Evidence that progesterone binding uteroglobin is similar to myosin alkali light chain.
Using a computer program designed to detect evolutionary relationships between proteins, I find that exon 2 of rabbit uteroglobin, a progesterone binder, and part of myosin alkali light chain have a comparison score that is 7.2 standard deviations higher than that obtained with a comparison of randomized sequences of these proteins. The probability (p) of getting this score by chance is less than 10(-12). This theoretical finding that these sequences are similar has led to the experimental finding that copper, calcium and the tranquilizer trifluoperazine, a calmodulin binding ligand, affect progesterone binding to uteroglobin.
D000595:Amino Acid Sequence; D000727:Androgen-Binding Protein / Q000032:analysis; D000818:Animals; D006023:Glycoproteins / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology; D008970:Molecular Weight; D009218:Myosins / Q000378:metabolism*; D011374:Progesterone / Q000378:metabolism*; D011817:Rabbits; D012984:Software; D014268:Trifluoperazine / Q000494:pharmacology; D014336:Troponin / Q000032:analysis; D019209:Troponin C; D014598:Uteroglobin / Q000378:metabolism*
D000727:Androgen-Binding Protein; D006023:Glycoproteins; D008670:Metals; D014336:Troponin; D019209:Troponin C; D014268:Trifluoperazine; D011374:Progesterone; D014598:Uteroglobin; D009218:Myosins