Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains

Abstract

The full length cDNA of porcine moesin and radixin have been cloned and sequenced. Comparison of the closely related sequences of human, murine and porcine moesin, ezrin and radixin with a protein from Echinococcus multilocularis, an evolutionarily quite distant human parasite, reveals several highly invariant domains in the aminoterminal and carboxyterminal regions. Most of these conserved domains are clustered around tyrosine residues that are putative phosphorylation sites for tyrosine phosphokinases.