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CPA2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1AYE, 1DTD, 1O6X
Identifiers
Aliases	CPA2, carboxypeptidase A2
External IDs	OMIM: 600688; MGI: 3617840; HomoloGene: 37541; GeneCards: CPA2; OMA:CPA2 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7q32.2 Start 130,266,863 bp End 130,289,798 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 A3.3 Start 30,541,581 bp End 30,564,475 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans pancreatic epithelial cell body of stomach beta cell duodenum testicle C1 segment fundus jejunal mucosa Top expressed in pyloric antrum islet of Langerhans embryo duodenum retinal pigment epithelium genital tubercle saccule sexually immature organism migratory enteric neural crest cell embryo More reference expression data BioGPS More reference expression data
Gene ontology Molecular function carboxypeptidase activity metallopeptidase activity zinc ion binding peptidase activity hydrolase activity metallocarboxypeptidase activity metal ion binding Cellular component extracellular region vacuole extracellular space Biological process proteolysis protein catabolic process in the vacuole Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1358 232680 Ensembl ENSG00000158516 ENSMUSG00000071553 UniProt P48052 Q504N0 RefSeq (mRNA) NM_001869 NM_001024698 RefSeq (protein) NP_001860 NP_001019869 Location (UCSC) Chr 7: 130.27 – 130.29 Mb Chr 6: 30.54 – 30.56 Mb PubMed search
Wikidata
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Carboxypeptidase A2 is an enzyme that in humans is encoded by the CPA2 gene.

Three different forms of human pancreatic procarboxypeptidase A have been isolated. The A1 and A2 forms are monomeric proteins with different biochemical properties. The A2 form of pancreatic procarboxypeptidase acts on aromatic C-terminal residues

References

1. ^ GRCh38: Ensembl release 89: ENSG00000158516 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000071553 – 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.
5. Catasus L, Vendrell J, Aviles FX, Carreira S, Puigserver A, Billeter M (Apr 1995). "The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model". J Biol Chem. 270 (12): 6651–7. doi:10.1074/jbc.270.12.6651. PMID 7896805.
6. Hayashida S, Yamasaki K, Asada Y, Soeda E, Niikawa N, Kishino T (Aug 2000). "Construction of a physical and transcript map flanking the imprinted MEST/PEG1 region at 7q32". Genomics. 66 (2): 221–5. doi:10.1006/geno.2000.6206. PMID 10860668.
7. ^ "Entrez Gene: CPA2 carboxypeptidase A2 (pancreatic)".

Further reading

• Pascual R, Burgos FJ, Salva M, et al. (1989). "Purification and properties of five different forms of human procarboxypeptidases". Eur. J. Biochem. 179 (3): 609–16. doi:10.1111/j.1432-1033.1989.tb14590.x. PMID 2920728.
• Laethem RM, Blumenkopf TA, Cory M, et al. (1996). "Expression and characterization of human pancreatic preprocarboxypeptidase A1 and preprocarboxypeptidase A2". Arch. Biochem. Biophys. 332 (1): 8–18. doi:10.1006/abbi.1996.0310. PMID 8806703.
• García-Sáez I, Reverter D, Vendrell J, et al. (1998). "The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen". EMBO J. 16 (23): 6906–13. doi:10.1093/emboj/16.23.6906. PMC 1170294. PMID 9384570.
• Reverter D, García-Sáez I, Catasús L, et al. (1998). "Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2". FEBS Lett. 420 (1): 7–10. doi:10.1016/S0014-5793(97)01476-2. PMID 9450539. S2CID 7781802.
• Reverter D, Fernández-Catalán C, Baumgartner R, et al. (2000). "Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2". Nat. Struct. Biol. 7 (4): 322–8. doi:10.1038/74092. PMID 10742178. S2CID 24225493.
• Wouters MA, Husain A (2002). "Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily". J. Mol. Biol. 314 (5): 1191–207. doi:10.1006/jmbi.2000.5161. PMID 11743734.
• 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.
• Jiménez MA, Villegas V, Santoro J, et al. (2003). "NMR solution structure of the activation domain of human procarboxypeptidase A2". Protein Sci. 12 (2): 296–305. doi:10.1110/ps.0227303. PMC 2312417. PMID 12538893.
• Dantas G, Kuhlman B, Callender D, et al. (2003). "A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins". J. Mol. Biol. 332 (2): 449–60. CiteSeerX 10.1.1.66.8110. doi:10.1016/S0022-2836(03)00888-X. PMID 12948494.
• 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.
• Dantas G, Corrent C, Reichow SL, et al. (2007). "High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design". J. Mol. Biol. 366 (4): 1209–21. doi:10.1016/j.jmb.2006.11.080. PMC 3764424. PMID 17196978.

External links

• The MEROPS online database for peptidases and their inhibitors: M14.002
• Overview of all the structural information available in the PDB for UniProt: P48052 (Human Carboxypeptidase A2) at the PDBe-KB.

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