CPN1

CPN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2NSM
Identifiers
Aliases	CPN1, CPN, SCPN, carboxypeptidase N subunit 1
External IDs	MGI: 2135874 HomoloGene: 1002 GeneCards: CPN1
Gene ontology Molecular function • carboxypeptidase activity • peptidase activity • zinc ion binding • hydrolase activity • metallopeptidase activity • metal ion binding • serine-type carboxypeptidase activity • metallocarboxypeptidase activity Cellular component • extracellular space • extracellular region Biological process • protein processing • response to glucocorticoid • bradykinin catabolic process • proteolysis • peptide metabolic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1369	93721
Ensembl	ENSG00000120054	ENSMUSG00000025196
UniProt	P15169	Q9JJN5
RefSeq (mRNA)	NM_001308	NM_030703
RefSeq (protein)	NP_001299.1	NP_109628.1
Location (UCSC)	Chr 10: 100.04 – 100.08 Mb	Chr 19: 43.96 – 43.99 Mb
PubMed search	[1]	[2]
Wikidata

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View/Edit Mouse

Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene.^[3][4][5]

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 composed 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.^[5]

In melanocytic cells CPN1 gene expression may be regulated by MITF.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Riley DA, Tan F, Miletich DJ, Skidgel RA (Apr 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.
4. Gebhard W, Schube M, Eulitz M (Mar 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. doi:10.1111/j.1432-1033.1989.tb14488.x. PMID 2912725.
5. "Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1".
6. Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.

Further reading

• Matthews KW, Mueller-Ortiz SL, Wetsel RA (2004). "Carboxypeptidase N: a pleiotropic regulator of inflammation.". Mol. Immunol. 40 (11): 785–93. doi:10.1016/j.molimm.2003.10.002. PMID 14687935.
• Gebhard W, Schube M, Eulitz M (1990). "cDNA cloning of kininase 1.". Adv. Exp. Med. Biol. 247B: 261–4. doi:10.1007/978-1-4615-9546-5_43. PMID 2610070.
• 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. doi:10.1016/0006-291X(88)90284-7. PMID 3408501.
• 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. doi:10.1515/bchm3.1993.374.7-12.843. PMID 8267877.
• 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. doi:10.4049/jimmunol.165.2.1053. PMID 10878383.
• 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. doi:10.1111/j.1348-0421.2002.tb02669.x. PMID 11939578.
• 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. PMC 139241. PMID 12477932.
• 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. doi:10.1111/j.1348-0421.2003.tb03383.x. PMID 12725295.
• 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. PMC 528928. PMID 15489334.
• 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. PMC 1895000. PMID 15718415.
• 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.