Carbonic anhydrase II: Difference between revisions

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{{Infobox_gene}}
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| image = PBB_Protein_CA2_image.jpg
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| Name = Carbonic anhydrase II
| HGNCid = 1373
| Symbol = CA2
| AltSymbols =; CA II; CA-II; CAII; Car2
| OMIM = 259730
| ECnumber = 
| Homologene = 37256
| MGIid = 88269
| GeneAtlas_image1 = PBB_GE_CA2_209301_at_tn.png
| Function = {{GNF_GO|id=GO:0004089 |text = carbonate dehydratase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0002009 |text = morphogenesis of an epithelium}} {{GNF_GO|id=GO:0006730 |text = one-carbon compound metabolic process}} {{GNF_GO|id=GO:0015670 |text = carbon dioxide transport}} {{GNF_GO|id=GO:0046903 |text = secretion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 760
    | Hs_Ensembl = ENSG00000104267
    | Hs_RefseqProtein = NP_000058
    | Hs_RefseqmRNA = NM_000067
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 86563433
    | Hs_GenLoc_end = 86580945
    | Hs_Uniprot = P00918
    | Mm_EntrezGene = 12349
    | Mm_Ensembl = ENSMUSG00000027562
    | Mm_RefseqmRNA = NM_009801
    | Mm_RefseqProtein = NP_033931
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 14863450
    | Mm_GenLoc_end = 14877513
    | Mm_Uniprot = Q6LDQ7
  }}
}}


'''Carbonic anhydrase II''' (gene name '''CA2'''), is one of fourteen forms of human [[Carbonic anhydrase|α carbonic anhydrases]]. Carbonic anhydrase catalyzes reversible hydration of [[carbon dioxide]].  Defects in this enzyme are associated with [[osteopetrosis]] and [[renal tubular acidosis]]<ref>{{cite web | title = Entrez Gene: CA2 carbonic anhydrase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=760| accessdate = }}</ref>
'''Carbonic anhydrase II''' (gene name '''CA2'''), is one of fourteen forms of human [[Carbonic anhydrase|α carbonic anhydrases]]. 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.
<ref>{{cite web | title = Entrez Gene: CA2 carbonic anhydrase II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=760| accessdate = }}</ref> Loss of carbonic anhydrase activity in bones impairs the ability of [[Osteoclast|osteoclasts]] to promote bone resorption, leading to osteopetrosis. <ref>{{Cite web|url=https://ghr.nlm.nih.gov/condition/osteopetrosis|title=Osteopetrosis|last=Reference|first=Genetics Home|website=Genetics Home Reference|language=en|access-date=2018-10-31}}</ref>


==Interactions==
Carbonic anhydrase II has been shown to [[Protein-protein interaction|interact]] with [[band 3]]<ref name=pmid11606574>{{cite journal |last=Sterling |first=D |author2=Reithmeier R A |author3=Casey J R  |date=December 2001  |title=A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers |journal=J. Biol. Chem. |volume=276 |issue=51 |pages=47886–94 |publisher= |location = United States| issn = 0021-9258| pmid = 11606574 |doi = 10.1074/jbc.M105959200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid9774471>{{cite journal |doi=10.1074/jbc.273.43.28430 |last=Vince |first=J W |author2=Reithmeier R A |date=October 1998  |title=Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger |journal=J. Biol. Chem. |volume=273 |issue=43 |pages=28430–7 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9774471 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid11063570>{{cite journal |doi=10.1021/bi0015111 |last=Vince |first=J W |author2=Carlsson U |author3=Reithmeier R A  |date=November 2000  |title=Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II |journal=Biochemistry |volume=39 |issue=44 |pages=13344–9 |publisher= |location = UNITED STATES| issn = 0006-2960| pmid = 11063570 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid10820026>{{cite journal |doi=10.1021/bi992564p |last=Vince |first=J W |author2=Reithmeier R A |date=May 2000 |title=Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1 |journal=Biochemistry |volume=39 |issue=18 |pages=5527–33 |publisher= |location = UNITED STATES| issn = 0006-2960| pmid = 10820026 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[sodium-hydrogen antiporter 1]].<ref name=pmid12138085>{{cite journal |last=Li |first=Xiuju |author2=Alvarez Bernardo |author3=Casey Joseph R |author4=Reithmeier Reinhart A F |author5=Fliegel Larry  |date=September 2002  |title=Carbonic anhydrase II binds to and enhances activity of the Na+/H+ exchanger |journal=J. Biol. Chem. |volume=277 |issue=39 |pages=36085–91 |publisher= |location = United States| issn = 0021-9258| pmid = 12138085 |doi = 10.1074/jbc.M111952200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Sly WS, Hu PY |title=Human carbonic anhydrases and carbonic anhydrase deficiencies. |journal=Annu. Rev. Biochem. |volume=64 |issue=  |pages= 375-401 |year= 1995 |pmid= 7574487 |doi= 10.1146/annurev.bi.64.070195.002111 }}
*{{cite journal  | vauthors=Sly WS, Hu PY |title=Human carbonic anhydrases and carbonic anhydrase deficiencies. |journal=Annu. Rev. Biochem. |volume=64 |issue=  1|pages= 375–401 |year= 1995 |pmid= 7574487 |doi= 10.1146/annurev.bi.64.070195.002111 }}
*{{cite journal  | author=Kumpulainen T |title=Immunohistochemical localization of human carbonic anhydrase isoenzyme C. |journal=Histochemistry |volume=62 |issue= 3 |pages= 271-80 |year= 1979 |pmid= 114507 |doi=  }}
*{{cite journal  | author=Kumpulainen T |title=Immunohistochemical localization of human carbonic anhydrase isoenzyme C. |journal=Histochemistry |volume=62 |issue= 3 |pages= 271–80 |year= 1979 |pmid= 114507 |doi=10.1007/BF00508355 }}
*{{cite journal  | author=Henderson LE, Henriksson D, Nyman PO |title=Primary structure of human carbonic anhydrase C. |journal=J. Biol. Chem. |volume=251 |issue= 18 |pages= 5457-63 |year= 1976 |pmid= 823150 |doi=  }}
*{{cite journal  | vauthors=Henderson LE, Henriksson D, Nyman PO |title=Primary structure of human carbonic anhydrase C. |journal=J. Biol. Chem. |volume=251 |issue= 18 |pages= 5457–63 |year= 1976 |pmid= 823150 |doi=  }}
*{{cite journal  | author=Hu PY, Roth DE, Skaggs LA, ''et al.'' |title=A splice junction mutation in intron 2 of the carbonic anhydrase II gene of osteopetrosis patients from Arabic countries. |journal=Hum. Mutat. |volume=1 |issue= 4 |pages= 288-92 |year= 1993 |pmid= 1301935 |doi= 10.1002/humu.1380010404 }}
*{{cite journal  | vauthors=Hu PY, Roth DE, Skaggs LA |title=A splice junction mutation in intron 2 of the carbonic anhydrase II gene of osteopetrosis patients from Arabic countries. |journal=Hum. Mutat. |volume=1 |issue= 4 |pages= 288–92 |year= 1993 |pmid= 1301935 |doi= 10.1002/humu.1380010404 |display-authors=etal}}
*{{cite journal  | author=Roth DE, Venta PJ, Tashian RE, Sly WS |title=Molecular basis of human carbonic anhydrase II deficiency. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1804-8 |year= 1992 |pmid= 1542674 |doi= }}
*{{cite journal  | vauthors=Roth DE, Venta PJ, Tashian RE, Sly WS |title=Molecular basis of human carbonic anhydrase II deficiency. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1804–8 |year= 1992 |pmid= 1542674 |doi=10.1073/pnas.89.5.1804  | pmc=48541  |bibcode=1992PNAS...89.1804R }}
*{{cite journal  | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal  | vauthors=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=10.1016/S0163-4453(05)80037-4  }}
*{{cite journal  | author=Schwartz GJ, Brion LP, Corey HE, Dorfman HD |title=Case report 668. Carbonic anhydrase II deficiency syndrome (osteopetrosis associated with renal tubular acidosis and cerebral calcification). |journal=Skeletal Radiol. |volume=20 |issue= 6 |pages= 447-52 |year= 1991 |pmid= 1925679 |doi=  }}
*{{cite journal  | vauthors=Schwartz GJ, Brion LP, Corey HE, Dorfman HD |title=Case report 668. Carbonic anhydrase II deficiency syndrome (osteopetrosis associated with renal tubular acidosis and cerebral calcification). |journal=Skeletal Radiol. |volume=20 |issue= 6 |pages= 447–52 |year= 1991 |pmid= 1925679 |doi=  }}
*{{cite journal  | author=Venta PJ, Welty RJ, Johnson TM, ''et al.'' |title=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. |journal=Am. J. Hum. Genet. |volume=49 |issue= 5 |pages= 1082-90 |year= 1991 |pmid= 1928091 |doi=  }}
*{{cite journal  | vauthors=Venta PJ, Welty RJ, Johnson TM |title=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. |journal=Am. J. Hum. Genet. |volume=49 |issue= 5 |pages= 1082–90 |year= 1991 |pmid= 1928091 |doi=  | pmc=1683243  |display-authors=etal}}
*{{cite journal  | author=Venta PJ, Tashian RE |title=PCR detection of the TAQ1 polymorphism at the CA2 locus. |journal=Nucleic Acids Res. |volume=18 |issue= 18 |pages= 5585 |year= 1990 |pmid= 1977133 |doi= }}
*{{cite journal  | vauthors=Venta PJ, Tashian RE |title=PCR detection of the TAQ1 polymorphism at the CA2 locus. |journal=Nucleic Acids Res. |volume=18 |issue= 18 |pages= 5585 |year= 1990 |pmid= 1977133 |doi=10.1093/nar/18.18.5585  | pmc=332284  }}
*{{cite journal  | author=Sato S, Zhu XL, Sly WS |title=Carbonic anhydrase isozymes IV and II in urinary membranes from carbonic anhydrase II-deficient patients. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6073-6 |year= 1990 |pmid= 2117271 |doi=  }}
*{{cite journal  | vauthors=Sato S, Zhu XL, Sly WS |title=Carbonic anhydrase isozymes IV and II in urinary membranes from carbonic anhydrase II-deficient patients. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6073–6 |year= 1990 |pmid= 2117271 |doi=10.1073/pnas.87.16.6073 | pmc=54474  |bibcode=1990PNAS...87.6073S }}
*{{cite journal  | author=Kaunisto K, Parkkila S, Tammela T, ''et al.'' |title=Immunohistochemical localization of carbonic anhydrase isoenzymes in the human male reproductive tract. |journal=Histochemistry |volume=94 |issue= 4 |pages= 381-6 |year= 1990 |pmid= 2121671 |doi=  }}
*{{cite journal  | vauthors=Kaunisto K, Parkkila S, Tammela T |title=Immunohistochemical localization of carbonic anhydrase isoenzymes in the human male reproductive tract. |journal=Histochemistry |volume=94 |issue= 4 |pages= 381–6 |year= 1990 |pmid= 2121671 |doi=10.1007/BF00266444 |display-authors=etal}}
*{{cite journal  | author=Backman U, Danielsson B, Wistrand PJ |title=The excretion of carbonic anhydrase isozymes CA I and CA II in the urine of apparently healthy subjects and in patients with kidney disease. |journal=Scand. J. Clin. Lab. Invest. |volume=50 |issue= 6 |pages= 627-33 |year= 1991 |pmid= 2123360 |doi=  }}
*{{cite journal  | vauthors=Backman U, Danielsson B, Wistrand PJ |title=The excretion of carbonic anhydrase isozymes CA I and CA II in the urine of apparently healthy subjects and in patients with kidney disease. |journal=Scand. J. Clin. Lab. Invest. |volume=50 |issue= 6 |pages= 627–33 |year= 1991 |pmid= 2123360 |doi=10.3109/00365519009089180 }}
*{{cite journal  | author=Forsman C, Behravan G, Osterman A, Jonsson BH |title=Production of active human carbonic anhydrase II in E. coli. |journal=Acta Chem. Scand., B, Org. Chem. Biochem. |volume=42 |issue= 5 |pages= 314-8 |year= 1989 |pmid= 2850697 |doi=  }}
*{{cite journal  | vauthors=Forsman C, Behravan G, Osterman A, Jonsson BH |title=Production of active human carbonic anhydrase II in E. coli. |journal=Acta Chemica Scandinavica B |volume=42 |issue= 5 |pages= 314–8 |year= 1989 |pmid= 2850697 |doi=  }}
*{{cite journal  | author=Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE |title=Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements. |journal=Biochim. Biophys. Acta |volume=826 |issue= 4 |pages= 195-201 |year= 1986 |pmid= 3000449 |doi=  }}
*{{cite journal  | vauthors=Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE |title=Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements. |journal=Biochim. Biophys. Acta |volume=826 |issue= 4 |pages= 195–201 |year= 1986 |pmid= 3000449 |doi=  10.1016/0167-4781(85)90006-5}}
*{{cite journal  | author=Ohlsson A, Cumming WA, Paul A, Sly WS |title=Carbonic anhydrase II deficiency syndrome: recessive osteopetrosis with renal tubular acidosis and cerebral calcification. |journal=Pediatrics |volume=77 |issue= 3 |pages= 371-81 |year= 1986 |pmid= 3081869 |doi=  }}
*{{cite journal  | vauthors=Ohlsson A, Cumming WA, Paul A, Sly WS |title=Carbonic anhydrase II deficiency syndrome: recessive osteopetrosis with renal tubular acidosis and cerebral calcification. |journal=Pediatrics |volume=77 |issue= 3 |pages= 371–81 |year= 1986 |pmid= 3081869 |doi=  }}
*{{cite journal  | author=Nakai H, Byers MG, Venta PJ, ''et al.'' |title=The gene for human carbonic anhydrase II (CA2) is located at chromosome 8q22. |journal=Cytogenet. Cell Genet. |volume=44 |issue= 4 |pages= 234-5 |year= 1987 |pmid= 3107918 |doi=  }}
*{{cite journal  | vauthors=Nakai H, Byers MG, Venta PJ |title=The gene for human carbonic anhydrase II (CA2) is located at chromosome 8q22. |journal=Cytogenet. Cell Genet. |volume=44 |issue= 4 |pages= 234–5 |year= 1987 |pmid= 3107918 |doi=10.1159/000132378 |display-authors=etal}}
*{{cite journal  | author=Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D |title=Nucleotide sequence of human liver carbonic anhydrase II cDNA. |journal=Nucleic Acids Res. |volume=15 |issue= 11 |pages= 4687 |year= 1987 |pmid= 3108857 |doi= }}
*{{cite journal  | vauthors=Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D |title=Nucleotide sequence of human liver carbonic anhydrase II cDNA. |journal=Nucleic Acids Res. |volume=15 |issue= 11 |pages= 4687 |year= 1987 |pmid= 3108857 |doi=10.1093/nar/15.11.4687  | pmc=340889  }}
*{{cite journal  | author=Murakami H, Marelich GP, Grubb JH, ''et al.'' |title=Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II. |journal=Genomics |volume=1 |issue= 2 |pages= 159-66 |year= 1988 |pmid= 3121496 |doi=  }}
*{{cite journal  | vauthors=Murakami H, Marelich GP, Grubb JH |title=Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II. |journal=Genomics |volume=1 |issue= 2 |pages= 159–66 |year= 1988 |pmid= 3121496 |doi=10.1016/0888-7543(87)90008-5  |display-authors=etal}}
*{{cite journal  | author=Eriksson AE, Jones TA, Liljas A |title=Refined structure of human carbonic anhydrase II at 2.0 A resolution. |journal=Proteins |volume=4 |issue= 4 |pages= 274-82 |year= 1989 |pmid= 3151019 |doi= 10.1002/prot.340040406 }}
*{{cite journal  | vauthors=Eriksson AE, Jones TA, Liljas A |title=Refined structure of human carbonic anhydrase II at 2.0 A resolution. |journal=Proteins |volume=4 |issue= 4 |pages= 274–82 |year= 1989 |pmid= 3151019 |doi= 10.1002/prot.340040406 }}
*{{cite journal  | author=Eriksson AE, Kylsten PM, Jones TA, Liljas A |title=Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH. |journal=Proteins |volume=4 |issue= 4 |pages= 283-93 |year= 1989 |pmid= 3151020 |doi= 10.1002/prot.340040407 }}
*{{cite journal  | vauthors=Eriksson AE, Kylsten PM, Jones TA, Liljas A |title=Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH. |journal=Proteins |volume=4 |issue= 4 |pages= 283–93 |year= 1989 |pmid= 3151020 |doi= 10.1002/prot.340040407 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=760}}
{{Carbonic anhydrases}}
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Latest revision as of 08:40, 10 January 2019

"CA II" redirects here. For the spectral features of calcium, see Calcium § H and K lines.
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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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Wikidata
View/Edit Human

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. Renal carbonic anhydrase allows the reabsorption of bicarbonate ions in the proximal tubule. [1] Loss of carbonic anhydrase activity in bones impairs the ability of osteoclasts to promote bone resorption, leading to osteopetrosis. [2]

Interactions

Carbonic anhydrase II has been shown to interact with band 3[3][4][5][6] and sodium-hydrogen antiporter 1.[7]

References

  1. ↑ "Entrez Gene: CA2 carbonic anhydrase II".
  2. ↑ Reference, Genetics Home. "Osteopetrosis". Genetics Home Reference. Retrieved 2018-10-31.
  3. ↑ 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. United States. 276 (51): 47886–94. doi:10.1074/jbc.M105959200. ISSN 0021-9258. PMID 11606574.
  4. ↑ 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. UNITED STATES. 273 (43): 28430–7. doi:10.1074/jbc.273.43.28430. ISSN 0021-9258. PMID 9774471.
  5. ↑ 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. UNITED STATES. 39 (44): 13344–9. doi:10.1021/bi0015111. ISSN 0006-2960. PMID 11063570.
  6. ↑ 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. UNITED STATES. 39 (18): 5527–33. doi:10.1021/bi992564p. ISSN 0006-2960. PMID 10820026.
  7. ↑ 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. United States. 277 (39): 36085–91. doi:10.1074/jbc.M111952200. ISSN 0021-9258. PMID 12138085.

Further reading



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