| IED ID | IndEnz0002005900 |
| Enzyme Type ID | protease005900 |
| Protein Name |
Carboxypeptidase Z CPZ EC 3.4.17.- |
| Gene Name | Cpz |
| 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 | MPTTPLLLAALAALAALAVAAYPSCSPGPDPSGKCQRLASTHSATCVDLHLRTCADAAYNHTSFPTPLEHRSWEAVEASPEYTLLGVLHFLLEGQCNPDLRLLGCSVLAPRCQGGHTQRPCRRVCEGLREACQPAFDAIDMAWPYFLDCTQYFAPEEEGCYDPLEQLRGELDVEEALPSGLPPTFIRFAHHSYAQMVRVLKRTAARCSQVAKTYSIGRSFEGKDLVVIEFSSRPGQHELMEPEVKLIGNIHGNEVAGREILIYLAQYLCSEYLLGNPRIQRLLNTTRIHLLPSMNPDGYEVAAAEGAGYNGWTSGRQNAQNLDLNRNFPDLTSEYYRLASTRGVRTDHIPISQYYWWGKVAPETKAIMKWIQTIPFVLSASLHGGDLVVSYPFDFSKHPHEEKMFSPTPDEKMFKLLARAYADVHPMMMDRSENRCGGNFLKRGSIINGADWYSFTGGMSDFNYLHTNCFEITVELGCVKFPPEEALYGLWQHNKEPLLNFLEMVHRGIKGVVTDKYGKPVKNARILVKGIRHDVTTAPDGDYWRLLPPGSHIVIAQAPGYSKVMKRVTIPLRMKRAGRVDFILQPLGTGPKNFLPGPSRALPRSLDPQGAPAQLDFEPPRARRQPASGSKPWWWAYFTSLSPHKPRWLLKY |
| Enzyme Length | 652 |
| Uniprot Accession Number | O54858 |
| Absorption | |
| Active Site | ACT_SITE 475; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14384 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid (MGTA) and guanidinoethylmercaptosuccinic acid (GEMSA). Inhibited by chelating agents such as EDTA and EGTA (By similarity). {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.17.- |
| Enzyme Function | FUNCTION: Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (2); Metal binding (3); Region (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Carboxypeptidase;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Wnt signaling pathway;Zinc |
| Interact With | |
| Induction | INDUCTION: By Alachlor. {ECO:0000269|PubMed:12419858}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10671522}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18847325; |
| Motif | |
| Gene Encoded By | |
| Mass | 73,082 |
| Kinetics | |
| Metal Binding | METAL 251; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 254; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 383; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | |
| Cross Reference Brenda |