Detail Information for IndEnz0002018861
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