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
- Functionscarbonate dehydratase activity / zinc ion bindingProcessesbicarbonate transport / one-carbon metabolic process / small molecule metabolic processComponentsmitochondrial matrix / mitochondrion
- General Function
- Zinc ion binding
- Specific Function
- Reversible hydration of carbon dioxide. Low activity.
- Pfam Domain Function
- Carb_anhydrase (PF00194)
- 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
Resource Link UniProtKB ID P35218 UniProtKB Entry Name CAH5A_HUMAN GenBank Protein ID 306483 GenBank Gene ID L19297 HGNC ID HGNC:1377 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB03385 4-Methylimidazole experimental unknown Details DB00909 Zonisamide approved, investigational unknown inhibitor Details DB01194 Brinzolamide approved unknown inhibitor Details DB08846 Ellagic acid investigational unknown inhibitor Details DB00562 Benzthiazide approved yes inhibitor Details DB00606 Cyclothiazide approved yes inhibitor Details