Thiamine Triphosphatase (THTPA)

The deduced 230-amino acid protein has a predicted molecular mass of 25.55 kD and contains a high percentage of negatively-charged residues (17.4% glutamic acid and aspartic acid). THTPA shares 80% and 70% sequence identity with the bovine and macaque Thtpa enzymes, respectively. All 3 enzyme homologs contain several potential phosphorylation sites. Dot-blot hybridization of multiple human tissues detected widespread THTPA expression, but only at low levels. The highest hybridization signals were observed in uterus, testis, and prostate, followed by bladder, kidney, lung, and thyroid gland. Lower signals were detected in various brain regions with no detectable signal in cerebellum. Expression was particularly low in the digestive system, fetal tissues, and transformed cell lines.