CPM (gene): Difference between revisions

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{{Infobox_gene}}
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'''Carboxypeptidase M''' is an [[enzyme]] that in humans is encoded by the ''CPM'' [[gene]].<ref name="pmid8586455">{{cite journal | vauthors = Kas K, Schoenmakers EF, Van de Ven WJ | title = Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15 | journal = Genomics | volume = 30 | issue = 2 | pages = 403–5 |date=Mar 1996 | pmid = 8586455 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CPM carboxypeptidase M| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1368| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_CPM_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1uwy.
| PDB = {{PDB2|1uwy}}
| Name = Carboxypeptidase M
| HGNCid = 2311
| Symbol = CPM
| AltSymbols =;
| OMIM = 114860
| ECnumber = 
| Homologene = 35367
| MGIid = 1917824
| GeneAtlas_image1 = PBB_GE_CPM_206100_at_tn.png
| Function = {{GNF_GO|id=GO:0004182 |text = carboxypeptidase A activity}} {{GNF_GO|id=GO:0008199 |text = ferric iron binding}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
  | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
  | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006725 |text = aromatic compound metabolic process}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1368
    | Hs_Ensembl = ENSG00000135678
    | Hs_RefseqProtein = NP_001005502
    | Hs_RefseqmRNA = NM_001005502
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 67531227
    | Hs_GenLoc_end = 67612891
    | Hs_Uniprot = P14384
    | Mm_EntrezGene = 70574
    | Mm_Ensembl = ENSMUSG00000020183
    | Mm_RefseqmRNA = XM_917914
    | Mm_RefseqProtein = XP_923007
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 117032498
    | Mm_GenLoc_end = 117088295
    | Mm_Uniprot = Q80V42
  }}
}}
'''Carboxypeptidase M''', also known as '''CPM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CPM carboxypeptidase M| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1368| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CPM carboxypeptidase M| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1368| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CPM carboxypeptidase M| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1368| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CPM}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Fujiwara H, Imai K, Inoue T, ''et al.'' |title=Membrane-bound cell surface peptidases in reproductive organs. |journal=Endocr. J. |volume=46 |issue= 1 |pages= 11-25 |year= 1999 |pmid= 10426564 |doi=  }}
*{{cite journal  | vauthors=Fujiwara H, Imai K, Inoue T |title=Membrane-bound cell surface peptidases in reproductive organs. |journal=Endocr. J. |volume=46 |issue= 1 |pages= 11–25 |year= 1999 |pmid= 10426564 |doi=10.1507/endocrj.46.11 |display-authors=etal}}
*{{cite journal  | author=Rehli M, Krause SW, Andreesen R |title=The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo. |journal=Adv. Exp. Med. Biol. |volume=477 |issue=  |pages= 205-16 |year= 2000 |pmid= 10849748 |doi=  }}
*{{cite journal  | vauthors=Rehli M, Krause SW, Andreesen R |title=The membrane-bound ectopeptidase CPM as a marker of macrophage maturation in vitro and in vivo. |journal=Adv. Exp. Med. Biol. |volume=477 |issue=  |pages= 205–16 |year= 2000 |pmid= 10849748 |doi=10.1007/0-306-46826-3_23 }}
*{{cite journal  | author=Nagae A, Deddish PA, Becker RP, ''et al.'' |title=Carboxypeptidase M in brain and peripheral nerves. |journal=J. Neurochem. |volume=59 |issue= 6 |pages= 2201-12 |year= 1992 |pmid= 1431901 |doi=  }}
*{{cite journal  | vauthors=Nagae A, Deddish PA, Becker RP |title=Carboxypeptidase M in brain and peripheral nerves. |journal=J. Neurochem. |volume=59 |issue= 6 |pages= 2201–12 |year= 1992 |pmid= 1431901 |doi=10.1111/j.1471-4159.1992.tb10112.x |display-authors=etal}}
*{{cite journal  | author=Tan F, Chan SJ, Steiner DF, ''et al.'' |title=Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N. |journal=J. Biol. Chem. |volume=264 |issue= 22 |pages= 13165-70 |year= 1989 |pmid= 2753907 |doi=  }}
*{{cite journal  | vauthors=Tan F, Chan SJ, Steiner DF |title=Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N. |journal=J. Biol. Chem. |volume=264 |issue= 22 |pages= 13165–70 |year= 1989 |pmid= 2753907 |doi=  |display-authors=etal}}
*{{cite journal  | author=Skidgel RA, Davis RM, Tan F |title=Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones. |journal=J. Biol. Chem. |volume=264 |issue= 4 |pages= 2236-41 |year= 1989 |pmid= 2914904 |doi=  }}
*{{cite journal  | vauthors=Skidgel RA, Davis RM, Tan F |title=Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones. |journal=J. Biol. Chem. |volume=264 |issue= 4 |pages= 2236–41 |year= 1989 |pmid= 2914904 |doi=  }}
*{{cite journal  | author=McGwire GB, Skidgel RA |title=Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M. |journal=J. Biol. Chem. |volume=270 |issue= 29 |pages= 17154-8 |year= 1995 |pmid= 7615511 |doi=  }}
*{{cite journal  | vauthors=McGwire GB, Skidgel RA |title=Extracellular conversion of epidermal growth factor (EGF) to des-Arg53-EGF by carboxypeptidase M. |journal=J. Biol. Chem. |volume=270 |issue= 29 |pages= 17154–8 |year= 1995 |pmid= 7615511 |doi=10.1074/jbc.270.29.17154 }}
*{{cite journal  | author=de Saint-Vis B, Cupillard L, Pandrau-Garcia D, ''et al.'' |title=Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13. |journal=Blood |volume=86 |issue= 3 |pages= 1098-105 |year= 1995 |pmid= 7620164 |doi=  }}
*{{cite journal  | vauthors=de Saint-Vis B, Cupillard L, Pandrau-Garcia D |title=Distribution of carboxypeptidase M on lymphoid and myeloid cells parallels the other zinc-dependent proteases CD10 and CD13. |journal=Blood |volume=86 |issue= 3 |pages= 1098–105 |year= 1995 |pmid= 7620164 |doi=  |display-authors=etal}}
*{{cite journal  | author=Rehli M, Krause SW, Kreutz M, Andreesen R |title=Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation. |journal=J. Biol. Chem. |volume=270 |issue= 26 |pages= 15644-9 |year= 1995 |pmid= 7797563 |doi=  }}
*{{cite journal  | vauthors=Rehli M, Krause SW, Kreutz M, Andreesen R |title=Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation. |journal=J. Biol. Chem. |volume=270 |issue= 26 |pages= 15644–9 |year= 1995 |pmid= 7797563 |doi=10.1074/jbc.270.26.15644 }}
*{{cite journal  | author=Nagae A, Abe M, Becker RP, ''et al.'' |title=High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells. |journal=Am. J. Respir. Cell Mol. Biol. |volume=9 |issue= 2 |pages= 221-9 |year= 1993 |pmid= 8338689 |doi=  }}
*{{cite journal  | vauthors=Nagae A, Abe M, Becker RP |title=High concentration of carboxypeptidase M in lungs: presence of the enzyme in alveolar type I cells. |journal=Am. J. Respir. Cell Mol. Biol. |volume=9 |issue= 2 |pages= 221–9 |year= 1993 |pmid= 8338689 |doi=  10.1165/ajrcmb/9.2.221|display-authors=etal}}
*{{cite journal  | author=Kas K, Schoenmakers EF, Van de Ven WJ |title=Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15. |journal=Genomics |volume=30 |issue= 2 |pages= 403-5 |year= 1996 |pmid= 8586455 |doi= }}
*{{cite journal  | vauthors=Michel B, Igić R, Leray V |title=Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M. |journal=Circ. Res. |volume=78 |issue= 4 |pages= 635–42 |year= 1996 |pmid= 8635221 |doi=  10.1161/01.res.78.4.635|display-authors=etal}}
*{{cite journal  | author=Michel B, Igić R, Leray V, ''et al.'' |title=Removal of Arg141 from the alpha chain of human hemoglobin by carboxypeptidases N and M. |journal=Circ. Res. |volume=78 |issue= 4 |pages= 635-42 |year= 1996 |pmid= 8635221 |doi=  }}
*{{cite journal  | vauthors=Skidgel RA, McGwire GB, Li XY |title=Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones. |journal=Immunopharmacology |volume=32 |issue= 1–3 |pages= 48–52 |year= 1997 |pmid= 8796265 |doi=10.1016/0162-3109(96)00008-2 }}
*{{cite journal  | author=Skidgel RA, McGwire GB, Li XY |title=Membrane anchoring and release of carboxypeptidase M: implications for extracellular hydrolysis of peptide hormones. |journal=Immunopharmacology |volume=32 |issue= 1-3 |pages= 48-52 |year= 1997 |pmid= 8796265 |doi=  }}
*{{cite journal  | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | vauthors=Yoshioka S, Fujiwara H, Yamada S |title=Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy |journal=Mol. Hum. Reprod. |volume=4 |issue= 7 |pages= 709–17 |year= 1998 |pmid= 9701794 |doi=10.1093/molehr/4.7.709 |display-authors=etal}}
*{{cite journal  | author=Yoshioka S, Fujiwara H, Yamada S, ''et al.'' |title=Membrane-bound carboxypeptidase-M is expressed on human ovarian follicles and corpora lutea of menstrual cycle and early pregnancy. |journal=Mol. Hum. Reprod. |volume=4 |issue= 7 |pages= 709-17 |year= 1998 |pmid= 9701794 |doi=  }}
*{{cite journal  | vauthors=Li XY, Skidgel RA |title=Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis |journal=Biochem. Biophys. Res. Commun. |volume=258 |issue= 1 |pages= 204–10 |year= 1999 |pmid= 10222261 |doi= 10.1006/bbrc.1999.0619 }}
*{{cite journal  | author=Li XY, Skidgel RA |title=Release of glycosylphosphatidylinositol-anchored carboxypeptidase M by phosphatidylinositol-specific phospholipase C upregulates enzyme synthesis. |journal=Biochem. Biophys. Res. Commun. |volume=258 |issue= 1 |pages= 204-10 |year= 1999 |pmid= 10222261 |doi= 10.1006/bbrc.1999.0619 }}
*{{cite journal  | vauthors=Bektas A, Hughes JN, Warram JH |title=Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes |journal=Diabetes |volume=50 |issue= 1 |pages= 204–8 |year= 2001 |pmid= 11147789 |doi=10.2337/diabetes.50.1.204 |display-authors=etal}}
*{{cite journal  | author=Bektas A, Hughes JN, Warram JH, ''et al.'' |title=Type 2 diabetes locus on 12q15. Further mapping and mutation screening of two candidate genes. |journal=Diabetes |volume=50 |issue= 1 |pages= 204-8 |year= 2001 |pmid= 11147789 |doi=  }}
*{{cite journal  | vauthors=Suzuki Y, Taira H, Tsunoda T |title=Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites |journal=EMBO Rep. |volume=2 |issue= 5 |pages= 388–93 |year= 2001 |pmid= 11375929 |doi= 10.1093/embo-reports/kve085 | pmc=1083880 |display-authors=etal}}
*{{cite journal  | author=Suzuki Y, Taira H, Tsunoda T, ''et al.'' |title=Diverse transcriptional initiation revealed by fine, large-scale mapping of mRNA start sites. |journal=EMBO Rep. |volume=2 |issue= 5 |pages= 388-93 |year= 2001 |pmid= 11375929 |doi= 10.1093/embo-reports/kve085 }}
*{{cite journal  | vauthors=Lendeckel U, Arndt M, Wrenger S |title=Expression and activity of ectopeptidases in fibrillating human atria |journal=J. Mol. Cell. Cardiol. |volume=33 |issue= 6 |pages= 1273–81 |year= 2001 |pmid= 11444929 |doi= 10.1006/jmcc.2001.1389 |display-authors=etal}}
*{{cite journal  | author=Lendeckel U, Arndt M, Wrenger S, ''et al.'' |title=Expression and activity of ectopeptidases in fibrillating human atria. |journal=J. Mol. Cell. Cardiol. |volume=33 |issue= 6 |pages= 1273-81 |year= 2001 |pmid= 11444929 |doi= 10.1006/jmcc.2001.1389 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=1368}}
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Revision as of 09:59, 30 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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. ↑ 2.0 2.1 "Entrez Gene: CPM carboxypeptidase M".

External links

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.



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