CA1 (gene)

Carbonic anhydrase I
PDB rendering based on 1azm.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1azm​, 1bzm​, 1crm​, 1czm​, 1hcb​, 1hug​, 1huh​, 1j9w​, 1jv0​, 2cab​, 2foy​, 2fw4​, 2nmx​, 2nn1​, 2nn7​
Identifiers
Symbols	CA1 ; Car1
External IDs	Template:OMIM5 Template:MGI HomoloGene: 20414
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Carbonic anhydrase I, also known as CA1, is a human gene.

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.

Further reading

• Tashian RE, Carter ND (1977). "Biochemical genetics of carbonic anhydrase". Adv. Hum. Genet. 7: 1–56. PMID 827930.
• 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.
• Kendall AG, Tashian RE (1977). "Erythrocyte carbonic anhydrase I: inherited deficiency in humans". Science. 197 (4302): 471–2. PMID 406674.
• Kannan KK, Notstrand B, Fridborg K; et al. (1975). "Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution". Proc. Natl. Acad. Sci. U.S.A. 72 (1): 51–5. PMID 804171.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. PMID 1602151.
• Lowe N, Edwards YH, Edwards M, Butterworth PH (1991). "Physical mapping of the human carbonic anhydrase gene cluster on chromosome 8". Genomics. 10 (4): 882–8. PMID 1916821.CS1 maint: Multiple names: authors list (link)
• Lowe N, Brady HJ, Barlow JH; et al. (1990). "Structure and methylation patterns of the gene encoding human carbonic anhydrase I.". Gene. 93 (2): 277–83. PMID 2121614.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Noda Y, Sumitomo S, Hikosaka N, Mori M (1986). "Immunohistochemical observations on carbonic anhydrase I and II in human salivary glands and submandibular obstructive adenitis". J. Oral Pathol. 15 (4): 187–90. PMID 3088232.CS1 maint: Multiple names: authors list (link)
• Barlow JH, Lowe N, Edwards YH, Butterworth PH (1987). "Human carbonic anhydrase I cDNA". Nucleic Acids Res. 15 (5): 2386. PMID 3104879.CS1 maint: Multiple names: authors list (link)
• Edwards YH, Barlow JH, Konialis CP; et al. (1988). "Assignment of the gene determining human carbonic anhydrase, CAI, to chromosome 8". Ann. Hum. Genet. 50 (Pt 2): 123–9. PMID 3124707.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lin KT, Deutsch HF (1974). "Human carbonic anhydrases. XII. The complete primary structure of the C isozyme". J. Biol. Chem. 249 (8): 2329–37. PMID 4207120.
• Giraud N, Marriq C, Laurent-Tabusse G (1975). "[Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)]". Biochimie. 56 (8): 1031–43. PMID 4217196.CS1 maint: Multiple names: authors list (link)
• Andersson B, Nyman PO, Strid L (1972). "Amino acid sequence of human erythrocyte carbonic anhydrase B.". Biochem. Biophys. Res. Commun. 48 (3): 670–7. PMID 4625868.CS1 maint: Multiple names: authors list (link)
• Lin KT, Deutsch HF (1973). "Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B.". J. Biol. Chem. 248 (6): 1885–93. PMID 4632246.
• Omoto K, Ueda S, Goriki K; et al. (1981). "Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam". Am. J. Hum. Genet. 33 (1): 105–11. PMID 6781336.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chegwidden WR, Wagner LE, Venta PJ; et al. (1995). "Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I.". Hum. Mutat. 4 (4): 294–6. doi:10.1002/humu.1380040411. PMID 7866410.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bekku S, Mochizuki H, Takayama E; et al. (1999). "Carbonic anhydrase I and II as a differentiation marker of human and rat colonic enterocytes". Research in experimental medicine. Zeitschrift für die gesamte experimentelle Medizin einschliesslich experimenteller Chirurgie. 198 (4): 175–85. PMID 9879596.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Puscas I, Coltau M, Baican M; et al. (2001). "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". Drugs under experimental and clinical research. 27 (2): 53–60. PMID 11392054.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)