| IED ID | IndEnz0002004887 |
| Enzyme Type ID | protease004887 |
| Protein Name |
Cathepsin Z-1 EC 3.4.18.1 |
| Gene Name | cpz-1 F32B5.8 |
| 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 | MRTFVLLLALCAICILASSAYGKVRKYSNRNRYNLKGCYKQTGRVFEHKRYDRIYETEDFDSEDLPKTWDWRDANGINYASADRNQHIPQYCGSCWAFGATSALADRINIKRKNAWPQAYLSVQEVIDCSGAGTCVMGGEPGGVYKYAHEHGIPHETCNNYQARDGKCDPYNRCGSCWPGECFSIKNYTLYKVSEYGTVHGYEKMKAEIYHKGPIACGIAATKAFETYAGGIYKEVTDEDIDHIISVHGWGVDHESGVEYWIGRNSWGEPWGEHGWFKIVTSQYKNAGSKYNLKIEEDCVWADPIV |
| Enzyme Length | 306 |
| Uniprot Accession Number | G5EGP8 |
| Absorption | |
| Active Site | ACT_SITE 95; /evidence=ECO:0000250|UniProtKB:Q9UBR2; ACT_SITE 243; /evidence=ECO:0000250|UniProtKB:Q9UBR2; ACT_SITE 265; /evidence=ECO:0000250|UniProtKB:Q9UBR2 |
| Activity Regulation | ACTIVITY REGULATION: The disulfide bridge formed between Cys-38 in the propeptide and the active site residue Cys-95 may prevent activation of the zymogen through formation of a reversible covalent bond with the active site residue. {ECO:0000250|UniProtKB:Q9UBR2}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.; EC=3.4.18.1; Evidence={ECO:0000250|UniProtKB:Q9UBR2}; |
| DNA Binding | |
| EC Number | 3.4.18.1 |
| Enzyme Function | FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (PubMed:14630920). Probably, required for the degradation of the old cuticle (PubMed:14630920). {ECO:0000250|UniProtKB:Q9UBR2, ECO:0000269|PubMed:14630920}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (6); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Alternative splicing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14630920, ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:16857685}. Note=In molting larvae, localizes in both the new and old cuticles, specifically at the interface where the old cuticle is being degraded before ecdysis (PubMed:14630920). Localizes to yolk granules in the developing oocyte (PubMed:16857685). {ECO:0000269|PubMed:14630920, ECO:0000269|PubMed:16857685}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11099033; 11685900; 14704431; 16439208; 21085631; 21177967; 21367940; 22560298; 23800452; 25487147; 26009280; 29348603; 30140741; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,741 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |