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.
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Division of Hematology/Oncology, Children's Hospital, Boston, Massachusetts.
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Bennett
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D000595:Amino Acid Sequence; D000818:Animals; D017487:Ankyrins; D001483:Base Sequence; D001798:Blood Proteins / Q000235:genetics*; D002453:Cell Cycle / Q000235:genetics; D002454:Cell Differentiation / Q000235:genetics; D003001:Cloning, Molecular; D004247:DNA; D004912:Erythrocytes; D005656:Fungal Proteins; D006801:Humans; D007448:Invertebrates; D008565:Membrane Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011519:Proto-Oncogenes; D012091:Repetitive Sequences, Nucleic Acid; D012689:Sequence Homology, Nucleic Acid; D014764:Viral Proteins; D015003:Yeasts
D017487:Ankyrins; D001798:Blood Proteins; D005656:Fungal Proteins; D008565:Membrane Proteins; D014764:Viral Proteins; D004247:DNA