The strong hydrophobic domain of the activated estrogen receptor of porcine uterus

Abstract
Basic estrogen receptor (ER) molecule (vero‐ER) of porcine uterus, which was previously shown to be the activated ER necessary to translocate from the cytoplasm into the nucleus, possesses a strongly hydrophobic nature. The strong hydrophobicity of vero‐ER was concealed through binding with ER‐binding factors (ERBFs). Vero‐ER lost its strong hydrophobicity and its capability to bind with ERBFs after limited proteolysis by endogenous protease. The strong hydrophobic domain of vero‐ER, indispensable for the nuclear translocation, was assumed to be located near the binding site with ERBFs.