The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence
- 15 December 1988
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 256 (3) , 703-712
- https://doi.org/10.1042/bj2560703
Abstract
1. We have isolated cDNA clones corresponding to the red cell membrane anion-transport protein (Band 3). 2. The cDNA clones cover 3475 bases of the mRNA and contain the entire protein-coding region, 150 bases of the 5′ untranslated region and part of the 3′ non-coding region, but do not extend to the 3′ end of the mRNA. 3. The translated protein sequence predicts that the human red cell anion transporter contains 911 amino acids. 4. The availability of the amino acid sequence allows the interpretation of some of the many studies on the chemical and proteolytic modification of the human protein aimed at examining the structure and mechanism of this membrane transport protein.This publication has 34 references indexed in Scilit:
- Carboxypeptidase Y digestion of band 3, the anion transport protein of human erythrocyte membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1987
- Structure and function of the cytoplasmic domain of band 3: center of erythrocyte membrane—peripheral protein interactionsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1986
- STRUCTURAL ASPECTS OF THE RED CELL ANION EXCHANGE PROTEINAnnual Review of Biochemistry, 1986
- Glycosylation site of band 3, the human erythrocyte anion-exchange proteinBiochemistry, 1986
- Kinetics and Mechanism of Anion Transport in Red Blood CellsAnnual Review of Physiology, 1985
- Primary structure and transmembrane orientation of the murine anion exchange proteinNature, 1985
- The locations of the three cysteine residues in the primary structure of the intrinsic segments of band 3 protein, and implications concerning the arrangement of band 3 protein in the bilayerBiochimica et Biophysica Acta (BBA) - Biomembranes, 1983
- Chloride-bicarbonate exchange in red blood cells: physiology of transport and chemical modification of binding sitesPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1982
- Modification by papain of the structure and function of band 3, the erythrocyte anion transport proteinBiochemistry, 1981
- Isolation of biologically active ribonucleic acid from sources enriched in ribonucleaseBiochemistry, 1979