CPZ (gene)

From Wikipedia, the free encyclopedia

Carboxypeptidase Z

Identifiers

CPZ; MGC99682

External IDs

OMIM: 603105 MGI: 88487 HomoloGene: 2709

Gene ontology
Molecular Function:	• carboxypeptidase A activity • metallopeptidase activity • zinc ion binding • metal ion binding
Cellular Component:	• proteinaceous extracellular matrix
Biological Process:	• proteolysis • Wnt receptor signaling pathway

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001014447 (mRNA)
NP_001014447 (protein)

XM_994610 (mRNA)
XP_999704 (protein)

Location

Chr 4: 8.65 - 8.67 Mb

Chr 5: 35.82 - 35.84 Mb

Pubmed search

[1]

[2]

Carboxypeptidase Z, also known as CPZ, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CPZ carboxypeptidase Z.

[edit] 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. PMID 11766880.
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. 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. 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. 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. 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.
Song L, Fricker LD (1997). "Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase.". J. Biol. Chem. 272 (16): 10543-50. PMID 9099699.