Carbonic anhydrase II

CA2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCA2, CA-II, CAC, CAII, Car2, HEL-76, HEL-S-282, Carbonic anhydrase II, carbonic anhydrase 2
External IDsOMIM: 611492; MGI: 88269; HomoloGene: 37256; GeneCards: CA2; OMA:CA2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001293675
NM_000067

NM_009801
NM_001357334

RefSeq (protein)

NP_000058
NP_001280604

NP_033931
NP_001344263

Location (UCSC)Chr 8: 85.46 – 85.48 MbChr 3: 14.95 – 14.97 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Carbonic anhydrase II (gene name CA2) is one of sixteen forms of human α carbonic anhydrases.[5] Carbonic anhydrase catalyzes reversible hydration of carbon dioxide. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of bicarbonate ions in the proximal tubule. [6] Loss of carbonic anhydrase activity in bones impairs the ability of osteoclasts to promote bone resorption, leading to osteopetrosis.[7]

Interactions

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Carbonic anhydrase II has been shown to interact with band 3[8][9][10][11] and sodium-hydrogen antiporter 1.[12]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000104267Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027562Ensembl, 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. ^ Frost, S., & McKenna, R. (2014). Carbonic anhydrase : Mechanism, regulation, links to disease, and industrial applications(Subcellular biochemistry). Dordrecht: Springer. doi:10.1007/978-94-007-7359-2
  6. ^ "Entrez Gene: CA2 carbonic anhydrase II".
  7. ^ Reference, Genetics Home. "Osteopetrosis". Genetics Home Reference. Retrieved 2018-10-31.
  8. ^ Sterling, D; Reithmeier R A; Casey J R (December 2001). "A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers". J. Biol. Chem. 276 (51). United States: 47886–94. doi:10.1074/jbc.M105959200. ISSN 0021-9258. PMID 11606574.
  9. ^ Vince, J W; Reithmeier R A (October 1998). "Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger". J. Biol. Chem. 273 (43). UNITED STATES: 28430–7. doi:10.1074/jbc.273.43.28430. ISSN 0021-9258. PMID 9774471.
  10. ^ Vince, J W; Carlsson U; Reithmeier R A (November 2000). "Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II". Biochemistry. 39 (44). UNITED STATES: 13344–9. doi:10.1021/bi0015111. ISSN 0006-2960. PMID 11063570.
  11. ^ Vince, J W; Reithmeier R A (May 2000). "Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1". Biochemistry. 39 (18). UNITED STATES: 5527–33. doi:10.1021/bi992564p. ISSN 0006-2960. PMID 10820026.
  12. ^ Li, Xiuju; Alvarez Bernardo; Casey Joseph R; Reithmeier Reinhart A F; Fliegel Larry (September 2002). "Carbonic anhydrase II binds to and enhances activity of the Na+/H+ exchanger". J. Biol. Chem. 277 (39). United States: 36085–91. doi:10.1074/jbc.M111952200. ISSN 0021-9258. PMID 12138085.

Further reading

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