CA5B

CA5B
Identifiers
Aliases	CA5B, CA-VB, carbonic anhydrase 5B
External IDs	MGI: 1926249 HomoloGene: 21413 GeneCards: CA5B
Gene ontology Molecular function • lyase activity • metal ion binding • zinc ion binding • carbonate dehydratase activity Cellular component • mitochondrial matrix • mitochondrion Biological process • one-carbon metabolic process • bicarbonate transport Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	11238	56078
Ensembl	ENSG00000169239	ENSMUSG00000031373
UniProt	Q9Y2D0	Q9QZA0
RefSeq (mRNA)	NM_007220	NM_181315
RefSeq (protein)	NP_009151.1 NP_009151.1	NP_851832.2
Location (UCSC)	Chr X: 15.69 – 15.79 Mb	Chr X: 163.98 – 164.03 Mb
PubMed search	[1]	[2]
Wikidata

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Carbonic anhydrase 5B, mitochondrial is an enzyme that in humans is encoded by the CA5B gene.^[3][4]

Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA VB is localized in the mitochondria and shows the highest sequence similarity to the other mitochondrial CA, CA VA. It has a wider tissue distribution than CA VA, which is restricted to the liver. The differences in tissue distribution suggest that the two mitochondrial carbonic anhydrases evolved to assume different physiologic roles.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Fujikawa-Adachi K, Nishimori I, Taguchi T, Onishi S (Aug 1999). "Human mitochondrial carbonic anhydrase VB. cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome x". J Biol Chem. 274 (30): 21228–33. doi:10.1074/jbc.274.30.21228. PMID 10409679.
4. "Entrez Gene: CA5B carbonic anhydrase VB, mitochondrial".

Further reading

• Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies". Annu. Rev. Biochem. 64: 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
• Nishimori I, Onishi S (2001). "Carbonic anhydrase isozymes in the human pancreas". Digestive and Liver Disease. 33 (1): 68–74. doi:10.1016/s1590-8658(01)80138-9. PMID 11303978.
• Shah GN, Hewett-Emmett D, Grubb JH, et al. (2000). "Mitochondrial carbonic anhydrase CA VB: Differences in tissue distribution and pattern of evolution from those of CA VA suggest distinct physiological roles". Proc. Natl. Acad. Sci. U.S.A. 97 (4): 1677–82. doi:10.1073/pnas.97.4.1677. PMC 26495. PMID 10677517.
• 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.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence Comparison of Human and Mouse Genes Reveals a Homologous Block Structure in the Promoter Regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• 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.
• Vullo D, Nishimori I, Innocenti A, et al. (2007). "Carbonic anhydrase activators: an activation study of the human mitochondrial isoforms VA and VB with amino acids and amines". Bioorg. Med. Chem. Lett. 17 (5): 1336–40. doi:10.1016/j.bmcl.2006.11.075. PMID 17174092.