Sequence of a novel carbonic anhydrase-related polypeptide and its exclusive presence in Purkinje cells.
I isolated a mouse cDNA clone encoding a novel polypeptide which has strong homology with carbonic anhydrase. Unlike the other carbonic anhydrases, it has an additional N-terminal domain with a glutamic acid stretch and an arginine substitutes one of the three histidine residues which bind zinc ion. In the central nervous system, carbonic anhydrase is known to be expressed only in glia cells, but this gene is expressed in neuron, but only in Purkinje cells.
Kato
K
K
MRC Molecular Genetics Unit, Cambridge, UK.
D000818:Animals; D001483:Base Sequence; D001921:Brain / Q000201:enzymology; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000235:genetics; D051379:Mice; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics; D011689:Purkinje Cells / Q000201:enzymology*; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D012756:Sheep
D009419:Nerve Tissue Proteins; D002256:Carbonic Anhydrases