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| Carboxypeptidase N, polypeptide 1 | |||||||||||||
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 PDB rendering based on 2nsm. |
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| Identifiers | |||||||||||||
| Symbols | CPN1; CPN; SCPN | ||||||||||||
| External IDs | OMIM: 603103 MGI: 2135874 HomoloGene: 1002 ChEMBL: 4713 GeneCards: CPN1 Gene | ||||||||||||
| EC number | 3.4.17.3 | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 1369 | 93721 | |||||||||||
| Ensembl | ENSG00000120054 | ENSMUSG00000025196 | |||||||||||
| UniProt | P15169 | Q9JJN5 | |||||||||||
| RefSeq (mRNA) | NM_001308.2 | NM_030703.2 | |||||||||||
| RefSeq (protein) | NP_001299.1 | NP_109628.1 | |||||||||||
| Location (UCSC) | Chr 10: 101.8 – 101.84 Mb |
Chr 19: 44.03 – 44.06 Mb |
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| PubMed search | [1] | [2] | |||||||||||
Carboxypeptidase N catalytic chain is an enzyme that in humans is encoded by the CPN1 gene.[1][2][3]
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.[3]
In melanocytic cells CPN1 gene expression may be regulated by MITF[4].
References [link]
- ^ 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". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1369.
- ^ 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 [link]
- 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. 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. 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. 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. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- 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. PMC 528928. PMID 15489334. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1895000.
- 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.
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