| IED ID | IndEnz0002015293 |
| Enzyme Type ID | protease015293 |
| Protein Name |
Calpastatin Calpain inhibitor |
| Gene Name | Cast |
| 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 | MSQPGPKPAASPRPSRGAAARHTQEHVNEKNIGSSSKPGEKKGSDEKKAASLGSSQPSRPHVGEAATATKVTASSAATSKSPSMSTTETKAIPVNKQLEGPDQKRPREQAVKTESKKPQSSEQPVVHEKKSKGGPKEGSEPKNLPKHTSSTGSKHAHKEKALSRSNEQMVSEKPSESKTKFQDVPSAGGESVAGGGTVATALDKVVGKKKEQKPFTPASPVQSTPSKPSDKSGMDAALDDLIDTLGGHEDTNRDDPPYTGPVVLDPMYSTYLEALGIKEGTIPPEYRKLLEKNEGITQPLPDSPKPMGTDQAIDALSSDFTCSSPTGKQSEKEKSTGEIFKAQSAGVTRSSVPPKEKKRKVEEEVINDQALQALSDSLGTRQPDPPSHVSQAEQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKSLSESELIGELSADFDRSTYQDKPSTPAEKKSNDTSQTPPGETVPRASMCSIRSAPPKLASLKGVVPEDAVETLAGSLGTREADPEHEKTVEDKVKEKAKEEEHEKLGEKEETVPPDYRLEEVKDKDGKPLLPKESQEQLAPLSDDFLLDALSQDFSSPANISSLEFEDAKLSAAISEVVSQTPAPSTHAAAPLPGTEQKDKELDDALDELSDSLGQRPPDPDENKPLDDKVKEKIKPEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPPTKKTEKPDQDRDPIDALSEDLDSCPSTTETSKNTAKGKSKKTSSSKASKDGEKTKDSSKKTEEVSKPKAKEDARHS |
| Enzyme Length | 788 |
| Uniprot Accession Number | P51125 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (8); Chain (1); Compositional bias (14); Cross-link (1); Modified residue (16); Region (4); Repeat (4) |
| Keywords | Acetylation;Alternative splicing;Isopeptide bond;Phosphoprotein;Protease inhibitor;Reference proteome;Repeat;Thiol protease inhibitor;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19131326"; MOD_RES 129; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 165; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 216; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P27321"; MOD_RES 219; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"; MOD_RES 303; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 324; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810"; MOD_RES 444; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810"; MOD_RES 446; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810"; MOD_RES 453; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810"; MOD_RES 479; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"; MOD_RES 518; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810"; MOD_RES 594; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810"; MOD_RES 605; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810"; MOD_RES 653; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810"; MOD_RES 655; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P20810" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11090425; 11217851; 11673859; 11952156; 12466851; 12520002; 14996907; 15223839; 15691848; 15699033; 15863237; 16141072; 16496301; 16602821; 16615898; 16635246; 16705056; 16927317; 17513017; 17640526; 17853947; 18258859; 18799693; 18803809; 19318376; 19683220; 19880516; 20661225; 21099278; 21267068; 21268016; 21338355; 21791606; 21849499; 21982763; 22173972; 23100324; 23250437; 23455548; 23565252; 23986532; 23986533; 24194600; 24210906; 24333421; 24619358; 24728269; 24891510; 25026177; 25648699; 25698931; 25786109; 26248159; 26453333; 26747784; 26756888; 26974350; 27626380; 27656030; 28386216; 28700664; 29089532; 29355642; 29996090; 30190286; 30199285; 32251313; 34197232; 34440632; 34489447; 9473662; |
| Motif | |
| Gene Encoded By | |
| Mass | 84,922 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |