CPM (gene)

Carboxypeptidase M
PDB rendering based on 1uwy.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1UWY​
Identifiers
Symbol	CPM
External IDs	OMIM: 114860 MGI: 1917824 HomoloGene: 35367 ChEMBL: 3038 GeneCards: CPM Gene
EC number	3.4.17.12
Gene ontology Molecular function • carboxypeptidase activity • metallocarboxypeptidase activity • zinc ion binding Cellular component • plasma membrane • cell surface • anchored component of membrane • extracellular exosome Biological process • proteolysis • anatomical structure morphogenesis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1368	70574
Ensembl	ENSG00000135678	ENSMUSG00000020183
UniProt	P14384	Q80V42
RefSeq (mRNA)	NM_001005502	NM_027468
RefSeq (protein)	NP_001005502	NP_081744
Location (UCSC)	Chr 12: 68.84 – 68.97 Mb	Chr 10: 117.63 – 117.69 Mb
PubMed search

Carboxypeptidase M is an enzyme that in humans is encoded by the CPM gene.^[1][2]

The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.^[2]

References

1. Kas K, Schoenmakers EF, Van de Ven WJ (Mar 1996). "Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15". Genomics 30 (2): 403–5. PMID 8586455.
2. "Entrez Gene: CPM carboxypeptidase M".

Further reading

• Fujiwara H, Imai K, Inoue T; et al. (1999). "Membrane-bound cell surface peptidases in reproductive organs.". Endocr. J. 46 (1): 11–25. doi:10.1507/endocrj.46.11. PMID 10426564.
• Rehli M, Krause SW, Andreesen R (2000). "The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo.". Adv. Exp. Med. Biol. 477: 205–16. doi:10.1007/0-306-46826-3_23. PMID 10849748.
• Nagae A, Deddish PA, Becker RP; et al. (1992). "Carboxypeptidase M in brain and peripheral nerves.". J. Neurochem. 59 (6): 2201–12. doi:10.1111/j.1471-4159.1992.tb10112.x. PMID 1431901.
• Tan F, Chan SJ, Steiner DF; et al. (1989). "Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N.". J. Biol. Chem. 264 (22): 13165–70. PMID 2753907.
• Skidgel RA, Davis RM, Tan F (1989). "Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones.". J. Biol. Chem. 264 (4): 2236–41. PMID 2914904.
• McGwire GB, Skidgel RA (1995). "Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M.". J. Biol. Chem. 270 (29): 17154–8. doi:10.1074/jbc.270.29.17154. PMID 7615511.
• de Saint-Vis B, Cupillard L, Pandrau-Garcia D; et al. (1995). "Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13.". Blood 86 (3): 1098–105. PMID 7620164.
• Rehli M, Krause SW, Kreutz M, Andreesen R (1995). "Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation.". J. Biol. Chem. 270 (26): 15644–9. doi:10.1074/jbc.270.26.15644. PMID 7797563.
• Nagae A, Abe M, Becker RP; et al. (1993). "High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells.". Am. J. Respir. Cell Mol. Biol. 9 (2): 221–9. doi:10.1165/ajrcmb/9.2.221. PMID 8338689.
• Michel B, Igić R, Leray V; et al. (1996). "Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M.". Circ. Res. 78 (4): 635–42. doi:10.1161/01.res.78.4.635. PMID 8635221.
• Skidgel RA, McGwire GB, Li XY (1997). "Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones.". Immunopharmacology 32 (1–3): 48–52. doi:10.1016/0162-3109(96)00008-2. PMID 8796265.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Yoshioka S, Fujiwara H, Yamada S; et al. (1998). "Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy". Mol. Hum. Reprod. 4 (7): 709–17. doi:10.1093/molehr/4.7.709. PMID 9701794.
• Li XY, Skidgel RA (1999). "Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis". Biochem. Biophys. Res. Commun. 258 (1): 204–10. doi:10.1006/bbrc.1999.0619. PMID 10222261.
• Bektas A, Hughes JN, Warram JH; et al. (2001). "Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes". Diabetes 50 (1): 204–8. doi:10.2337/diabetes.50.1.204. PMID 11147789.
• Suzuki Y, Taira H, Tsunoda T; et al. (2001). "Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites". EMBO Rep. 2 (5): 388–93. doi:10.1093/embo-reports/kve085. PMC 1083880. PMID 11375929.
• Lendeckel U, Arndt M, Wrenger S; et al. (2001). "Expression and activity of ectopeptidases in fibrillating human atria". J. Mol. Cell. Cardiol. 33 (6): 1273–81. doi:10.1006/jmcc.2001.1389. PMID 11444929.