Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3.

Erythroid anion transporter assembly is mediated by a developmentally regulated recruitment onto a preassembled membrane cytoskeleton.

“…In addition to its interaction with the membrane cytoskeleton, band 3 also possesses high-affinity binding sites for hemoglobin (9) and the glycolytic enzymes aldolase (38) and glyceraldehyde-3phosphate dehydrogenase (47), although the latter site is absent in the chicken band 3 molecule (23). The complete amino acid sequence of the murine erythrocyte band 3 polypeptide has been deduced recently by cDNA sequencing (27) and shown to be highly homologous with the regions of the human erythrocyte band 3 protein which had been sequenced previously (6,24,31). Furthermore, eDNA clones for human nonerythroid band 3 polypeptides, which have been described in many tissues (12,14,25), have been sequenced and shown to possess extensive homology with the murine erythroid molecule in the transmembrane domain but little, if any, homology in the cytoplasmic domain (13).…”

Alternative Primary Structures in the Transmembrane Domain of the Chicken Erythroid Anion Transporter

“…Characterization of the murine band 3 gene (29) has indicated that each of these hydrophobic membrane-spanning segments roughly corresponds to an exon of the band 3 gene. The predicted sequence of the cytoplasmic domain of the murine erythroid band 3 polypeptide is also very similar to those regions of the cytoplasmic domain of the human erythroid band 3 polypeptide that have been sequenced (26), although the sequence has diverged at the extreme N terminus where the binding sites for the glycolytic enzymes are located in the human molecule (38,47). Both the murine and human erythroid band 3 polypeptides have relatively little similarity to the predicted sequence of the cytoplasmic domain of the human nonerythroid band 3 polypeptide.…”

“…The N terminus of the chicken erythroid band 3 polypeptide is -90 amino acids shorter than that of the murine (30) and the human (26) erythroid band 3 polypeptides. This truncated chicken band 3 polypeptide is consistent with the absence of binding to glyceraldehyde-3-phosphate dehydrogenase ( 22), which associates with the extreme N terminus of the human erythroid band 3 polypeptide (47).…”

“…Furthermore, many of the amino acids implicated in anion transport through drug binding studies are conserved in the chicken erythroid band 3 polypeptide. Sequence analysis in conjunction with in vitro transcription and in vitro translation studies indicates that the -90 N-terminal amino acids of human (26) and murine (30) erythroid band 3 are absent in chicken erythroid band 3. The lack of this cytoplasmic region is consistent with the absence of binding of chicken erythroid band 3 to glyceraldehyde-3-phosphate dehydrogenase (22).…”

The capacity of basic peptides to trigger exocytosis from mast cells correlates with their capacity to immobilize band 3 proteins in erythrocyte membranes

“…The major anionic moieties present in the ghost membrane are the intracellular portions of band 3 (Kaul et al, 1983) and the extracellular portions of glycophorin. It has been postulated that mutual electrostatic repulsion between the anionic glycophorin molecules is a major reason for its even distribution across the surface of the membrane (Elgsaeter et al, 1976;Gahmberg et al, 1978), and also that an interaction between glycophorin and band 3 exists ).…”