Carbonic anhydrase 5B, mitochondrial

CA5B
Identifiers
Aliases	CA5B, CA-VB, carbonic anhydrase 5B, CAVB
External IDs	OMIM: 300230; MGI: 1926249; HomoloGene: 21413; GeneCards: CA5B; OMA:CA5B - orthologs
Gene location (Human) Chr. X chromosome (human)[1] Band Xp22.2 Start 15,688,830 bp[1] End 15,788,411 bp[1]
Gene location (Mouse) Chr. X chromosome (mouse)[2] Band X|X F5 Start 162,759,818 bp[2] End 162,810,993 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon monocyte granulocyte ascending aorta right coronary artery tibial arteries canal of the cervix Descending thoracic aorta left ovary right ovary Top expressed in white adipose tissue right kidney mammary gland seminal vesicula subcutaneous adipose tissue brown adipose tissue proximal tubule human kidney intercostal muscle tunica adventitia of aorta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function lyase activity metal ion binding zinc ion binding carbonate dehydratase activity carbonic anhydrase Cellular component mitochondrial matrix mitochondrion Biological process bicarbonate transport response to bacterium one-carbon metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11238 56078 Ensembl ENSG00000169239 ENSMUSG00000031373 UniProt Q9Y2D0 Q9QZA0 RefSeq (mRNA) NM_007220 NM_181315 RefSeq (protein) NP_009151 NP_009151.1 NP_851832 Location (UCSC) Chr X: 15.69 – 15.79 Mb Chr X: 162.76 – 162.81 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Carbonic anhydrase 5B, mitochondrial is an enzyme that in humans is encoded by the CA5B gene.^[5][6]

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.^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000169239 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031373 – 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. 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.
6. "Entrez Gene: CA5B carbonic anhydrase VB, mitochondrial".

External links

• Human CA5B genome location and CA5B gene details page in the UCSC Genome Browser.

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. Bibcode:2000PNAS...97.1677S. 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. Bibcode:2002PNAS...9916899M. 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.

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