CA1 (gene)
| Carbonic anhydrase I |
PDB rendering based on 1azm. |
| Available structures |
| PDB |
1AZM, 1BZM, 1CRM, 1CZM, 1HCB, 1HUG, 1HUH, 1J9W, 1JV0, 2CAB, 2FOY, 2FW4, 2IT4, 2NMX, 2NN1, 2NN7, 3LXE |
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| Identifiers |
| Symbols |
CA1; CA-I; CAB; Car1 |
| External IDs |
OMIM: 114800 MGI: 88268 HomoloGene: 20414 GeneCards: CA1 Gene |
| EC number |
4.2.1.1 |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
759 |
12346 |
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| Ensembl |
ENSG00000133742 |
ENSMUSG00000027556 |
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| UniProt |
P00915 |
n/a |
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| RefSeq (mRNA) |
NM_001128829.2 |
XM_978562 |
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| RefSeq (protein) |
NP_001122301.1 |
XP_983656 |
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| Location (UCSC) |
Chr 8:
86.24 – 86.29 Mb |
Chr 3:
14.77 – 14.78 Mb |
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| PubMed search |
[1] |
[2] |
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Carbonic anhydrase 1 is an enzyme that in humans is encoded by the CA1 gene.[1][2]
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 cellular 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.[2]
References
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 (1): 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. doi:10.1126/science.406674. 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. doi:10.1073/pnas.72.1.51. PMC 432238. PMID 804171. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=432238.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
- 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. doi:10.1016/0378-1119(90)90236-K. 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. doi:10.1111/j.1600-0714.1986.tb00604.x. PMID 3088232.
- Barlow JH, Lowe N, Edwards YH, Butterworth PH (1987). "Human carbonic anhydrase I cDNA.". Nucleic Acids Res. 15 (5): 2386. doi:10.1093/nar/15.5.2386. PMC 340641. PMID 3104879. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=340641.
- 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. doi:10.1111/j.1469-1809.1986.tb01030.x. 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. doi:10.1016/S0300-9084(74)80093-3. 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. doi:10.1016/0006-291X(72)90400-7. 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. PMC 1684865. PMID 6781336. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1684865.
- 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.
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PDB gallery
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1azm: DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I
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1bzm: DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I
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1crm: STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES
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1czm: DRUG-PROTEIN INTERACTIONS: STRUCTURE OF SULFONAMIDE DRUG COMPLEXED WITH HUMAN CARBONIC ANHYDRASE I
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1hcb: ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE
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1hug: DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES
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1huh: DIFFERENCES IN ANIONIC INHIBITION OF HUMAN CARBONIC ANHYDRASE I REVEALED FROM THE STRUCTURES OF IODIDE AND GOLD CYANIDE INHIBITOR COMPLEXES
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1j9w: Solution Structure of the CAI Michigan 1 Variant
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1jv0: THE CRYSTAL STRUCTURE OF THE ZINC(II) ADDUCT OF THE CAI MICHIGAN 1 VARIANT
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2cab: STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I
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2foy: Human Carbonic Anhydrase I complexed with a two-prong inhibitor
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2fw4: Carbonic anhydrase activators. The first X-ray crystallographic study of an activator of isoform I, structure with L-histidine.
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2nmx: Structure of inhibitor binding to Carbonic Anhydrase I
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2nn1: Structure of inhibitor binding to Carbonic Anhydrase I
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2nn7: Structure of inhibitor binding to Carbonic Anhydrase I
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