The nucleotide sequence of the estrogen receptor gene of Oreochromis aureus (OaER) indicates that the hormone-binding E domain is composed of 4 exons interspersed by short introns of only 0.18-1.3 kb each. All 4 E exons exhibit consensus sequences flanking the donor and acceptor splice sites. Analysis of introns revealed (i) numerous palindromic and half-palindromic steroid responsive elements including ERE, TRE and GRE, (ii) six alternative polyadenylation signals and (iii) putative control regions identified by the clustering of transcription factor binding sites. Of particular interest is the presence of a TATA and CAAT box in intron IV. The hydropathicity profile shows that the E exons are relatively hydrophobic. Two receptor dimerization regions have been observed: a conserved heptad repeat of hydrophobic residues (R168-M193) and a perfect leucine zipper (L36-L57). The presence of multiple sites for kinase activity in these regions suggests the importance of phosphorylation in the regulation of receptor functions and ligand-affinity.
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