| IED ID | IndEnz0002018971 |
| Enzyme Type ID | protease018971 |
| Protein Name |
Cathepsin Z EC 3.4.18.1 L3 cysteine protease LOVCP |
| Gene Name | cpz |
| Organism | Onchocerca volvulus |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Spirurina Spiruromorpha Filarioidea Onchocercidae Onchocerca Onchocerca volvulus |
| Enzyme Sequence | MLAILFNFFLLTYFTNITLGKVGKSIDLDTRNGYNVHGCYKQTGKIYAHKTYPRQYEAENYNFDDLPVAWDWRNINGVNYASVDRNQHIPQYCGSCWAFGSTSALADRFNIKRKGAWPPAYLSVQEVIDCANAGSCEGGEPGPVYKYAHEFGIPHETCNNYQARDGTCSSYNKCGSCWPGSCFSIKNYTIYRVKNYGAVSGLHKMKAEIYHHGPIACGIAATKAFETYAGGIYNERTNEDIDHIISAHGWGVDSESGVPYWIGRNSWGTPWGENGWFRIVTSEYKNSSSKYNLKIEEDCVWADPIA |
| Enzyme Length | 306 |
| Uniprot Accession Number | Q6PN98 |
| Absorption | |
| Active Site | ACT_SITE 96; /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-39 in the propeptide and the active site residue Cys-96 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 (Probable) (PubMed:15555728). Required for the degradation and shedding of the old cuticle (Probable) (PubMed:15555728). {ECO:0000250|UniProtKB:Q9UBR2, ECO:0000269|PubMed:15555728, ECO:0000305|PubMed:8939969}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Glycosylation (2); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:8939969}. Secreted {ECO:0000269|PubMed:8939969}. Note=Localizes in secretory vesicles in the hypodermis of L3 larvae. {ECO:0000269|PubMed:8939969}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,424 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |