| IED ID | IndEnz0002006018 |
| Enzyme Type ID | protease006018 |
| Protein Name |
Caspase A EC 3.4.22.36 Cleaved into: Caspase A subunit p16; Caspase A subunit p14 |
| Gene Name | csp-1 Y48E1B.13 |
| 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 | MVLKTIEDNCKSQFDDDLVEDFNNFQTTSSMSSSTTISTEDFNTIEIESTFEICRSGSYTEEPILGENDEFLIDFEMERFLKFLKDKTKQVEKRKEPFSQKEIYAVFQRRIKSELCIETVKKKFQPLLPNAIQTCEFDEETMIRMIYGAGIRIDSVDFWNRFTSKATISLDCYSRLISYSSDSLTLSGTHRSGFTYHWISTPPVTYHRTENKDPNIQEPSPVEFLDVQSSLGSSMKPPILDKPTKLDDPAETRHDCSYSLEEYDSQSRMPRTDAKKSNHKHKYCYEMNSNPRGTVLILSNENFKNMERRVGTKQDEVNLTKLFQKLQYTVICKRNLEAESMLEAIKEFAEMAHTDSIILFLLSHGDGAGSVFGIDDMPVNVMEVSTYLAYHQNLLLKPKWVAVSACRGGKLNMGVPVDGLPALEDKCAPISKFWNLMMSRIMPGTFTSLNADVIISFSTTDGFTSYRDEEAGTWYIKSMCKVFNKHSKTMHLLDILTETGRNVVTKYENVQGNVVLKQAPEILSRLTKQWHFSRSM |
| Enzyme Length | 536 |
| Uniprot Accession Number | G5EBM1 |
| Absorption | |
| Active Site | ACT_SITE 364; /evidence=ECO:0000250|UniProtKB:P29466; ACT_SITE 406; /evidence=ECO:0000269|PubMed:9857046 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by cysteine protease inhibitor iodoacetic acid (CH3COOI) but not by N-[N-(L-3-transcarboxirane-2-carbonyl)-leucyl]-agmatine (E-64) or benzyloxycarbonyl-DEVD-fluoro-methyl ketone (Z-DEVD-FMK). {ECO:0000269|PubMed:9857046}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.; EC=3.4.22.36; Evidence={ECO:0000269|PubMed:9857046}; |
| DNA Binding | |
| EC Number | 3.4.22.36 |
| Enzyme Function | FUNCTION: Cysteine protease which, in vitro, cleaves itself and caspase ced-3 into their mature active forms (PubMed:9857046). Also cleaves, in vitro, inactive caspase csp-2 isoform b (PubMed:9857046). Required maternally to induce apoptosis in a subset of cells fated to die during embryogenesis, mostly independently of the ced-9, ced-4 and ced-3 canonical apoptosis pathway (PubMed:23505386). Involved in the degeneration of dopaminergic CEP neurons in response to high Mn(2+) levels (PubMed:23721876). {ECO:0000269|PubMed:23505386, ECO:0000269|PubMed:23721876, ECO:0000269|PubMed:9857046}.; FUNCTION: [Isoform a]: Dispensable for regulating apoptosis during embryogenesis. {ECO:0000269|PubMed:23505386}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (3); Chain (2); Mutagenesis (1); Propeptide (1) |
| Keywords | Alternative splicing;Apoptosis;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Autocatalytic cleavage removes the propeptide and generates the two active subunits p16 and p14 in vitro. Cannot be cleaved by ced-3 in vitro. {ECO:0000269|PubMed:9857046}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12097347; 20439776; 21085631; 21367940; 22286215; 22560298; 23800452; 25487147; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,467 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |