Detail Information for IndEnz0002019207
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;