ANALYSIS OF CDNA FOR HUMAN ERYTHROCYTE ANKYRIN INDICATES A REPEATED STRUCTURE WITH HOMOLOGY TO TISSUE-DIFFERENTIATION AND CELL-CYCLE CONTROL PROTEINS

Analysis of complementary DNA for human erythroid ankyrin indicates that the mature protein contains 1,880 amino acids comprising an N-terminal domain binding integral membrane proteins and tubulin, a central domain binding spectrin and vimentin, and an acidic C-terminal 'regulatory' domain containing an alternatively spliced sequence missing from ankyrin variant 2.2. The N-terminal domain is almost entirely composed of 22 tandem 33-amino-acid repeats. Similar repeats are found in yeast and invertebrate proteins involved in cell-cycle control and tissue differentiation. © 1990 Nature Publishing Group.