CPN1

Carboxypeptidase N, polypeptide 1
PDB rendering based on 2nsm.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 2nsm​
Identifiers
Symbols	CPN1 ; CPN; FLJ40792; SCPN
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1002
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
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 N, polypeptide 1, also known as CPN1, is a human gene.

Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer comprised of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency.

Further reading

• Matthews KW, Mueller-Ortiz SL, Wetsel RA (2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation". Mol. Immunol. 40 (11): 785–93. PMID 14687935.CS1 maint: Multiple names: authors list (link)
• Gebhard W, Schube M, Eulitz M (1990). "cDNA cloning of kininase 1". Adv. Exp. Med. Biol. 247B: 261–4. PMID 2610070.CS1 maint: Multiple names: authors list (link)
• Gebhard W, Schube M, Eulitz M (1989). "cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1)". Eur. J. Biochem. 178 (3): 603–7. PMID 2912725.CS1 maint: Multiple names: authors list (link)
• Skidgel RA, Bennett CD, Schilling JW; et al. (1988). "Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: comparison with other carboxypeptidases". Biochem. Biophys. Res. Commun. 154 (3): 1323–9. PMID 3408501.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hendriks D, Vingron M, Vriend G; et al. (1994). "On the specificity of carboxypeptidase N, a comparative study". Biol. Chem. Hoppe-Seyler. 374 (9): 843–9. PMID 8267877.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Riley DA, Tan F, Miletich DJ, Skidgel RA (1999). "Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1)". Genomics. 50 (1): 105–8. doi:10.1006/geno.1998.5295. PMID 9628828.CS1 maint: Multiple names: authors list (link)
• Sato T, Miwa T, Akatsu H; et al. (2000). "Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not". J. Immunol. 165 (2): 1053–8. PMID 10878383.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Campbell WD, Lazoura E, Okada N, Okada H (2002). "Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N.". Microbiol. Immunol. 46 (2): 131–4. PMID 11939578.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Cao H, Hegele RA (2003). "DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency". J. Hum. Genet. 48 (1): 20–2. doi:10.1007/s100380300003. PMID 12560874.
• Shimomura Y, Kawamura T, Komura H; et al. (2003). "Modulation of procarboxypeptidase R (ProCPR) activation by complementary peptides to thrombomodulin". Microbiol. Immunol. 47 (3): 241–5. PMID 12725295.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Davis DA, Singer KE, De La Luz Sierra M; et al. (2005). "Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1alpha in the circulation". Blood. 105 (12): 4561–8. doi:10.1182/blood-2004-12-4618. PMID 15718415.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)