| IED ID | IndEnz0002015292 |
| Enzyme Type ID | protease015292 |
| Protein Name |
Calpastatin Calpain inhibitor Sperm BS-17 component |
| Gene Name | CAST |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MNPTETKAIPVSQQMEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD |
| Enzyme Length | 708 |
| Uniprot Accession Number | P20810 |
| 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 (7); Chain (1); Compositional bias (9); Cross-link (1); Modified residue (20); Natural variant (4); Region (4); Repeat (4); Sequence caution (1); Sequence conflict (5) |
| Keywords | Acetylation;Alternative splicing;Isopeptide bond;Palmoplantar keratoderma;Phosphoprotein;Protease inhibitor;Reference proteome;Repeat;Thiol protease inhibitor;Ubl conjugation |
| Interact With | P16333; O35505 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 50; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:P51125"; MOD_RES 87; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P51125"; MOD_RES 133; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 135; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P27321"; MOD_RES 222; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P51125"; MOD_RES 243; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 364; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 366; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 373; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 440; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 516; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 527; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 563; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 575; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 577; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES P20810-5:11; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES P20810-6:11; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES P20810-7:11; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES P20810-9:11; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231"; MOD_RES P20810-10:11; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231" |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10830966; 11849768; 12843408; 17137217; 17474147; 17608959; 18519038; 19581569; 21030783; 21670566; 21864727; 23035980; 24462690; 26496610; 27626661; 7698360; |
| Motif | |
| Gene Encoded By | |
| Mass | 76,573 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |