CPZ (gene)

CPZ
Identifiers
Aliases	CPZ, carboxypeptidase Z
External IDs	OMIM: 603105; MGI: 88487; HomoloGene: 2709; GeneCards: CPZ; OMA:CPZ - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4p16.1 Start 8,592,660 bp End 8,619,759 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 B3 Start 35,659,562 bp End 35,683,042 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left ovary right ovary placenta gallbladder canal of the cervix ectocervix stromal cell of endometrium vagina uterine tube right uterine tube Top expressed in body of femur calvaria molar skin of back lens urethra vestibular sensory epithelium cornea skin of abdomen embryo More reference expression data BioGPS More reference expression data
Gene ontology Molecular function carboxypeptidase activity zinc ion binding peptidase activity hydrolase activity metallopeptidase activity metal ion binding metallocarboxypeptidase activity serine-type carboxypeptidase activity Cellular component extracellular region extracellular space Biological process protein processing Wnt signaling pathway proteolysis peptide metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8532 242939 Ensembl ENSG00000109625 ENSMUSG00000036596 UniProt Q66K79 Q8R4V4 RefSeq (mRNA) NM_003652 NM_001014447 NM_001014448 NM_153107 RefSeq (protein) NP_001014447 NP_001014448 NP_003643 NP_694747 Location (UCSC) Chr 4: 8.59 – 8.62 Mb Chr 5: 35.66 – 35.68 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Carboxypeptidase Z is an enzyme that in humans is encoded by the CPZ gene.

This gene encodes a member of the metallocarboxypeptidase family. This enzyme displays carboxypeptidase activity towards substrates with basic C-terminal residues. It is most active at neutral pH and is inhibited by active site-directed inhibitors of metallocarboxypeptidases. Alternative splicing in the coding region results in multiple transcript variants encoding different isoforms.

External links

• Human CPZ genome location and CPZ gene details page in the UCSC Genome Browser.

Further reading

• Reznik SE, Fricker LD (2002). "Carboxypeptidases from A to z: implications in embryonic development and Wnt binding". Cell. Mol. Life Sci. 58 (12–13): 1790–804. doi:10.1007/PL00000819. PMC 11337317. PMID 11766880. S2CID 22530649.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Fan X, Olson SJ, Blevins LS, et al. (2003). "Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary". J. Histochem. Cytochem. 50 (11): 1509–16. doi:10.1177/002215540205001111. PMID 12417617.
• Novikova EG, Reznik SE, Varlamov O, Fricker LD (2000). "Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues". J. Biol. Chem. 275 (7): 4865–70. doi:10.1074/jbc.275.7.4865. PMID 10671522.
• Novikova EG, Fricker LD (1999). "Purification and characterization of human metallocarboxypeptidase Z.". Biochem. Biophys. Res. Commun. 256 (3): 564–8. doi:10.1006/bbrc.1999.0378. PMID 10080937.