Carbonic Anhydrase III, Muscle Specific (CA3)

CA-III; CAIII; Car3; Carbonate dehydratase III

SPN	T716
HGNC	1374
MGI	88270
PubMed	15509796
RGD	2241
UniProt	P07451
Wiki	CA3

CAIII is a member of a multigene family (at least six separate genes are known) that encode carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyze the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue specific and present at high levels in skeletal muscle and much lower levels in cardiac and smooth muscle. A proportion of carriers of Duchenne muscle dystrophy have a higher CA3 level than normal. The gene spans 10.3 kb and contains seven exons and six introns.This RefSeq record was created from transcript and genomic sequence data because no single transcript was available for the full length of the gene. The extent of this transcript is supported by transcript alignments.

Reference

"Nucleotide sequence and derived amino acid sequence of a cDNA encoding human muscle carbonic anhydrase."
Gene 41:233-239(1986) [PubMed] [Europe PMC] [Abstract]

"Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes."
Proc. Natl. Acad. Sci. U.S.A. 83:9571-9575(1986) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues."
Genes Dev. 1:594-602(1987) [PubMed] [Europe PMC] [Abstract]

"Sequence comparisons and functional studies of the proximal promoter of the carbonic anhydrase 3 (CA3) gene."
Gene 214:157-165(1998) [PubMed] [Europe PMC] [Abstract]

"A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]

"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]

"Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer."
Biochemistry 44:10046-10053(2005) [PubMed] [Europe PMC] [Abstract]

"Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III."
Proteins 68:337-343(2007) [PubMed] [Europe PMC] [Abstract]