| IED ID | IndEnz0002015296 |
| Enzyme Type ID | protease015296 |
| Protein Name |
Calpastatin Calpain inhibitor |
| Gene Name | Cast |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSRPGPKPAASSRPRRGAAASHTQEHVNEKNIGSSSKPAEKKGSDEVTASSAATGTSPRMSTTGAKAVKIESEKSQSSEPPVIHEKKPKGKPKEGSEPQTLPKHASDTGSKHAHKEKALSRSNEQIVSEKSSESKTKFQDAPSADGESVAGGVTVATASDKVVVKKKEKKSLTPTLPMESTLNKLSDKSGVNAALDDLIDTLGECEDTNKDDPPYTGPVVLDPMDSTYLEALGIKEGTIPPEYRKLLEKNEAITGPLPDSPKPMGIDHAIDALSSDFTCSSPTGKQTEKEKSTGESSKAQSAGVTRSAVPPQEKKRKVEEEVMNDQALQALSDSLGTRQPDPQSHLRQAKQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKCLSESELIGELSADFVQPTYQEKPSMPAAKIKKGVVPDDAVETLARSLGTRKEDPEDEKSLVDKVKEKAKEEDHEKLGEKEETIPPDYRLEIVKDKDGKPLLPKEAEEQLPPLSDDFLLDALSQDFSSPANILSLGFEDAKLSAAVSETVSQVPAPSNHTAAPPPGTERRDKELDDALDELSDSLGQRQPDPDENKPLDDKVKEKIKAEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPLTKNTEKLGQDQDPIDALSEDLDSCPPTTETSQNTTKEKGKKTSSSKASKNEEKTKDSSKKTEEVPKPKVDEDAT |
| Enzyme Length | 713 |
| Uniprot Accession Number | P27321 |
| 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 (4); Chain (1); Compositional bias (8); Cross-link (1); Erroneous initiation (6); Frameshift (1); Helix (8); Modified residue (15); Mutagenesis (2); Region (4); Repeat (4); Sequence conflict (20); Turn (1) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Isopeptide bond;Phosphoprotein;Protease inhibitor;Reference proteome;Repeat;Thiol protease inhibitor;Ubl conjugation |
| Interact With | Q07009 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 57; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 86; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P51125; MOD_RES 122; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 171; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 173; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 260; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 281; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 401; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 403; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 410; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 445; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 521; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 532; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 580; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 582; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3BOW; 3DF0; |
| Mapped Pubmed ID | 10318818; 10601010; 10639123; 11035539; 11893336; 12482022; 12665854; 12684003; 12832042; 15132950; 15307896; 15453993; 15491615; 15543935; 15563579; 15904894; 16388007; 16467455; 16871587; 16997608; 17429681; 17543955; 17712625; 18544539; 18599308; 18809371; 19318376; 19751724; 20116408; 20393603; 27626661; |
| Motif | |
| Gene Encoded By | |
| Mass | 77,313 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |