oryctolagus cuniculus (Rabbit)
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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit)
Enzyme Sequence QKLIRIRNPWGEVEWTGRWNDNCPNWNTVDPEVRERLAERHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYVIKLEEEDEDQEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELRGQTNIHLGKNFFLTTRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKNGDFCVRVFSEKKADYQAVDDEIEADLEEADVSEDDIDDGFRRLFAQLAGEDAEISAFELQNILRRVLAKRQDIKTDGLSIETCKIMVDMLDSDGTGKLGLKEFYVLWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHEVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPDNTGMIQLDLISWLCFSVL
Enzyme Length 422
Uniprot Accession Number P06814
Absorption
Active Site ACT_SITE 8; /evidence="ECO:0000255|PROSITE-ProRule:PRU00239, ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090"
Activity Regulation ACTIVITY REGULATION: Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.
Binding Site
Calcium Binding CA_BIND 307..318; /note=1; /evidence=ECO:0000269|PubMed:3038855; CA_BIND 337..348; /note=2; /evidence=ECO:0000269|PubMed:3038855
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'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs. {ECO:0000250|UniProtKB:O08529, ECO:0000250|UniProtKB:P17655}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Calcium binding (2); Chain (1); Domain (4); Metal binding (19); Non-terminal residue (1); Region (3)
Keywords Calcium;Cell membrane;Cytoplasm;Hydrolase;Membrane;Metal-binding;Protease;Reference proteome;Repeat;Thiol protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 49,494
Kinetics
Metal Binding METAL 14; /note=Calcium 4; /evidence=ECO:0000250; METAL 21; /note=Calcium 4; /evidence=ECO:0000250; METAL 45; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 264; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 267; /note=Calcium 5; /evidence=ECO:0000250; METAL 269; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 274; /note=Calcium 5; /evidence=ECO:0000250; METAL 307; /note=Calcium 6; /evidence=ECO:0000250; METAL 309; /note=Calcium 6; /evidence=ECO:0000250; METAL 311; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250; METAL 313; /note=Calcium 6; via carbonyl oxygen; /evidence=ECO:0000250; METAL 318; /note=Calcium 6; /evidence=ECO:0000250; METAL 337; /note=Calcium 7; /evidence=ECO:0000250; METAL 339; /note=Calcium 7; /evidence=ECO:0000250; METAL 341; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250; METAL 343; /note=Calcium 7; via carbonyl oxygen; /evidence=ECO:0000250; METAL 348; /note=Calcium 7; /evidence=ECO:0000250; METAL 380; /note=Calcium 1; /evidence=ECO:0000250; METAL 383; /note=Calcium 1; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda 3.4.22.53;