CPN1

From Wikipedia, the free encyclopedia

Carboxypeptidase N, polypeptide 1

PDB rendering based on 2nsm.

Available structures: 2nsm

Identifiers

Symbol(s)

CPN1; CPN; FLJ40792; SCPN

External IDs

OMIM: 603103 MGI: 2135874 HomoloGene: 1002

Gene ontology
Molecular Function:	• carboxypeptidase activity • carboxypeptidase A activity • lysine carboxypeptidase activity • metallopeptidase activity • zinc ion binding • metal ion binding
Cellular Component:	• extracellular space
Biological Process:	• proteolysis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001308 (mRNA)
NP_001299 (protein)

XM_978873 (mRNA)
XP_983967 (protein)

Location

Chr 10: 101.79 - 101.83 Mb

Chr 19: 44.01 - 44.04 Mb

Pubmed search

[1]

[2]

Carboxypeptidase N, polypeptide 1, also known as CPN1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CPN1 carboxypeptidase N, polypeptide 1.

[edit] 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.
Gebhard W, Schube M, Eulitz M (1990). "cDNA cloning of kininase 1.". Adv. Exp. Med. Biol. 247B: 261–4. PMID 2610070.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.