At least 14 distinct isozymes of carbonic anhydrase have been identified in
mammals. These enzymes catalyze the hydration of carbon dioxide and are es
sential for regulation of cellular pH and carbon dioxide transport. Carboni
c anhydrase III is highly expressed in certain tissues, including muscle an
d fat where it constitutes up to 25% of the soluble protein. We cloned a cD
NA encoding mouse carbonic anhydrase III. This cDNA contains 1653 bp, consi
sting of 79 bp in the 5' UTR, a 780 bp open reading frame, and 794 bp of th
e 3' UTR, including two potential polyadenylation signals. Fluorescent in s
itu hybridization confirmed the existence of a single copy of the gene on c
hromosome 3. We then isolated the genomic DNA for mouse carbonic anhydrase
III and analyzed its structure. The gene consists of seven exons and six in
trons which spun 10.5 kb. The 5' flanking region of the genomic DNA is nota
ble for a pyrimidine rich region consisting of two dinucleotide repeats con
taining 23 and 20 TC pairs separated by the same 15 bp spacer. Published by
Elsevier Science B.V.