IED ID | IndEnz0002019207 |
Enzyme Type ID | protease019207 |
Protein Name |
Calpain-8 EC 3.4.22.53 New calpain 2 nCL-2 Stomach-specific M-type calpain |
Gene Name | Capn8 Ncl2 |
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 | MAALAAGISKQRAAAQGLGSNQNAVKYLGQDFETLRKQCLNSGVLFKDPEFPACPSALGYRDLGPGSAETQGIIWKRPTELCSNPQFIVGGATRTDIRQGGLGDCWLLAAIASLTLNEKLLYRVVPRDQSFQKNYAGIFHFQFWQYGEWVEVVIDDRLPTKNGQLLFLHSEEGNEFWSALLEKAYAKLNGSYEALAGGSTIEGFEDFTGGISEFYDLRKPPGNLYYTIQKALRKGSLLGCSIDVSNAAEAEATTRQKLVKGHAYSVTGVEEVDFRGLPEKLIRLRNPWGEVEWTGAWSDSAPEWNYIDPQKKGELDKRAEDGEFWMSFSDFLKQFSRLEICNLSPDSLSSEEIHKWNLVLFNGRWTRGSTAGGCQNYPATYWTNPQFKIHLDEVDEDQEEGTSEPCCTVLLGLMQKNRRRQRRIGQGMLSIGYAVYQIPKELENHTDEHLGRDFFQGRQPSTCSSTYMNLREVSSRVQLPPGQYLVVPSTFEPFKDGDFCLRVFSEKKAQALEIGDAVPGDPHEPHPRDMDGEDEHFWSLSEEFADKDSEISAHQLKRVLNGLLSKRTDMKFDGFNINTCREMISLLDGDGTGSLRPVEFKTLWLKICKYLEIYQEMDHSRAGTIDAHEMRTALKKAGFTLNNQVQQTIATRYACSKLGVDFDGFVACMIRLEILFKLFRLLDKDQNGIVQLSLAEWLCRALV |
Enzyme Length | 703 |
Uniprot Accession Number | Q91VA3 |
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: The concentration of calcium for half-maximal activity is 0.3 mM. Inhibited by calpastatin and calpeptin. {ECO:0000269|PubMed:17646163}. |
Binding Site | |
Calcium Binding | CA_BIND 588..599; /note=1; /evidence=ECO:0000255; CA_BIND 618..629; /note=2; /evidence=ECO:0000255 |
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 (By similarity). Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. Proteolytically cleaves the beta-subunit of coatomer complex. {ECO:0000250, ECO:0000269|PubMed:16476741}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 20 degrees Celsius. {ECO:0000269|PubMed:17646163}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:17646163}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (2); Calcium binding (2); Chain (1); Domain (5); Mutagenesis (1); Region (3); Sequence conflict (5) |
Keywords | Alternative splicing;Autocatalytic cleavage;Calcium;Cytoplasm;Golgi apparatus;Hydrolase;Metal-binding;Protease;Reference proteome;Repeat;Thiol protease |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:16476741}. |
Modified Residue | |
Post Translational Modification | PTM: Undergoes autolytic cleavage between Ala-5 and Ala-6 which gives rise to fragments extending from Ala-6 to the C-terminus, Ala-6 to the EF-hand 2 domain and from Ala-6 to the beginning of domain III. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 16141072; 19416960; 20686710; 24194600; 27626380; 27881674; |
Motif | |
Gene Encoded By | |
Mass | 79,335 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.22.B28; |