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Showing drug card for Acetazolamide (DB00819)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:14
Primary Accession Number DB00819
Secondary Accession Number
  • APRD00119
  • EXPT00604
Name Acetazolamide
Drug Type
  • Approved
  • Small Molecule
Description One of the carbonic anhydrase inhibitors that is sometimes effective against absence seizures. It is sometimes useful also as an adjunct in the treatment of tonic-clonic, myoclonic, and atonic seizures, particularly in women whose seizures occur or are exacerbated at specific times in the menstrual cycle. However, its usefulness is transient often because of rapid development of tolerance. Its antiepileptic effect may be due to its inhibitory effect on brain carbonic anhydrase, which leads to an increased transneuronal chloride gradient, increased chloride current, and increased inhibition. (From Smith and Reynard, Textbook of Pharmacology, 1991, p337)
Synonyms
  1. Acetamidothiadiazolesulfonamide
  2. Acetazolamid
  3. Acetazolamide Sodium
  4. Acetazolamine
  5. Acetazoleamide
  6. Acetozalamide
  7. Carbonic Anhydrase Inhibitor 6063
Brand Names
  1. Acetamox
  2. Acetazolam
  3. Ak-Zol
  4. Apo-Acetazolamide
  5. Atenezol
  6. Cidamex
  7. Dazamide
  8. Defiltran
  9. Dehydratin
  10. Diacarb
  11. Diakarb
  12. Diamox
  13. Diamox Sequels
  14. Didoc
  15. Diluran
  16. Diuramid
  17. Diureticum-Holzinger
  18. Diuriwas
  19. Diutazol
  20. Donmox
  21. Duiramid
  22. Edemox
  23. Eumicton
  24. Fonurit
  25. Glaupax
  26. Glupax
  27. Natrionex
  28. Nephramid
  29. Nephramide
  30. Phonurit
  31. Sk-Acetazolamide
  32. Storzolamide
  33. Vetamox
Brand Mixtures Not Available
Chemical IUPAC Name N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)acetamide
Chemical Formula C4H6N4O3S2
Chemical Structure Structure
CAS Registry Number 59-66-5
InChI Identifier InChI=1/C4H6N4O3S2/c1-2(9)6-3-7-8-4(12-3)13(5,10)11/h1H3,(H2,5,10,11)(H,6,7,9)/f/h6H,5H2
InChI Key BZKPWHYZMXOIDC-WQDBGGICCO
KEGG Drug D00218 Link Image
KEGG Compound C06805 Link Image
PubChem Compound 1986 Link Image
PubChem Substance 9024 Link Image
ChEBI ID 27690 Link Image
PharmGKB ID PA448018 Link Image
HET ID AZM Link Image
GenBank ID Not Available
Drug ID Number [DIN] 00545015 Link Image
RxList Link http://www.rxlist.com/cgi/generic/aceta.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Acetazolamide Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 222.2450
Monoisotopic Molecular Weight 221.9881
State Solid
Melting Point 260.5 oC
Experimental Water Solubility 0.98 mg/mL at 30 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 2.79e+00 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.26 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP -0.39 Calculated using ALOGPS
Experimental LogS -2.36 [ADME Research, USCD]
Predicted LogS -1.90 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 7.2
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1CZM Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES CC(=O)NC1=NN=C(S1)S(N)(=O)=O
Canonical SMILES CC(=O)NC1=NN=C(S1)S(N)(=O)=O
Drug Category
  • Anticonvulsants
  • Carbonic Anhydrase Inhibitors
  • Diuretics
ATC Codes
AHFS Codes
  • 52:10.00
Indication For adjunctive treatment of: edema due to congestive heart failure; drug-induced edema; centrencephalic epilepsies; chronic simple (open-angle) glaucoma
Pharmacology Acetazolamide is a potent carbonic anhydrase inhibitor, effective in the control of fluid secretion, in the treatment of certain convulsive disorders and in the promotion of diuresis in instances of abnormal fluid retention. Acetazolamide is not a mercurial diuretic. Rather, it is a nonbacteriostatic sulfonamide possessing a chemical structure and pharmacological activity distinctly different from the bacteriostatic sulfonamides.
Mechanism of Action The anticonvulsant activity of Acetazolamide may depend on a direct inhibition of carbonic anhydrase in the CNS, which decreases carbon dioxide tension in the pulmonary alveoli, thus increasing arterial oxygen tension. The diuretic effect depends on the inhibition of carbonic anhydrase, causing a reduction in the availability of hydrogen ions for active transport in the renal tubule lumen. This leads to alkaline urine and an increase in the excretion of bicarbonate, sodium, potassium, and water.
Absorption Not Available
Toxicity Not Available
Protein Binding 98%
Biotransformation Not Available
Half Life 3 to 9 hours
Dosage Forms
Form Route
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Aspirin The salicylate at high dose increases the effect of the carbonic anhydrase inhibitors
Bismuth Subsalicylate The salicylate at high dose increases the effect of the carbonic anhydrase inhibitors
Cyclosporine Acetazolamide increases the effect of toxicity of cyclosporine
Memantine Possible increased levels of memantine
Salicyclic acid The salicylate at high dose increases the effect of the carbonic anhydrase inhibitors
Food Interactions
  • Drink plenty of liquids.
  • Take with food; at least 6 hours before bedtime.
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Carbonic anhydrase 1
  2. Carbonic anhydrase 2
  3. Aquaporin-1
  4. Carbonic anhydrase 12
  5. Carbonic anhydrase 14
Drug Target 1 [top]
Target 1 ID 295
Target 1 Name Carbonic anhydrase 1
Target 1 Synonyms
  1. CA-I
  2. Carbonate dehydratase I
  3. Carbonic anhydrase I
  4. EC 4.2.1.1
Target 1 Gene Name CA1
Target 1 Protein Sequence >Carbonic anhydrase 1 
ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEII
NVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHV
AHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFD
PSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVP
MQHNNRPTQPLKGRTVRASF
Target 1 Number of Residues 264
Target 1 Molecular Weight 28739
Target 1 Theoretical pI 7.14
Target 1 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
carbonate dehydratase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 1 General Function Inorganic ion transport and metabolism
Target 1 Specific Function Reversible hydration of carbon dioxide
Target 1 Pathways
Name SMPDB Link KEGG Link
Nitrogen metabolism map00910 Link Image
Target 1 Reactions
  • H2CO3 = CO2 + H2O
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 29600 Link Image
Target 1 UniProtKB/Swiss-Prot ID P00915 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name CAH1_HUMAN Link Image
Target 1 PDB ID 1CZM Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasm
Target 1 Gene Sequence >786 bp 
ATGGCAAGTCCAGACTGGGGATATGATGACAAAAATGGTCCTGAACAATGGAGCAAGCTG
TATCCCATTGCCAATGGAAATAACCAATCCCCTGTTGATATTAAAACCAGTGAAACCAAA
CATGACACCTCTCTGAAACCTATTAGTGTCTCCTACAACCCAGCCACAGCCAAAGAAATT
ATCAATGTGGGGCATTCTTTCCATGTAAATTTTGAGGACAACGATAACCGATCAGTGCTG
AAAGGTGGTCCTTTCTCTGACAGCTACAGGCTCTTTCAGTTTCATTTTCACTGGGGCAGT
ACAAATGAGCATGGTTCAGAACATACAGTGGATGGAGTCAAATATTCTGCCGAGCTTCAC
GTAGCTCACTGGAATTCTGCAAAGTACTCCAGCCTTGCTGAAGCTGCCTCAAAGGCTGAT
GGTTTGGCAGTTATTGGTGTTTTGATGAAGGTTGGTGAGGCCAACCCAAAGCTGCAGAAA
GTACTTGATGCCCTCCAAGCAATTAAAACCAAGGGCAAACGAGCCCCATTCACAAATTTT
GACCCCTCTACTCTCCTTCCTTCATCCCTGGATTTCTGGACCTACCCTGGCTCTCTGACT
CATCCTCCTCTTTATGAGAGTGTAACTTGGATCATCTGTAAGGAGAGCATCAGTGTCAGC
TCAGAGCAGCTGGCACAATTCCGCAGCCTTCTATCAAATGTTGAAGGTGATAACGCTGTC
CCCATGCAGCACAACAACCGCCCAACCCAACCTCTGAAGGGCAGAACAGTGAGAGCTTCA
TTTTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID CA1 Link Image
Target 1 GenAtlas ID CA1 Link Image
Target 1 HGNC ID HGNC:1368 Link Image
Target 1 Chromosome Location 8
Target 1 Locus 8q13-q22.1
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Lowe N, Brady HJ, Barlow JH, Sowden JC, Edwards M, Butterworth PH: Structure and methylation patterns of the gene encoding human carbonic anhydrase I. Gene. 1990 Sep 14;93(2):277-83. [PubMed Link Image]
  2. Barlow JH, Lowe N, Edwards YH, Butterworth PH: Human carbonic anhydrase I cDNA. Nucleic Acids Res. 1987 Mar 11;15(5):2386. [PubMed Link Image]
  3. Lin KT, Deutsch HF: Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. J Biol Chem. 1974 Apr 25;249(8):2329-37. [PubMed Link Image]
  4. Giraud N, Marriq C, Laurent-Tabusse G: [Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260)] Biochimie. 1974;56(8):1031-43. [PubMed Link Image]
  5. Andersson B, Nyman PO, Strid L: Amino acid sequence of human erythrocyte carbonic anhydrase B. Biochem Biophys Res Commun. 1972 Aug 7;48(3):670-7. [PubMed Link Image]
  6. Lin KT, Deutsch HF: Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B. J Biol Chem. 1973 Mar 25;248(6):1885-93. [PubMed Link Image]
  7. Omoto K, Ueda S, Goriki K, Takahashi N, Misawa S, Pagaran IG: Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam. Am J Hum Genet. 1981 Jan;33(1):105-11. [PubMed Link Image]
  8. Chegwidden WR, Wagner LE, Venta PJ, Bergenhem NC, Yu YS, Tashian RE: 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. 1994;4(4):294-6. [PubMed Link Image]
  9. Kannan KK, Notstrand B, Fridborg K, Lovgren S, Ohlsson A, Petef M: 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. 1975 Jan;72(1):51-5. [PubMed Link Image]
Target 1 Drug References
  1. Meierkord H, Grunig F, Gutschmidt U, Gutierrez R, Pfeiffer M, Draguhn A, Bruckner C, Heinemann U: Sodium bromide: effects on different patterns of epileptiform activity, extracellular pH changes and GABAergic inhibition. Naunyn Schmiedebergs Arch Pharmacol. 2000 Jan;361(1):25-32. [PubMed Link Image]
  2. Puscas I, Coltau M, Baican M, Domuta G, Hecht A: Vasodilatory effect of diuretics is dependent on inhibition of vascular smooth muscle carbonic anhydrase by a direct mechanism of action. Drugs Exp Clin Res. 1999;25(6):271-9. [PubMed Link Image]
  3. Puscas I, Ifrim M, Maghiar T, Coltau M, Domuta G, Baican M, Hecht A: Indomethacin activates carbonic anhydrase and antagonizes the effect of the specific carbonic anhydrase inhibitor acetazolamide, by a direct mechanism of action. Int J Clin Pharmacol Ther. 2001 Jun;39(6):265-70. [PubMed Link Image]
  4. Perez Velazquez JL: Bicarbonate-dependent depolarizing potentials in pyramidal cells and interneurons during epileptiform activity. Eur J Neurosci. 2003 Sep;18(5):1337-42. [PubMed Link Image]
  5. Puscas I, Coltau M, Pasca R: Nonsteroidal anti-inflammatory drugs activate carbonic anhydrase by a direct mechanism of action. J Pharmacol Exp Ther. 1996 Jun;277(3):1464-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 357
Target 2 Name Carbonic anhydrase 2
Target 2 Synonyms
  1. CA-II
  2. Carbonate dehydratase II
  3. Carbonic anhydrase C
  4. Carbonic anhydrase II
  5. EC 4.2.1.1
Target 2 Gene Name CA2
Target 2 Protein Sequence >Carbonic anhydrase 2 
SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILN
NGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV
HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPR
GLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK
Target 2 Number of Residues 263
Target 2 Molecular Weight 29115
Target 2 Theoretical pI 7.47
Target 2 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
carbonate dehydratase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 2 General Function Inorganic ion transport and metabolism
Target 2 Specific Function Reversible hydration of carbon dioxide
Target 2 Pathways
Name SMPDB Link KEGG Link
Nitrogen metabolism map00910 Link Image
Target 2 Reactions
  • H2CO3 = CO2 + H2O
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 179780 Link Image
Target 2 UniProtKB/Swiss-Prot ID P00918 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CAH2_HUMAN Link Image
Target 2 PDB ID 1T9N Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasm
Target 2 Gene Sequence >783 bp 
ATGTCCCATCACTGGGGGTACGGCAAACACAACGGACCTGAGCACTGGCATAAGGACTTC
CCCATTGCCAAGGGAGAGCGCCAGTCCCCTGTTGACATCGACACTCATACAGCCAAGTAT
GACCCTTCCCTGAAGCCCCTGTCTGTTTCCTATGATCAAGCAACTTCCCTGAGGATCCTC
AACAATGGTCATGCTTTCAACGTGGAGTTTGATGACTCTCAGGACAAAGCAGTGCTCAAG
GGAGGACCCCTGGATGGCACTTACAGATTGATTCAGTTTCACTTTCACTGGGGTTCACTT
GATGGACAAGGTTCAGAGCATACTGTGGATAAAAAGAAATATGCTGCAGAACTTCACTTG
GTTCACTGGAACACCAAATATGGGGATTTTGGGAAAGCTGTGCAGCAACCTGATGGACTG
GCCGTTCTAGGTATTTTTTTGAAGGTTGGCAGCGCTAAACCGGGCCTTCAGAAAGTTGTT
GATGTGCTGGATTCCATTAAAACAAAGGGCAAGAGTGCTGACTTCACTAACTTCGATCCT
CGTGGCCTCCTTCCTGAATCCTTGGATTACTGGACCTACCCAGGCTCACTGACCACCCCT
CCTCTTCTGGAATGTGTGACCTGGATTGTGCTCAAGGAACCCATCAGCGTCAGCAGCGAG
CAGGTGTTGAAATTCCGTAAACTTAACTTCAATGGGGAGGGTGAACCCGAAGAACTGATG
GTGGACAACTGGCGCCCAGCTCAGCCACTGAAGAACAGGCAAATCAAAGCTTCCTTCAAA
TAA
Target 2 GenBank Gene ID
Target 2 GeneCard ID CA2 Link Image
Target 2 GenAtlas ID CA2 Link Image
Target 2 HGNC ID HGNC:1373 Link Image
Target 2 Chromosome Location 8
Target 2 Locus 8q22
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Cox JD, Hunt JA, Compher KM, Fierke CA, Christianson DW: Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II. Biochemistry. 2000 Nov 14;39(45):13687-94. [PubMed Link Image]
  2. Roth DE, Venta PJ, Tashian RE, Sly WS: Molecular basis of human carbonic anhydrase II deficiency. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1804-8. [PubMed Link Image]
  3. Venta PJ, Welty RJ, Johnson TM, Sly WS, Tashian RE: 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. Am J Hum Genet. 1991 Nov;49(5):1082-90. [PubMed Link Image]
  4. Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE: Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements. Biochim Biophys Acta. 1985 Dec 18;826(4):195-201. [PubMed Link Image]
  5. Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D: Nucleotide sequence of human liver carbonic anhydrase II cDNA. Nucleic Acids Res. 1987 Jun 11;15(11):4687. [PubMed Link Image]
  6. Murakami H, Marelich GP, Grubb JH, Kyle JW, Sly WS: Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II. Genomics. 1987 Oct;1(2):159-66. [PubMed Link Image]
  7. Eriksson AE, Jones TA, Liljas A: Refined structure of human carbonic anhydrase II at 2.0 A resolution. Proteins. 1988;4(4):274-82. [PubMed Link Image]
  8. Eriksson AE, Kylsten PM, Jones TA, Liljas A: Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH. Proteins. 1988;4(4):283-93. [PubMed Link Image]
  9. Lin KT, Deutsch HF: Human carbonic anhydrases. XII. The complete primary structure of the C isozyme. J Biol Chem. 1974 Apr 25;249(8):2329-37. [PubMed Link Image]
  10. Liljas A, Kannan KK, Bergsten PC, Waara I, Fridborg K, Strandberg B, Carlbom U, Jarup L, Lovgren S, Petef M: Crystal structure of human carbonic anhydrase C. Nat New Biol. 1972 Feb 2;235(57):131-7. [PubMed Link Image]
  11. 6407977 Jones GL, Shaw DC: A chemical and enzymological comparison of the common major human erythrocyte carbonic anhydrase II, its minor component, and a new genetic variant, CA II Melbourne (237 Pro leads to His). Hum Genet. 1983;63(4):392-9.
  12. 6817747 Jones GL, Sofro AS, Shaw DC: Chemical and enzymological characterization of an Indonesian variant of human erythrocyte carbonic anhydrase II, CAII Jogjakarta (17 Lys leads to Glu). Biochem Genet. 1982 Oct;20(9-10):979-1000.
  13. 823150 Henderson LE, Henriksson D, Nyman PO: Primary structure of human carbonic anhydrase C. J Biol Chem. 1976 Sep 25;251(18):5457-63.
  14. 8834238 Soda H, Yukizane S, Yoshida I, Koga Y, Aramaki S, Kato H: A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese patients with carbonic anhydrase II deficiency with central nervous system involvement. Hum Genet. 1996 Apr;97(4):435-7.
  15. 9143915 Hu PY, Lim EJ, Ciccolella J, Strisciuglio P, Sly WS: Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis. Hum Mutat. 1997;9(5):383-7.
  16. 9541386 Stams T, Chen Y, Boriack-Sjodin PA, Hurt JD, Liao J, May JA, Dean T, Laipis P, Silverman DN, Christianson DW: Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination. Protein Sci. 1998 Mar;7(3):556-63.
Target 2 Drug References Not Available
Drug Target 3 [top]
Target 3 ID 1025
Target 3 Name Aquaporin-1
Target 3 Synonyms
  1. AQP-1
  2. Aquaporin-CHIP
  3. Urine water channel
  4. Water channel protein for red blood cells and kidney proximal tubule
Target 3 Gene Name AQP1
Target 3 Protein Sequence >Aquaporin-1 
MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSI
ATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLT
GNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGH
LLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTD
RVKVWTSGQVEEYDLDADDINSRVEMKPK
Target 3 Number of Residues 273
Target 3 Molecular Weight 28526
Target 3 Theoretical pI 7.50
Target 3 GO Classification
Function
transporter activity
Process
physiological process
cellular physiological process
transport
Component
cell
membrane
intrinsic to membrane
integral to membrane
Target 3 General Function Carbohydrate transport and metabolism
Target 3 Specific Function Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • None
Target 3 Transmembrane Regions
  • 8-36
  • 49-66
  • 77-84
  • 95-115
  • 137-155
  • 167-183
  • 193-200
  • 208-228
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 180501 Link Image
Target 3 UniProtKB/Swiss-Prot ID P29972 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name AQP1_HUMAN Link Image
Target 3 PDB ID 1H6I Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Membrane
  • multi-pass membrane protein
Target 3 Gene Sequence >810 bp 
ATGGCCAGCGAGTTCAAGAAGAAGCTCTTCTGGAGGGCAGTGGTGGCCGAGTTCCTGGCC
ACGACCCTCTTTGTCTTCATCAGCATCGGTTCTGCCCTGGGCTTCAAATACCCGGTGGGG
AACAACCAGACGGCGGTCCAGGACAACGTGAAGGTGTCGCTGGCCTTCGGGCTGAGCATC
GCCACGCTGGCGCAGAGTGTGGGCCACATCAGCGGCGCCCACCTCAACCCGGCTGTCACA
CTGGGGCTGCTGCTCAGCTGCCAGATCAGCATCTTCCGTGCCCTCATGTACATCATCGCC
CAGTGCGTGGGGGCCATCGTCGCCACCGCCATCCTCTCAGGCATCACCTCCTCCCTGACT
GGGAACTCGCTTGGCCGCAATGACCTGGCTGATGGTGTGAACTCGGGCCAGGGCCTGGGC
ATCGAGATCATCGGGACCCTCCAGCTGGTGCTATGCGTGCTGGCTACTACCGACCGGAGG
CGCCGTGACCTTGGTGGCTCAGCCCCCCTTGCCATCGGCCTCTCTGTAGCCCTTGGACAC
CTCCTGGCTATTGACTACACTGGCTGTGGGATTAACCCTGCTCGGTCCTTTGGCTCCGCG
GTGATCACACACAACTTCAGCAACCACTGGATTTTCTGGGTGGGGCCATTCATCGGGGGA
GCCCTGGCTGTACTCATCTACGACTTCATCCTGGCCCCACGCAGCAGTGACCTCACAGAC
CGCGTGAAGGTGTGGACCAGCGGCCAGGTGGAGGAGTATGACCTGGATGCCGACGACATC
AACTCCAGGGTGGAGATGAAGCCCAAATAG
Target 3 GenBank Gene ID
Target 3 GeneCard ID AQP1 Link Image
Target 3 GenAtlas ID AQP1 Link Image
Target 3 HGNC ID HGNC:633 Link Image
Target 3 Chromosome Location 7
Target 3 Locus 7p14
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann JB, Engel A, Fujiyoshi Y: Structural determinants of water permeation through aquaporin-1. Nature. 2000 Oct 5;407(6804):599-605. [PubMed Link Image]
  2. de Groot BL, Engel A, Grubmuller H: A refined structure of human aquaporin-1. FEBS Lett. 2001 Aug 31;504(3):206-11. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Preston GM, Carroll TP, Guggino WB, Agre P: Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 1992 Apr 17;256(5055):385-7. [PubMed Link Image]
  5. Preston GM, Agre P: Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11110-4. [PubMed Link Image]
  6. Preston GM, Jung JS, Guggino WB, Agre P: Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis. J Biol Chem. 1994 Jan 21;269(3):1668-73. [PubMed Link Image]
  7. Li X, Yu H, Koide SS: The water channel gene in human uterus. Biochem Mol Biol Int. 1994 Feb;32(2):371-7. [PubMed Link Image]
  8. Walz T, Smith BL, Agre P, Engel A: The three-dimensional structure of human erythrocyte aquaporin CHIP. EMBO J. 1994 Jul 1;13(13):2985-93. [PubMed Link Image]
  9. Preston GM, Smith BL, Zeidel ML, Moulds JJ, Agre P: Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. Science. 1994 Sep 9;265(5178):1585-7. [PubMed Link Image]
  10. Smith BL, Preston GM, Spring FA, Anstee DJ, Agre P: Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens. J Clin Invest. 1994 Sep;94(3):1043-9. [PubMed Link Image]
  11. 7677994 Preston GM, Jung JS, Guggino WB, Agre P: The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. J Biol Chem. 1993 Jan 5;268(1):17-20.
  12. 8340403 Moon C, Preston GM, Griffin CA, Jabs EW, Agre P: The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization. J Biol Chem. 1993 Jul 25;268(21):15772-8.
  13. 8703970 Ruiz A, Bok D: Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium. Biochim Biophys Acta. 1996 Jul 25;1282(2):174-8.
  14. 9177353 Walz T, Hirai T, Murata K, Heymann JB, Mitsuoka K, Fujiyoshi Y, Smith BL, Agre P, Engel A: The three-dimensional structure of aquaporin-1. Nature. 1997 Jun 5;387(6633):624-7.
Target 3 Drug References
  1. Xiang Y, Ma B, Li T, Yu HM, Li XJ: Acetazolamide suppresses tumor metastasis and related protein expression in mice bearing Lewis lung carcinoma. Acta Pharmacol Sin. 2002 Aug;23(8):745-51. [PubMed Link Image]
  2. Mu SM, Ji XH, Ma B, Yu HM, Li XJ: [Differential protein analysis in rat renal proximal tubule epithelial cells in response to acetazolamide and its relation with the inhibition of AQP1] Yao Xue Xue Bao. 2003 Mar;38(3):169-72. [PubMed Link Image]
  3. Ma B, Xiang Y, Mu SM, Li T, Yu HM, Li XJ: Effects of acetazolamide and anordiol on osmotic water permeability in AQP1-cRNA injected Xenopus oocyte. Acta Pharmacol Sin. 2004 Jan;25(1):90-7. [PubMed Link Image]
  4. Oshio K, Song Y, Verkman AS, Manley GT: Aquaporin-1 deletion reduces osmotic water permeability and cerebrospinal fluid production. Acta Neurochir Suppl. 2003;86:525-8. [PubMed Link Image]
  5. Xiang Y, Ma B, Li T, Gao JW, Yu HM, Li XJ: Acetazolamide inhibits aquaporin-1 protein expression and angiogenesis. Acta Pharmacol Sin. 2004 Jun;25(6):812-6. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 3007
Target 4 Name Carbonic anhydrase 12
Target 4 Synonyms
  1. CA-XII
  2. Carbonate dehydratase XII
  3. Carbonic anhydrase 12 precursor
  4. Carbonic anhydrase XII
  5. EC 4.2.1.1
  6. Tumor antigen HOM-RCC-3.1.3
Target 4 Gene Name CA12
Target 4 Protein Sequence >Carbonic anhydrase 12 precursor 
MPRRSLHAAAVLLLVILKEQPSSPAPVNGSKWTYFGPDGENSWSKKYPSCGGLLQSPIDL
HSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGLQSRYSATQLHL
HWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFN
PSYDKIFSHLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFR
NPVQISQEQLLALETALYCTHMDDPSPREMINNFRQVQKFDERLVYTSFSQVQVCTAAGL
SLGIILSLALAGILGICIVVVVSIWLFRRKSIKKGDNKGVIYKPATKMETEAHA
Target 4 Number of Residues 359
Target 4 Molecular Weight 39451
Target 4 Theoretical pI 7.24
Target 4 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
carbonate dehydratase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 4 General Function Inorganic ion transport and metabolism
Target 4 Specific Function Reversible hydration of carbon dioxide
Target 4 Pathways
Name SMPDB Link KEGG Link
Nitrogen metabolism map00910 Link Image
Target 4 Reactions
  • H2CO3 = CO2 + H2O
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-24
Target 4 Transmembrane Regions
  • 302-322
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 2984693 Link Image
Target 4 UniProtKB/Swiss-Prot ID O43570 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name CAH12_HUMAN Link Image
Target 4 PDB ID 1JD0 Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Membrane
  • single-pass type I membrane protein
Target 4 Gene Sequence >1065 bp 
ATGCCCCGGCGCAGCCTGCACGCGGCGGCCGTGCTCCTGCTGGTGATCTTAAAGGAACAG
CCTTCCAGCCCGGCCCCAGTGAACGGTTCCAAGTGGACTTATTTTGGTCCTGATGGGGAG
AATAGCTGGTCCAAGAAGTACCCGTCGTGTGGGGGCCTGCTGCAGTCCCCCATAGACCTG
CACAGTGACATCCTCCAGTATGACGCCAGCCTCACGCCCCTCGAGTTCCAAGGCTACAAT
CTGTCTGCCAACAAGCAGTTTCTCCTGACCAACAATGGCCATTCAGTGAAGCTGAACCTG
CCCTCGGACATGCACATCCAGGGCCTCCAGTCTCGCTACAGTGCCACGCAGCTGCACCTG
CACTGGGGGAACCCGAATGACCCGCACGGCTCTGAGCACACCGTCAGCGGACAGCACTTC
GCCGCCGAGCTGCACATTGTCCATTATAACTCAGACCTTTATCCTGACGCCAGCACTGCC
AGCAACAAGTCAGAAGGCCTCGCTGTCCTGGCTGTTCTCATTGAGATGGGCTCCTTCAAT
CCGTCCTATGACAAGATCTTCAGTCACCTTCAACATGTAAAGTACAAAGGCCAGGAAGCA
TTCGTCCCGGGATTCAACATTGAAGAGCTGCTTCCGGAGAGGACCGCTGAATATTACCGC
TACCGGGGGTCCCTGACCACACCCCCTTGCAACCCCACTGTGCTCTGGACAGTTTTCCGA
AACCCCGTGCAAATTTCCCAGGAGCAGCTGCTGGCTTTGGAGACAGCCCTGTACTGCACA
CACATGGACGACCCTTCCCCCAGAGAAATGATCAACAACTTCCGGCAGGTCCAGAAGTTC
GATGAGAGGCTGGTATACACCTCCTTCTCCCAAGTGCAAGTCTGTACTGCGGCAGGACTG
AGTCTGGGCATCATCCTCTCACTGGCCCTGGCTGGCATTCTTGGCATCTGTATTGTGGTG
GTGGTGTCCATTTGGCTTTTCAGAAGGAAGAGTATCAAAAAAGGTGATAACAAGGGAGTC
ATTTACAAGCCAGCCACCAAGATGGAGACTGAGGCCCACGCTTGA
Target 4 GenBank Gene ID
Target 4 GeneCard ID CA12 Link Image
Target 4 GenAtlas ID CA12 Link Image
Target 4 HGNC ID HGNC:1371 Link Image
Target 4 Chromosome Location 15
Target 4 Locus 15q22
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Whittington DA, Waheed A, Ulmasov B, Shah GN, Grubb JH, Sly WS, Christianson DW: Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells. Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9545-50. Epub 2001 Aug 7. [PubMed Link Image]
  2. Tureci O, Sahin U, Vollmar E, Siemer S, Gottert E, Seitz G, Parkkila AK, Shah GN, Grubb JH, Pfreundschuh M, Sly WS: Human carbonic anhydrase XII: cDNA cloning, expression, and chromosomal localization of a carbonic anhydrase gene that is overexpressed in some renal cell cancers. Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7608-13. [PubMed Link Image]
  3. Ivanov SV, Kuzmin I, Wei MH, Pack S, Geil L, Johnson BE, Stanbridge EJ, Lerman MI: Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes. Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12596-601. [PubMed Link Image]
Target 4 Drug References Not Available
Drug Target 5 [top]
Target 5 ID 3066
Target 5 Name Carbonic anhydrase 14
Target 5 Synonyms
  1. CA-XIV
  2. Carbonate dehydratase XIV
  3. Carbonic anhydrase 14 precursor
  4. Carbonic anhydrase XIV
  5. EC 4.2.1.1
Target 5 Gene Name Ca14
Target 5 Protein Sequence >Carbonic anhydrase 14 precursor 
MLFFALLLKVTWILAADGGHHWTYEGPHGQDHWPTSYPECGGDAQSPINIQTDSVIFDPD
LPAVQPHGYDQLGTEPLDLHNNGHTVQLSLPPTLHLGGLPRKYTAAQLHLHWGQRGSLEG
SEHQINSEATAAELHVVHYDSQSYSSLSEAAQKPQGLAVLGILIEVGETENPAYDHILSR
LHEIRYKDQKTSVPPFSVRELFPQQLEQFFRYNGSLTTPPCYQSVLWTVFNRRAQISMGQ
LEKLQETLSSTEEDPSEPLVQNYRVPQPLNQRTIFASFIQAGPLYTTGEMLGLGVGILAG
CLCLLLAVYFIAQKIRKKRLGNRKSVVFTSARATTEA
Target 5 Number of Residues 342
Target 5 Molecular Weight 37506
Target 5 Theoretical pI 6.34
Target 5 GO Classification
Function
binding
ion binding
cation binding
transition metal ion binding
zinc ion binding
catalytic activity
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
carbonate dehydratase activity
Process
physiological process
metabolism
cellular metabolism
one-carbon compound metabolism
Component
Not Available
Target 5 General Function Inorganic ion transport and metabolism
Target 5 Specific Function Reversible hydration of carbon dioxide
Target 5 Pathways
Name SMPDB Link KEGG Link
Nitrogen metabolism map00910 Link Image
Target 5 Reactions
  • H2CO3 = CO2 + H2O
Target 5 Pfam Domain Function
Target 5 Signals
  • 1-15
Target 5 Transmembrane Regions
  • 291-311
Target 5 Essentiality Essential
Target 5 GenBank ID Protein 5030908 Link Image
Target 5 UniProtKB/Swiss-Prot ID Q9WVT6 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name CAH14_MOUSE Link Image
Target 5 PDB ID 1RJ6 Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Membrane
  • single-pass type I membrane protein (Potential)
Target 5 Gene Sequence >1014 bp 
ATGTTGTTCTTCGCTCTCCTGTTAAAGGTGACTTGGATCCTGGCTGCAGATGGGGGTCAC
CACTGGACATATGAAGGCCCACACGGTCAGGACCATTGGCCAACCTCTTATCCTGAGTGT
GGAGGCGATGCCCAGTCCCCCATCAATATCCAGACAGACAGTGTGATATTTGACCCCGAT
CTGCCTGCTGTACAGCCCCATGGATATGACCAGCTTGGGACTGAGCCTTTGGATCTACAC
AATAATGGCCATACAGTGCAGCTTTCCCTGCCCCCAACCCTGCACCTGGGTGGACTGCCC
CGAAAATACACAGCAGCCCAGCTCCACCTGCACTGGGGTCAGAGAGGATCCCTCGAGGGA
TCAGAGCACCAGATCAACAGTGAAGCCACGGCTGCGGAGCTCCACGTGGTTCACTATGAC
TCCCAGTCCTACAGCAGCTTGAGTGAGGCAGCTCAGAAGCCACAGGGCCTGGCTGTCCTA
GGCATCCTCATTGAGGTGGGCGAGACTGAGAATCCAGCTTATGATCACATTCTGAGTCGT
CTACATGAAATAAGATACAAAGATCAGAAGACCTCTGTGCCTCCCTTCAGCGTGAGAGAG
CTGTTCCCCCAACAGCTGGAGCAATTCTTCCGCTACAACGGCTCACTCACAACTCCCCCC
TGCTACCAGAGTGTGCTCTGGACAGTCTTCAACAGAAGGGCCCAGATTTCAATGGGACAG
TTAGAGAAGCTCCAGGAGACATTGTCCTCTACAGAAGAGGACCCCTCTGAGCCCCTTGTA
CAGAACTACAGAGTCCCCCAGCCTCTCAACCAGAGGACCATCTTTGCTTCTTTCATCCAA
GCAGGACCACTGTATACCACAGGAGAGATGCTGGGTCTAGGTGTGGGAATCTTGGCTGGA
TGTCTTTGCCTTCTGCTGGCTGTTTATTTCATCGCTCAAAAAATTAGGAAGAAGCGGCTG
GGAAACAGGAAAAGTGTGGTTTTCACCTCTGCTCGGGCTACCACAGAGGCGTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID Not Available
Target 5 GenAtlas ID Not Available
Target 5 HGNC ID Not Available
Target 5 Chromosome Location Not Available
Target 5 Locus Not Available
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Mori K, Ogawa Y, Ebihara K, Tamura N, Tashiro K, Kuwahara T, Mukoyama M, Sugawara A, Ozaki S, Tanaka I, Nakao K: Isolation and characterization of CA XIV, a novel membrane-bound carbonic anhydrase from mouse kidney. J Biol Chem. 1999 May 28;274(22):15701-5. [PubMed Link Image]
Target 5 Drug References Not Available

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.