T. Kuriyama et al., CLONING OF THE MOUSE GENE FOR D-DOPACHROME TAUTOMERASE, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1388(2), 1998, pp. 506-512
D-Dopachrome tautomerase converts 2-carboxy-2,3-dihydroindole-5,6-quin
one (D-dopachrome) into 5,6-dihydroxyindole. The amino acid sequence o
f this protein is 27% identical with that of macrophage migration inhi
bitory factor, which is known as a cytokine, pituitary hormone, and gl
ucocorticoid-induced immunomodulator. In this study, we isolated and s
equenced a 3490 bp-long genomic DNA of mouse D-dopachrome tautomerase
that consists of three exons and two introns. By two procedures, 5' ra
pid amplification of cDNA ends and cap site labeling, we determined th
e transcription initiation site, which is located 46 bp upstream of th
e translation initiation site. The possible polyadenylation sequence (
AATAAA) is located 180 bp downstream of the termination codon. Compute
r-assisted analysis of the nucleotide sequence revealed a number of re
gulatory motifs, including multiple sites for Spl, C/EBP, NF-Y, and US
F. Although the precise pathophysiological functions of D-dopachrome t
automerase remain to be elucidated, the present results will contribut
e not only to elucidation of the mechanism of gene expression, but als
o to understanding of the molecular function of this protein. (C) 1998
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