Carbonic anhydrase 13

Carbonic anhydrase 13 is a protein that in humans is encoded by the CA13 gene.[5]

CA13
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3CZV, 3D0N, 3DA2, 4HU1, 4KNM, 4KNN, 4QIZ, 4QJP, 4QJX, 4QSJ
Identifiers
Aliases	CA13, CAXIII, carbonic anhydrase 13
External IDs	OMIM: 611436 MGI: 1931322 HomoloGene: 75207 GeneCards: CA13
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8q21.2 Start 85,220,587 bp[1] End 85,284,073 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 A1 Start 14,641,727 bp[2] End 14,663,002 bp[2]
Gene ontology Molecular function • zinc ion binding • lyase activity • metal ion binding • carbonate dehydratase activity • Carbonic anhydrase Cellular component • myelin • cytosol • intracellular membrane-bounded organelle Biological process • bicarbonate transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	377677	71934
Ensembl	ENSG00000185015	ENSMUSG00000027555
UniProt	Q8N1Q1	Q9D6N1
RefSeq (mRNA)	NM_198584	NM_024495
RefSeq (protein)	NP_940986	NP_078771
Location (UCSC)	Chr 8: 85.22 – 85.28 Mb	Chr 3: 14.64 – 14.66 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Carbonic anhydrases (CAs) are a family of zinc metalloenzymes that catalyze the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions).[6][7]

References

1. GRCh38: Ensembl release 89: ENSG00000185015 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027555 - 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. "Entrez Gene: Carbonic anhydrase 13". Retrieved 2019-12-31.
6. Badger MR, Price GD (1994). "The role of carbonic anhydrase in photosynthesis". Annu. Rev. Plant Physiol. Plant Mol. Biol. 45: 369–392. doi:10.1146/annurev.pp.45.060194.002101.
7. Lindskog S (1997). "Structure and mechanism of carbonic anhydrase". Pharmacology & Therapeutics. 74 (1): 1–20. doi:10.1016/S0163-7258(96)00198-2. PMID 9336012.

Further reading

• Lehtonen J, Shen B, Vihinen M, Casini A, Scozzafava A, Supuran CT, et al. (January 2004). "Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family". The Journal of Biological Chemistry. 279 (4): 2719–27. doi:10.1074/jbc.M308984200. PMID 14600151.
• Kummola L, Hämäläinen JM, Kivelä J, Kivelä AJ, Saarnio J, Karttunen T, Parkkila S (April 2005). "Expression of a novel carbonic anhydrase, CA XIII, in normal and neoplastic colorectal mucosa". BMC Cancer. 5: 41. doi:10.1186/1471-2407-5-41. PMC 1097719. PMID 15836783.
• Hilvo M, Innocenti A, Monti SM, De Simone G, Supuran CT, Parkkila S (2008). "Recent advances in research on the most novel carbonic anhydrases, CA XIII and XV". Current Pharmaceutical Design. 14 (7): 672–8. doi:10.2174/138161208783877811. PMID 18336313.

External links

• Overview of all the structural information available in the PDB for UniProt: Q8N1Q1 (Human Carbonic anhydrase 13) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.