| IED ID | IndEnz0002004757 |
| Enzyme Type ID | protease004757 |
| Protein Name |
Cathepsin Z EC 3.4.18.1 Cathepsin Y |
| Gene Name | Ctsz Ctsy |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MASSGSVQQLRLVLLMLLLAGAARASLYFRPGQTCYRPLHRDHLALLGRRTYPRPHEYLSPADLPKNWDWRNVNGVNYASVTRNQHIPQYCGSCWAHGSTSALADRINIKRKGAWPSTLLSVQNVIDCGNAGSCEGGNDLPVWEYAHKHGIPDETCNNYQAKDQECDKFNQCGTCTEFKECHTIQNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATERMSNYTGGIYTEYQNQAIINHIISVAGWGVSNDGIEYWIVRNSWGEPWGERGWMRIVTSTYKGGTGSSYNLAIEEACTFGDPIV |
| Enzyme Length | 306 |
| Uniprot Accession Number | Q9R1T3 |
| Absorption | |
| Active Site | ACT_SITE 94; /evidence=ECO:0000255|PROSITE-ProRule:PRU10090; ACT_SITE 243; /evidence=ECO:0000255|PROSITE-ProRule:PRU10090; ACT_SITE 264; /evidence=ECO:0000255|PROSITE-ProRule:PRU10090 |
| Activity Regulation | ACTIVITY REGULATION: The disulfide bridge formed between Cys-35 in the propeptide and the active site residue Cys-94 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:0000269|PubMed:10615013, ECO:0000269|PubMed:12553736}; |
| DNA Binding | |
| EC Number | 3.4.18.1 |
| Enzyme Function | FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (PubMed:12553736, PubMed:10615013). Capable of producing kinin potentiating peptides (PubMed:10615013). {ECO:0000269|PubMed:10615013, ECO:0000269|PubMed:12553736}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Glycosylation (2); Propeptide (1); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18700000; 19433310; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,194 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.6 uM for the synthetic substrate Z-Phe-Arg-NMec {ECO:0000269|PubMed:12553736}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |