THE SEQUENCE OF PORCINE 80 KDA 17-BETA-ESTRADIOL DEHYDROGENASE REVEALS SIMILARITIES TO THE SHORT-CHAIN ALCOHOL-DEHYDROGENASE FAMILY, TO ACTIN-BINDING MOTIFS AND TO STEROL CARRIER PROTEIN 2

The cDNA of porcine 17 beta-estradiol dehydrogenase codes for a polype ptide of 737 amino acids. The dehydrogenase activity of the 80 kDa tra nslation product is located in its N-terminal 32 kDa fragment, which i s the major form isolated from endometrial epithelium. beta-Actin co-p urifies with some of the 32 kDa enzyme, which contains actin-binding m otifs and is homologous to hydratase dehydrogenase-epimerase of Candid a tropicalis. The microbody-targeting signal AKI and sequences resembl ing sterol carrier protein 2 are present in the C-terminal part of the 80 kDa protein. The N- and C-terminal parts are connected by a sequen ce containing the putative protease recognition signal AAP.