Primary structure and transmembrane orientation of the murine anion exchange protein.
The amino-acid sequence of murine band 3, deduced from the nucleotide sequence of a complementary DNA clone, confirms that this integral membrane glycoprotein is composed of two major structural domains which correlate with its dual functions as the anchor for the erythrocyte cytoskeleton and as a plasma membrane anion antiporter. This latter activity resides within a highly hydrophobic domain that crosses the plasma membrane at least 12 times.
R R
RR
Kopito
H F
HF
Lodish
D000595:Amino Acid Sequence; D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D003593:Cytoplasm; D004247:DNA / Q000235:genetics; D004910:Erythrocyte Membrane / Q000648:ultrastructure*; D007473:Ion Channels; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012995:Solubility
D001457:Anion Exchange Protein 1, Erythrocyte; D007473:Ion Channels; C523515:Slc4a1 protein, mouse; D004247:DNA