Carbonic anhydrase 5A, mitochondrial

Details

Name
Carbonic anhydrase 5A, mitochondrial
Synonyms
  • 4.2.1.1
  • CA-VA
  • CA5
  • Carbonate dehydratase VA
  • Carbonic anhydrase VA
Gene Name
CA5A
Organism
Humans
Amino acid sequence
>lcl|BSEQ0017164|Carbonic anhydrase 5A, mitochondrial
MLGRNTWKTSAFSFLVEQMWAPLWSRSMRPGRWCSQRSCAWQTSNNTLHPLWTVPVSVPG
GTRQSPINIQWRDSVYDPQLKPLRVSYEAASCLYIWNTGYLFQVEFDDATEASGISGGPL
ENHYRLKQFHFHWGAVNEGGSEHTVDGHAYPAELHLVHWNSVKYQNYKEAVVGENGLAVI
GVFLKLGAHHQTLQRLVDILPEIKHKDARAAMRPFDPSTLLPTCWDYWTYAGSLTTPPLT
ESVTWIIQKEPVEVAPSQLSAFRTLLFSALGEEEKMMVNNYRPLQPLMNRKVWASFQATN
EGTRS
Number of residues
305
Molecular Weight
34750.21
Theoretical pI
7.68
GO Classification
Functions
carbonate dehydratase activity / zinc ion binding
Processes
bicarbonate transport / one-carbon metabolic process / small molecule metabolic process
Components
mitochondrial matrix / mitochondrion
General Function
Zinc ion binding
Specific Function
Reversible hydration of carbon dioxide. Low activity.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion
Gene sequence
>lcl|BSEQ0017165|Carbonic anhydrase 5A, mitochondrial (CA5A)
ATGTTGGGGAGGAACACTTGGAAGACCTCAGCTTTCTCCTTCTTGGTTGAGCAGATGTGG
GCCCCTCTCTGGAGTCGTTCGATGAGGCCAGGGCGATGGTGTTCTCAGCGTTCCTGTGCA
TGGCAAACCAGCAATAACACTTTGCACCCACTCTGGACGGTCCCGGTCTCCGTGCCAGGG
GGCACCCGGCAGTCTCCTATTAACATCCAGTGGAGGGACAGCGTCTATGACCCCCAGCTG
AAGCCACTCAGGGTCTCCTATGAAGCGGCATCCTGCCTGTACATCTGGAACACTGGCTAC
CTCTTCCAGGTGGAATTTGACGATGCCACCGAGGCATCAGGAATTAGTGGTGGGCCCTTG
GAAAACCACTACAGACTGAAGCAATTTCACTTCCACTGGGGAGCAGTGAACGAGGGGGGC
TCAGAGCACACAGTGGACGGCCACGCGTACCCCGCAGAGCTGCATTTAGTTCACTGGAAT
TCTGTGAAATACCAAAATTACAAGGAAGCTGTCGTGGGAGAGAATGGTTTGGCTGTGATA
GGCGTGTTTTTAAAGCTCGGGGCCCATCATCAGACGCTGCAGAGGCTGGTGGACATCTTG
CCGGAAATAAAACATAAGGACGCGCGGGCGGCCATGCGCCCCTTCGACCCCTCCACTCTG
CTGCCCACCTGCTGGGATTACTGGACCTACGCGGGCTCGCTCACCACCCCGCCGCTGACC
GAGTCGGTCACCTGGATCATCCAGAAGGAGCCCGTTGAAGTGGCCCCAAGCCAGCTCTCT
GCATTTCGTACTCTCCTGTTTTCTGCACTTGGTGAAGAGGAGAAGATGATGGTGAACAAC
TATCGCCCACTTCAACCCTTGATGAACCGGAAGGTCTGGGCGTCCTTCCAGGCCACTAAT
GAGGGCACAAGGTCCTAG
Chromosome Location
16
Locus
16q24.3
External Identifiers
ResourceLink
UniProtKB IDP35218
UniProtKB Entry NameCAH5A_HUMAN
GenBank Protein ID306483
GenBank Gene IDL19297
HGNC IDHGNC:1377
General References
  1. Nagao Y, Platero JS, Waheed A, Sly WS: Human mitochondrial carbonic anhydrase: cDNA cloning, expression, subcellular localization, and mapping to chromosome 16. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7623-7. [PubMed:8356065]
  2. Nagao Y, Batanian JR, Clemente MF, Sly WS: Genomic organization of the human gene (CA5) and pseudogene for mitochondrial carbonic anhydrase V and their localization to chromosomes 16q and 16p. Genomics. 1995 Aug 10;28(3):477-84. [PubMed:7490083]
  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. [PubMed: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. [PubMed: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. [PubMed:16686544]
  6. 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. [PubMed:17127057]
  7. 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]
  8. 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]
  9. 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]
  10. Di Fiore A, Monti SM, Hilvo M, Parkkila S, Romano V, Scaloni A, Pedone C, Scozzafava A, Supuran CT, De Simone G: Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide. Proteins. 2009 Jan;74(1):164-75. doi: 10.1002/prot.22144. [PubMed:18618712]
  11. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  12. van Karnebeek CD, Sly WS, Ross CJ, Salvarinova R, Yaplito-Lee J, Santra S, Shyr C, Horvath GA, Eydoux P, Lehman AM, Bernard V, Newlove T, Ukpeh H, Chakrapani A, Preece MA, Ball S, Pitt J, Vallance HD, Coulter-Mackie M, Nguyen H, Zhang LH, Bhavsar AP, Sinclair G, Waheed A, Wasserman WW, Stockler-Ipsiroglu S: Mitochondrial carbonic anhydrase VA deficiency resulting from CA5A alterations presents with hyperammonemia in early childhood. Am J Hum Genet. 2014 Mar 6;94(3):453-61. doi: 10.1016/j.ajhg.2014.01.006. Epub 2014 Feb 13. [PubMed:24530203]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB033854-MethylimidazoleexperimentalunknownDetails
DB00909Zonisamideapproved, investigationalunknowninhibitorDetails
DB01194BrinzolamideapprovedunknowninhibitorDetails
DB08846Ellagic AcidinvestigationalunknowninhibitorDetails