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NameCarbonic anhydrase 7
Synonyms
  • 4.2.1.1
  • CA-VII
  • Carbonate dehydratase VII
  • Carbonic anhydrase VII
Gene NameCA7
OrganismHuman
Amino acid sequence
>lcl|BSEQ0006977|Carbonic anhydrase 7
MTGHHGWGYGQDDGPSHWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELSYEACMSLS
ITNNGHSVQVDFNDSDDRTVVTGGPLEGPYRLKQFHFHWGKKHDVGSEHTVDGKSFPSEL
HLVHWNAKKYSTFGEAASAPDGLAVVGVFLETGDEHPSMNRLTDALYMVRFKGTKAQFSC
FNPKCLLPASRHYWTYPGSLTTPPLSESVTWIVLREPICISERQMGKFRSLLFTSEDDER
IHMVNNFRPPQPLKGRVVKASFRA
Number of residues264
Molecular Weight29658.235
Theoretical pI7.45
GO Classification
Functions
  • zinc ion binding
  • carbonate dehydratase activity
Processes
  • mitophagy in response to mitochondrial depolarization
  • positive regulation of synaptic transmission, GABAergic
  • regulation of chloride transport
  • small molecule metabolic process
  • positive regulation of cellular pH reduction
  • bicarbonate transport
  • one-carbon metabolic process
  • positive regulation of defense response to virus by host
  • xenophagy
Components
  • cytosol
General FunctionZinc ion binding
Specific FunctionReversible hydration of carbon dioxide.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID28192445
UniProtKB IDP43166
UniProtKB Entry NameCAH7_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0012523|Carbonic anhydrase 7 (CA7)
ATGTCCCTCAGCATCACCAACAATGGCCACTCTGTCCAGGTAGACTTCAATGACAGCGAT
GACCGAACCGTGGTGACTGGGGGCCCCCTGGAAGGGCCCTACCGCCTCAAGCAGTTTCAC
TTCCACTGGGGCAAGAAGCACGATGTGGGTTCTGAGCACACGGTGGACGGCAAGTCCTTC
CCCAGCGAGCTGCATCTGGTTCACTGGAATGCCAAGAAGTACAGCACTTTTGGGGAGGCG
GCCTCAGCACCTGATGGCCTGGCTGTGGTTGGTGTTTTTTTGGAGACAGGAGACGAGCAC
CCCAGCATGAATCGTCTGACAGATGCGCTCTACATGGTCCGGTTCAAGGGCACCAAAGCC
CAGTTCAGCTGCTTCAACCCCAAGTGCCTCCTGCCTGCCAGCCGGCACTACTGGACCTAC
CCGGGCTCTCTGACGACTCCCCCACTCAGTGAGAGTGTCACCTGGATTGTGCTCCGGGAG
CCCATCTGCATCTCTGAAAGGCAGATGGGGAAGTTCCGGAGCCTGCTTTTTACCTCGGAG
GACGATGAGAGGATCCACATGGTGAACAACTTCCGGCCACCACAGCCACTGAAGGGCCGC
GTGGTAAAGGCCTCCTTCCGGGCCTGA
GenBank Gene IDAY075019
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:1381
Chromosome Location16
Locus16q22.1
References
  1. Montgomery JC, Venta PJ, Eddy RL, Fukushima YS, Shows TB, Tashian RE: Characterization of the human gene for a newly discovered carbonic anhydrase, CA VII, and its localization to chromosome 16. Genomics. 1991 Dec;11(4):835-48. 1783392
  2. Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J, Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y, Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC, Adams MD: Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. Genomics. 1999 Sep 15;60(3):295-308. 10493829
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  4. Temperini C, Scozzafava A, Vullo D, Supuran CT: Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme. Chemistry. 2006 Sep 18;12(27):7057-66. 16807956
  5. Temperini C, Scozzafava A, Vullo D, Supuran CT: Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design. J Med Chem. 2006 May 18;49(10):3019-27. 16686544
  6. Kohler K, Hillebrecht A, Schulze Wischeler J, Innocenti A, Heine A, Supuran CT, Klebe G: Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste. Angew Chem Int Ed Engl. 2007;46(40):7697-9. 17705204
  7. Temperini C, Innocenti A, Scozzafava A, Mastrolorenzo A, Supuran CT: Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV. Bioorg Med Chem Lett. 2007 Feb 1;17(3):628-35. Epub 2006 Nov 15. 17127057
  8. Temperini C, Innocenti A, Guerri A, Scozzafava A, Rusconi S, Supuran CT: Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I. Bioorg Med Chem Lett. 2007 Apr 15;17(8):2210-5. Epub 2007 Feb 8. 17314045
  9. Crocetti L, Maresca A, Temperini C, Hall RA, Scozzafava A, Muhlschlegel FA, Supuran CT: A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases. Bioorg Med Chem Lett. 2009 Mar 1;19(5):1371-5. doi: 10.1016/j.bmcl.2009.01.038. Epub 2009 Jan 19. 19186056
  10. Maresca A, Temperini C, Vu H, Pham NB, Poulsen SA, Scozzafava A, Quinn RJ, Supuran CT: Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors. J Am Chem Soc. 2009 Mar 4;131(8):3057-62. doi: 10.1021/ja809683v. 19206230