CA1 (gene)

From Wikipedia, the free encyclopedia

Carbonic anhydrase I

PDB rendering based on 1azm.

Available structures: 1azm, 1bzm, 1crm, 1czm, 1hcb, 1hug, 1huh, 1j9w, 1jv0, 2cab, 2foy, 2fw4, 2nmx, 2nn1, 2nn7

Identifiers

Symbol(s)

CA1; Car1

External IDs

OMIM: 114800 MGI: 88268 HomoloGene: 20414

Gene ontology
Molecular Function:	• carbonate dehydratase activity • zinc ion binding • lyase activity • metal ion binding
Cellular Component:	• cytoplasm
Biological Process:	• one-carbon compound metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_001738 (mRNA)
NP_001729 (protein)

XM_978562 (mRNA)
XP_983656 (protein)

Location

Chr 8: 86.43 - 86.48 Mb

n/a

Pubmed search

[1]

[2]

Carbonic anhydrase I, also known as CA1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CA1 carbonic anhydrase I.

[edit] 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.
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.
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.
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.
Barlow JH, Lowe N, Edwards YH, Butterworth PH (1987). "Human carbonic anhydrase I cDNA.". Nucleic Acids Res. 15 (5): 2386. PMID 3104879.
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.
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.
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.
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.
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.
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.
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.