Carbonic anhydrase 6

NameCarbonic anhydrase 6
Synonyms
  • 4.2.1.1
  • CA-VI
  • Carbonate dehydratase VI
  • Carbonic anhydrase VI
  • Salivary carbonic anhydrase
  • Secreted carbonic anhydrase
Gene NameCA6
OrganismHuman
Amino acid sequence
>lcl|BSEQ0009331|Carbonic anhydrase 6
MRALVLLLSLFLLGGQAQHVSDWTYSEGALDEAHWPQHYPACGGQRQSPINLQRTKVRYN
PSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSE
ISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYPENTYYSNF
ISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLS
RTQVWKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFPNQEYTLGSEFQFYLHKIEEIL
DYLRRALN
Number of residues308
Molecular Weight35366.615
Theoretical pINot Available
GO Classification
Functions
  • zinc ion binding
  • carbonate dehydratase activity
Processes
  • small molecule metabolic process
  • bicarbonate transport
  • one-carbon metabolic process
  • detection of chemical stimulus involved in sensory perception of bitter taste
Components
  • extracellular region
  • extracellular space
  • cytosol
  • extracellular exosome
General FunctionZinc ion binding
Specific FunctionReversible hydration of carbon dioxide. Its role in saliva is unknown.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP23280
UniProtKB Entry NameCAH6_HUMAN
Cellular LocationSecreted
Gene sequence
>lcl|BSEQ0019449|Carbonic anhydrase 6 (CA6)
ATGAGGGCCCTGGTGCTTCTGCTGTCCCTGTTCCTGCTGGGTGGCCAGGCCCAGCATGTG
TCTGACTGGACCTACTCAGAAGGGGCACTGGACGAAGCGCACTGGCCACAGCACTACCCC
GCCTGTGGGGGCCAGAGACAGTCGCCTATCAACCTACAGAGGACGAAGGTGCGGTACAAC
CCCTCCTTGAAGGGGCTCAATATGACAGGCTATGAGACCCAGGCAGGGGAGTTCCCCATG
GTCAACAATGGCCACACAGTGCAGATCAGCCTGCCCTCCACCATGCGCATGACAGTGGCT
GACGGCACTGTATACATAGCCCAGCAGATGCACTTTCACTGGGGAGGTGCGTCCTCGGAG
ATCAGCGGCTCTGAGCACACCGTGGACGGGATCAGACATGTGATCGAGATTCACATTGTT
CACTACAATTCTAAATACAAGAGCTATGATATAGCCCAAGATGCGCCGGATGGTTTGGCT
GTACTGGCAGCCTTCGTTGAGGTGAAGAATTACCCTGAAAACACTTATTACAGCAACTTC
ATTTCTCATCTGGCCAACATCAAGTACCCAGGACAAAGAACAACCCTGACTGGCCTTGAC
GTTCAGGACATGCTGCCCAGGAACCTCCAGCACTACTACACCTACCATGGCTCACTCACC
ACGCCTCCCTGCACTGAGAACGTCCACTGGTTTGTGCTGGCAGATTTTGTCAAGCTCTCC
AGGACACAGGTTTGGAAGCTGGAGAATTCCTTACTGGATCACCGCAACAAGACCATCCAC
AACGATTACCGCAGGACCCAGCCCCTGAACCACAGAGTGGTGGAATCCAACTTCCCGAAT
CAGGAATACACTCTAGGCTCTGAATTCCAGTTTTACCTACATAAGATTGAGGAAATTCTT
GACTACTTAAGAAGAGCATTGAACTGA
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:1380
Chromosome Location1
LocusNot Available
References
  1. Aldred P, Fu P, Barrett G, Penschow JD, Wright RD, Coghlan JP, Fernley RT: Human secreted carbonic anhydrase: cDNA cloning, nucleotide sequence, and hybridization histochemistry. Biochemistry. 1991 Jan 15;30(2):569-75. 1899030
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  3. 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
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  5. 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
  6. 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
  7. Kannan KK, Liljas A, Waara I, Bergsten PC, Lovgren S, Strandberg B, Bengtsson U, Carlbom U, Fridborg K, Jarup L, Petef M: Crystal structure of human erythrocyte carbonic anhydrase C. VI. The three-dimensional structure at high resolution in relation to other mammalian carbonic anhydrases. Cold Spring Harb Symp Quant Biol. 1972;36:221-31. 4628675