Carbonic anhydrase II

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PDB rendering based on 12ca.

Available structures: 12ca, 1a42, 1am6, 1avn, 1bcd, 1bic, 1bn1, 1bn3, 1bn4, 1bnm, 1bnn, 1bnq, 1bnt, 1bnu, 1bnv, 1bnw, 1bv3, 1ca2, 1ca3, 1cah, 1cai, 1caj, 1cak, 1cal, 1cam, 1can, 1cao, 1cay, 1caz, 1ccs, 1cct, 1ccu, 1cil, 1cim, 1cin, 1cnb, 1cnc, 1cng, 1cnh, 1cni, 1cnj, 1cnk, 1cnw, 1cnx, 1cny, 1cra, 1cva, 1cvb, 1cvc, 1cvd, 1cve, 1cvf, 1cvh, 1dca, 1dcb, 1eou, 1f2w, 1fql, 1fqm, 1fqn, 1fqr, 1fr4, 1fr7, 1fsn, 1fsq, 1fsr, 1g0e, 1g0f, 1g1d, 1g3z, 1g45, 1g46, 1g48, 1g4j, 1g4o, 1g52, 1g53, 1g54, 1g6v, 1h4n, 1h9n, 1h9q, 1hca, 1hea, 1heb, 1hec, 1hed, 1hva, 1i8z, 1i90, 1i91, 1i9l, 1i9m, 1i9n, 1i9o, 1i9p, 1i9q, 1if4, 1if5, 1if6, 1if7, 1if8, 1if9, 1kwq, 1kwr, 1lg5, 1lg6, 1lgd, 1lug, 1lzv, 1moo, 1mua, 1okl, 1okm, 1okn, 1oq5, 1ray, 1raz, 1rza, 1rzb, 1rzc, 1rzd, 1rze, 1t9n, 1tb0, 1tbt, 1te3, 1teq, 1teu, 1tg3, 1tg9, 1th9, 1thk, 1ttm, 1uga, 1ugb, 1ugc, 1ugd, 1uge, 1ugf, 1ugg, 1xeg, 1xev, 1xpz, 1xq0, 1yda, 1ydb, 1ydc, 1ydd, 1yo0, 1yo1, 1yo2, 1z9y, 1ze8, 1zfk, 1zfq, 1zge, 1zgf, 1zh9, 1zsa, 1zsb, 1zsc, 2abe, 2aw1, 2ax2, 2ca2, 2cba, 2cbb, 2cbc, 2cbd, 2cbe, 2eu2, 2eu3, 2ez7, 2f14, 2fmg, 2fmz, 2fnk, 2fnm, 2fnn, 2foq, 2fos, 2fou, 2fov, 2gd8, 2geh, 2h15, 2h4n, 2hd6, 2hkk, 2hl4, 2hnc, 2hoc, 2ili, 2nng, 2nno, 2nns, 2nnv, 2nwo, 2nwp, 2nwy, 2nwz, 2nxr, 2nxs, 2nxt, 2o4z, 3ca2, 4ca2, 4cac, 5ca2, 5cac, 6ca2, 7ca2, 8ca2, 9ca2

Identifiers

Symbol(s)

CA2; CA II; CA-II; CAII; Car2

External IDs

OMIM: 259730 MGI: 88269 HomoloGene: 37256

Gene ontology
Molecular Function:	• carbonate dehydratase activity • zinc ion binding • lyase activity • metal ion binding
Cellular Component:	• cytoplasm
Biological Process:	• morphogenesis of an epithelium • one-carbon compound metabolic process • carbon dioxide transport • secretion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000067 (mRNA)
NP_000058 (protein)

NM_009801 (mRNA)
NP_033931 (protein)

Location

Chr 8: 86.56 - 86.58 Mb

Chr 3: 14.86 - 14.88 Mb

Pubmed search

[1]

[2]

Carbonic anhydrase II (gene name CA2), is one of fourteen forms of human α carbonic anhydrases. Carbonic anhydrase catalyzes reversible hydration of carbon dioxide. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis^[1]

[edit] References

^ Entrez Gene: CA2 carbonic anhydrase II.

[edit] 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.
Kumpulainen T (1979). "Immunohistochemical localization of human carbonic anhydrase isoenzyme C.". Histochemistry 62 (3): 271–80. PMID 114507.
Henderson LE, Henriksson D, Nyman PO (1976). "Primary structure of human carbonic anhydrase C.". J. Biol. Chem. 251 (18): 5457–63. PMID 823150.
Hu PY, Roth DE, Skaggs LA, et al. (1993). "A splice junction mutation in intron 2 of the carbonic anhydrase II gene of osteopetrosis patients from Arabic countries.". Hum. Mutat. 1 (4): 288–92. doi:10.1002/humu.1380010404. PMID 1301935.
Roth DE, Venta PJ, Tashian RE, Sly WS (1992). "Molecular basis of human carbonic anhydrase II deficiency.". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1804–8. PMID 1542674.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. PMID 1602151.
Schwartz GJ, Brion LP, Corey HE, Dorfman HD (1991). "Case report 668. Carbonic anhydrase II deficiency syndrome (osteopetrosis associated with renal tubular acidosis and cerebral calcification).". Skeletal Radiol. 20 (6): 447–52. PMID 1925679.
Venta PJ, Welty RJ, Johnson TM, et al. (1991). "Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene.". Am. J. Hum. Genet. 49 (5): 1082–90. PMID 1928091.
Venta PJ, Tashian RE (1990). "PCR detection of the TAQ1 polymorphism at the CA2 locus.". Nucleic Acids Res. 18 (18): 5585. PMID 1977133.
Sato S, Zhu XL, Sly WS (1990). "Carbonic anhydrase isozymes IV and II in urinary membranes from carbonic anhydrase II-deficient patients.". Proc. Natl. Acad. Sci. U.S.A. 87 (16): 6073–6. PMID 2117271.
Kaunisto K, Parkkila S, Tammela T, et al. (1990). "Immunohistochemical localization of carbonic anhydrase isoenzymes in the human male reproductive tract.". Histochemistry 94 (4): 381–6. PMID 2121671.
Backman U, Danielsson B, Wistrand PJ (1991). "The excretion of carbonic anhydrase isozymes CA I and CA II in the urine of apparently healthy subjects and in patients with kidney disease.". Scand. J. Clin. Lab. Invest. 50 (6): 627–33. PMID 2123360.
Forsman C, Behravan G, Osterman A, Jonsson BH (1989). "Production of active human carbonic anhydrase II in E. coli.". Acta Chem. Scand., B, Org. Chem. Biochem. 42 (5): 314–8. PMID 2850697.
Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE (1986). "Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements.". Biochim. Biophys. Acta 826 (4): 195–201. PMID 3000449.
Ohlsson A, Cumming WA, Paul A, Sly WS (1986). "Carbonic anhydrase II deficiency syndrome: recessive osteopetrosis with renal tubular acidosis and cerebral calcification.". Pediatrics 77 (3): 371–81. PMID 3081869.
Nakai H, Byers MG, Venta PJ, et al. (1987). "The gene for human carbonic anhydrase II (CA2) is located at chromosome 8q22.". Cytogenet. Cell Genet. 44 (4): 234–5. PMID 3107918.
Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D (1987). "Nucleotide sequence of human liver carbonic anhydrase II cDNA.". Nucleic Acids Res. 15 (11): 4687. PMID 3108857.
Murakami H, Marelich GP, Grubb JH, et al. (1988). "Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II.". Genomics 1 (2): 159–66. PMID 3121496.
Eriksson AE, Jones TA, Liljas A (1989). "Refined structure of human carbonic anhydrase II at 2.0 A resolution.". Proteins 4 (4): 274–82. doi:10.1002/prot.340040406. PMID 3151019.
Eriksson AE, Kylsten PM, Jones TA, Liljas A (1989). "Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH.". Proteins 4 (4): 283–93. doi:10.1002/prot.340040407. PMID 3151020.