CPN1

CPN1
Identifiers
Aliases	CPN1, CPN, SCPN, carboxypeptidase N subunit 1
External IDs	OMIM: 603103; MGI: 2135874; GeneCards: CPN1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2NSM
Enzyme activity
Gene location (Human)
Chr.	Chromosome 10 (human)
End	100,081,869 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	43,974,995 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; gonad; ; testicle; ; buccal mucosa cell; ; mucosa of ileum; ; skin of thigh; ; right testis; ; left testis; ; kidney; ; human kidney;
	Top expressed in
	left lobe of liver; ; yolk sac; ; islet of Langerhans; ; epithelium of stomach; ; blastocyst; ; right kidney; ; pyloric antrum; ; proximal tubule; ; morula; ; morula;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	carboxypeptidase activity; peptidase activity; zinc ion binding; hydrolase activity; metallopeptidase activity; metal ion binding; metallocarboxypeptidase activity; serine-type carboxypeptidase activity;
Cellular component	extracellular space; Golgi apparatus; secretory granule; soma; synaptic membrane; extracellular region;
Biological process	response to glucocorticoid; bradykinin catabolic process; proteolysis; insulin processing; regulation of complement activation; peptide metabolic process; protein processing;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	1369
	93721
	ENSG00000120054
	ENSMUSG00000025196
	P15169
	Q9JJN5
	NM_001308
	NM_030703
	NP_001299
	NP_109628
	Wikidata
View/Edit Human	View/Edit Mouse

Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene.^[5]^[6]^[7]

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.^[7]

In melanocytic cells CPN1 gene expression may be regulated by MITF.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000120054 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025196 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1".
^ 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. S2CID 24698373.

External links

Human CPN1 genome location and CPN1 gene details page in the UCSC Genome Browser.

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". Kinins V. Advances in Experimental Medicine and Biology. Vol. 247B. pp. 261–4. doi:10.1007/978-1-4615-9546-5_43 (inactive 11 July 2025). ISBN 978-1-4615-9548-9. PMID 2610070.{{cite book}}: CS1 maint: DOI inactive as of July 2025 (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. 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. S2CID 33755040.
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. Bibcode:2002PNAS...9916899M. 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. S2CID 24243086.
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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

This article on a gene on human chromosome 10 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000120054 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000025196 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9628828-5] 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.

[pmid2912725-6] 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.

[entrez-7] "Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1".

[pmid19067971-8] 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. S2CID 24698373.

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CPN1

References

External links

Further reading

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