CA1 (gene)

Carbonic anhydrase I, also known as CA1, is a human gene.cite web | title = Entrez Gene: CA1 carbonic anhydrase I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=759| accessdate = ]

PBB_Summary
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summary_text = 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. CA1 is closely linked to CA2 and CA3 genes on chromosome 8, and it encodes a cytosolic protein which is found at the highest level in erythrocytes. Transcript variants of CA1 utilizing alternative polyA_sites have been described in literature.cite web | title = Entrez Gene: CA1 carbonic anhydrase I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=759| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Tashian RE, Carter ND |title=Biochemical genetics of carbonic anhydrase. |journal=Adv. Hum. Genet. |volume=7 |issue= |pages= 1–56 |year= 1977 |pmid= 827930 |doi=
*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 | author=Kendall AG, Tashian RE |title=Erythrocyte carbonic anhydrase I: inherited deficiency in humans. |journal=Science |volume=197 |issue= 4302 |pages= 471–2 |year= 1977 |pmid= 406674 |doi=
*cite journal | author=Kannan KK, Notstrand B, Fridborg K, "et al." |title=Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=72 |issue= 1 |pages= 51–5 |year= 1975 |pmid= 804171 |doi=
*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 | author=Lowe N, Edwards YH, Edwards M, Butterworth PH |title=Physical mapping of the human carbonic anhydrase gene cluster on chromosome 8. |journal=Genomics |volume=10 |issue= 4 |pages= 882–8 |year= 1991 |pmid= 1916821 |doi=
*cite journal | author=Lowe N, Brady HJ, Barlow JH, "et al." |title=Structure and methylation patterns of the gene encoding human carbonic anhydrase I. |journal=Gene |volume=93 |issue= 2 |pages= 277–83 |year= 1990 |pmid= 2121614 |doi=
*cite journal | author=Noda Y, Sumitomo S, Hikosaka N, Mori M |title=Immunohistochemical observations on carbonic anhydrase I and II in human salivary glands and submandibular obstructive adenitis. |journal=J. Oral Pathol. |volume=15 |issue= 4 |pages= 187–90 |year= 1986 |pmid= 3088232 |doi=
*cite journal | author=Barlow JH, Lowe N, Edwards YH, Butterworth PH |title=Human carbonic anhydrase I cDNA. |journal=Nucleic Acids Res. |volume=15 |issue= 5 |pages= 2386 |year= 1987 |pmid= 3104879 |doi=
*cite journal | author=Edwards YH, Barlow JH, Konialis CP, "et al." |title=Assignment of the gene determining human carbonic anhydrase, CAI, to chromosome 8. |journal=Ann. Hum. Genet. |volume=50 |issue= Pt 2 |pages= 123–9 |year= 1988 |pmid= 3124707 |doi=
*cite journal | author=Lin KT, Deutsch HF |title=Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. |journal=J. Biol. Chem. |volume=249 |issue= 8 |pages= 2329–37 |year= 1974 |pmid= 4207120 |doi=
*cite journal | author=Giraud N, Marriq C, Laurent-Tabusse G |title= [Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)] |journal=Biochimie |volume=56 |issue= 8 |pages= 1031–43 |year= 1975 |pmid= 4217196 |doi=
*cite journal | author=Andersson B, Nyman PO, Strid L |title=Amino acid sequence of human erythrocyte carbonic anhydrase B. |journal=Biochem. Biophys. Res. Commun. |volume=48 |issue= 3 |pages= 670–7 |year= 1972 |pmid= 4625868 |doi=
*cite journal | author=Lin KT, Deutsch HF |title=Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B. |journal=J. Biol. Chem. |volume=248 |issue= 6 |pages= 1885–93 |year= 1973 |pmid= 4632246 |doi=
*cite journal | author=Omoto K, Ueda S, Goriki K, "et al." |title=Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam. |journal=Am. J. Hum. Genet. |volume=33 |issue= 1 |pages= 105–11 |year= 1981 |pmid= 6781336 |doi=
*cite journal | author=Chegwidden WR, Wagner LE, Venta PJ, "et al." |title=Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I. |journal=Hum. Mutat. |volume=4 |issue= 4 |pages= 294–6 |year= 1995 |pmid= 7866410 |doi= 10.1002/humu.1380040411
*cite journal | author=Bekku S, Mochizuki H, Takayama E, "et al." |title=Carbonic anhydrase I and II as a differentiation marker of human and rat colonic enterocytes. |journal=Research in experimental medicine. Zeitschrift für die gesamte experimentelle Medizin einschliesslich experimenteller Chirurgie |volume=198 |issue= 4 |pages= 175–85 |year= 1999 |pmid= 9879596 |doi=
*cite journal | author=Puscas I, Coltau M, Baican M, "et al." |title=Vasoconstrictive drugs increase carbonic anhydrase I in vascular smooth muscle while vasodilating drugs reduce the activity of this isozyme by a direct mechanism of action. |journal=Drugs under experimental and clinical research |volume=27 |issue= 2 |pages= 53–60 |year= 2001 |pmid= 11392054 |doi=

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