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Identification
HMDB Protein ID HMDBP10020
Secondary Accession Numbers
  • 15960
Name Carbonic anhydrase 6
Synonyms
  1. CA-VI
  2. Carbonate dehydratase VI
  3. Carbonic anhydrase VI
  4. Salivary carbonic anhydrase
  5. Secreted carbonic anhydrase
Gene Name CA6
Protein Type Enzyme
Biological Properties
General Function Involved in carbonate dehydratase activity
Specific Function Reversible hydration of carbon dioxide. Its role in saliva is unknown.
Pathways Not Available
Reactions
Hydrogen carbonate → CO(2) + Water details
Hydrogen carbonate → Carbon dioxide + Water details
GO Classification
Biological Process
small molecule metabolic process
bicarbonate transport
one-carbon metabolic process
Cellular Component
cytoplasm
extracellular region
extracellular space
Component
extracellular region
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
carbonate dehydratase activity
transition metal ion binding
zinc ion binding
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
Molecular Function
metal ion binding
zinc ion binding
carbonate dehydratase activity
Process
metabolic process
cellular metabolic process
one-carbon metabolic process
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location 1
Locus 1p36.2
SNPs CA6
Gene Sequence
>927 bp
ATGAGGGCCCTGGTGCTTCTGCTGTCCCTGTTCCTGCTGGGTGGCCAGGCCCAGCATGTG
TCTGACTGGACCTACTCAGAAGGGGCACTGGACGAAGCGCACTGGCCACAGCACTACCCC
GCCTGTGGGGGCCAGAGACAGTCGCCTATCAACCTACAGAGGACGAAGGTGCGGTACAAC
CCCTCCTTGAAGGGGCTCAATATGACAGGCTATGAGACCCAGGCAGGGGAGTTCCCCATG
GTCAACAATGGCCACACAGTGCAGATCGGCCTGCCCTCCACCATGCGCATGACAGTGGCT
GACGGCATTGTATACATAGCCCAGCAGATGCACTTTCACTGGGGAGGTGCGTCCTCGGAG
ATCAGCGGCTCTGAGCACACCGTGGACGGGATCAGACATGTGATCGAGATTCACATTGTT
CACTACAATTCTAAATACAAGACGTATGATATAGCCCAAGATGCGCCGGATGGTTTGGCT
GTACTGGCAGCCTTCGTTGAGGTGAAGAATTACCCTGAAAACACTTATTACAGCAACTTC
ATTTCTCATCTGGCCAACATCAAGTACCCAGGACAAAGAACAACCCTGACTGGCCTTGAC
GTTCAGGACATGCTGCCCAGGAACCTCCAGCACTACTACACCTACCATGGCTCACTCACC
ACGCCTCCCTGCACTGAGAACGTCCACTGGTTTGTGCTGGCAGATTTTGTCAAGCTCTCC
AGGACACAGGTTTGGAAGCTGGAGAATTCCTTACTGGATCACCGCAACAAGACCATCCAC
AACGATTACCGCAGGACCCAGCCCCTGAAACACAGAGTGGTGGAATCCAACTTCCCGAAT
CAGGAATACACTCTAGGCTCTGAATTCCAGTTTTACCTACATAAGATTGAGGAAATTCTT
GACTACTTAAGAAGAGCATTGAACTGA
Protein Properties
Number of Residues 308
Molecular Weight 35366.615
Theoretical pI 7.027
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Carbonic anhydrase 6
MRALVLLLSLFLLGGQAQHVSDWTYSEGALDEAHWPQHYPACGGQRQSPINLQRTKVRYN
PSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSE
ISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYPENTYYSNF
ISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLS
RTQVWKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFPNQEYTLGSEFQFYLHKIEEIL
DYLRRALN
GenBank ID Protein 179732
UniProtKB/Swiss-Prot ID P23280
UniProtKB/Swiss-Prot Entry Name CAH6_HUMAN
PDB IDs
GenBank Gene ID M57892
GeneCard ID CA6
GenAtlas ID CA6
HGNC ID HGNC:1380
References
General References
  1. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  2. 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. [PubMed:19186056 ]
  3. 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. [PubMed:19206230 ]
  4. 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. [PubMed:17314045 ]
  5. 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. [PubMed:17705204 ]
  6. 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. [PubMed:1899030 ]
  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. [PubMed:4628675 ]