| IED ID | IndEnz0002004892 |
| Enzyme Type ID | protease004892 |
| Protein Name |
Cathepsin Z EC 3.4.18.1 Cathepsin P Cathepsin X |
| Gene Name | CTSZ |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MARRGPGWRPLLLLVLLAGAAQGGLYFRRGQTCYRPLRGDGLAPLGRSTYPRPHEYLSPADLPKSWDWRNVDGVNYASITRNQHIPQYCGSCWAHASTSAMADRINIKRKGAWPSTLLSVQNVIDCGNAGSCEGGNDLSVWDYAHQHGIPDETCNNYQAKDQECDKFNQCGTCNEFKECHAIRNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATERLANYTGGIYAEYQDTTYINHVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIVTSTYKDGKGARYNLAIEEHCTFGDPIV |
| Enzyme Length | 303 |
| Uniprot Accession Number | Q9UBR2 |
| Absorption | |
| Active Site | ACT_SITE 92; /evidence="ECO:0000305|PubMed:10656802, ECO:0000305|PubMed:10745011"; ACT_SITE 241; /evidence="ECO:0000305|PubMed:10656802, ECO:0000305|PubMed:10745011"; ACT_SITE 261; /evidence="ECO:0000305|PubMed:10656802, ECO:0000305|PubMed:10745011" |
| Activity Regulation | ACTIVITY REGULATION: The disulfide bridge formed between Cys-33 in the propeptide and the active site residue Cys-92 may prevent activation of the zymogen through formation of a reversible covalent bond with the active site residue. {ECO:0000305|PubMed:10656802}. |
| 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:10504234}; |
| DNA Binding | |
| EC Number | 3.4.18.1 |
| Enzyme Function | FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (PubMed:10504234). Capable of producing kinin potentiating peptides (By similarity). {ECO:0000250|UniProtKB:Q9R1T3, ECO:0000269|PubMed:10504234}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (14); Chain (1); Disulfide bond (6); Glycosylation (2); Helix (10); Natural variant (3); Propeptide (1); Sequence conflict (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Disulfide bond;Glycoprotein;Hydrolase;Lysosome;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
| Interact With | Q9BYV9; Q8N9N5-2; A8MQ03; Q5TD97; O75031; Q92764; Q6A162; Q07627; P60014; Q9BYR9; Q9BYR6; P26371; Q9UJV3-2; Q5JR59; Q7Z3S9; P0DPK4; O15162; Q63HR2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1DEU; 1EF7; |
| Mapped Pubmed ID | 10394364; 10559958; 10652252; 10679020; 10747087; 10825291; 10903204; 10982397; 11035026; 11285137; 11306556; 11604418; 11694590; 11927603; 11994746; 12235121; 15680921; 16129679; 16155256; 16303754; 16624868; 17005010; 17038314; 17065156; 17116749; 17192411; 17287728; 17316621; 17601350; 18025080; 18283111; 18420963; 18843296; 18977241; 19164740; 19638414; 19656848; 19800993; 20477988; 20533886; 20545907; 20679433; 20966969; 21310951; 21354459; 21368909; 21454358; 21478858; 21516116; 21532587; 21616554; 21966391; 22013193; 22157747; 22451661; 22675024; 23378591; 23479643; 23650620; 23698585; 23827504; 24119662; 24725597; 24917561; 25406594; 25416956; 25433997; 25442015; 25586378; 25619252; 26496610; 28495172; 29795304; 30018008; 30046941; 30087368; 31090199; 34378678; 8374173; 8524399; 8663406; 8670264; 9094723; 9150144; 9307973; 9395526; 9647643; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,868 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.18.1; |