| IED ID | IndEnz0002018861 |
| Enzyme Type ID | protease018861 |
| Protein Name |
Calpain clp-1 EC 3.4.22.- |
| Gene Name | clp-1 C06G4.2 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MADDEEEIIQKVEVKPDEFNGLIGSIAGNLIRDKVGGAGGDILGGLASNFFGGGGGGGGGGGGGGFGGGNGGFGGGSNYDQGGNGNSGDQQKRKRDMAKDLIGGIFDNVVNRKGKKEQDNYGGGGNYGGGGGNQGGGGGGGFNFNDIGGLINSMGGGGGGGQRQGGGGGGFGDILGGIGSLIGGGGGGQYNGGGGNVNPNNLNGGMVNVIGNLIGEAAHRFLGVDPGTGRIIGAVAGNVIMGLGGKDNSLGNIGKVILDNIISGKFRRDVDPFVRPGPDPDRGGGGSGPSPISPRPTTEPQDFYELRDQCLESKRLFEDPQFLANDSSLFFSKRPPKRVEWLRPGEITREPQLITEGHSRFDVIQGELGDCWLLAAAANLTLKDELFYRVVPPDQSFTENYAGIFHFQFWQYGKWVDVVIDDRLPTSNGELLYMHSASNNEFWSALLEKAYAKLFGSYEALKGGTTSEALEDMTGGLTEFIDLKNPPRNLMQMMMRGFEMGSLFGCSIEADPNVWEAKMSNGLVKGHAYSITGCRIVDGPNGQTCILRIRNPWGNEQEWNGPWSDNSREWRSVPDSVKQDMGLKFDHDGEFWMSFDDFMRNFEKMEICNLGPDVMDEVYQMTGVKAAGMVWAANTHDGAWVRNQTAGGCRNYINTFANNPQFRVQLTDSDPDDDDELCTVIFAVLQKYRRNLKQDGLDNVPIGFAVYDAGNNRGRLSKQFFAANKSAMRSAAFINLREMTGRFRVPPGNYVVVPSTFEPNEEAEFMLRVYTNGFIESEEL |
| Enzyme Length | 780 |
| Uniprot Accession Number | P34308 |
| Absorption | |
| Active Site | ACT_SITE 371; /evidence=ECO:0000250|UniProtKB:Q07009; ACT_SITE 527; /evidence=ECO:0000250|UniProtKB:Q07009; ACT_SITE 551; /evidence=ECO:0000250|UniProtKB:Q07009 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates (By similarity). Required for assembly and maintenance of integrin attachment complexes which are essential for maintenance of adult muscle (PubMed:22253611). Proteolytic activity is activated in response to increased intracellular Ca(2+) levels during cell degeneration and promotes necrotic cell death (PubMed:12410314, PubMed:22479198). {ECO:0000250|UniProtKB:P07384, ECO:0000269|PubMed:12410314, ECO:0000269|PubMed:22253611, ECO:0000269|PubMed:22479198}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (6); Chain (1); Domain (1); Region (1) |
| Keywords | Alternative splicing;Cytoplasm;Hydrolase;Protease;Reference proteome;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:22479198}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:22479198}. Note=In body wall muscle cells, localizes at M-lines extending over the H-zone, and at adhesion plaques which form between adjacent cells. {ECO:0000269|PubMed:22479198}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11381264; 15338614; 16636145; 17164286; 17486083; 17850180; 17889653; 17901876; 19343510; 20439776; 21085631; 21177967; 21367940; 22157748; 22286215; 22347378; 22560298; 23800452; 24813946; 25487147; 25491313; 25635455; 27153400; 29348603; |
| Motif | |
| Gene Encoded By | |
| Mass | 83,643 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |