CPM (gene)

Carboxypeptidase M
PDB rendering based on 1uwy.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1uwy​
Identifiers
Symbols	CPM ;
External IDs	Template:OMIM5 Template:MGI HomoloGene: 35367
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Carboxypeptidase M, also known as CPM, is a human gene.

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.

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. PMID 10426564.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 10849748.CS1 maint: Multiple names: authors list (link)
• Nagae A, Deddish PA, Becker RP; et al. (1992). "Carboxypeptidase M in brain and peripheral nerves". J. Neurochem. 59 (6): 2201–12. PMID 1431901.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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. 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 7797563.CS1 maint: Multiple names: authors list (link)
• 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. PMID 8338689.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kas K, Schoenmakers EF, Van de Ven WJ (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.CS1 maint: Multiple names: authors list (link)
• 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. PMID 8635221.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 8796265.CS1 maint: Multiple names: authors list (link)
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.CS1 maint: Multiple names: authors list (link)
• 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. PMID 9701794.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 11147789.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 11375929.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)