CPZ (gene)

Carboxypeptidase Z is an enzyme that in humans is encoded by the CPZ gene.[5][6]

CPZ
Identifiers
Aliases	CPZ, carboxypeptidase Z
External IDs	OMIM: 603105 MGI: 88487 HomoloGene: 2709 GeneCards: CPZ
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4p16.1 Start 8,592,660 bp[1] End 8,619,759 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 B2 Start 35,502,218 bp[2] End 35,525,698 bp[2]
RNA expression pattern 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 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: 35.5 – 35.53 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000109625 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000036596 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Song L, Fricker LD (May 1997). "Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase". J Biol Chem. 272 (16): 10543–50. doi:10.1074/jbc.272.16.10543. PMID 9099699.
6. "Entrez Gene: CPZ carboxypeptidase Z".

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. 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. 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.