Cloning and Characterization of Band 3, the Human Erythrocyte Anion-Exchange Protein (AE1)

The human erythrocyte anion-exchange protein (band 3 or AE1) was cloned from a fetal liver cDNA library. Three overlapping clones, encompassing 3637 nucleotides, were analyzed in detail. These encode a 911-amino acid protein (Mr 101,791) and detect a single 4.7-kilobase species in human reticulocyte...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1989-12, Vol.86 (23), p.9089-9093
Main Authors: Lux, Samuel E., John, Kathryn M., Kopito, Ron R., Lodish, Harvey F.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Anion Exchange Protein 1, Erythrocyte - genetics
Anions
Base Sequence
Biochemistry
Biological and medical sciences
Chemical bases
Chickens
chromosome 17
Cloning, Molecular - methods
Complementary DNA
Erythrocyte Membrane - metabolism
Erythrocytes
Fundamental and applied biological sciences. Psychology
Gene Library
Genes
Genes. Genome
Humans
Introns
Liver
Mice
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Protein Conformation
Proteins
Restriction Mapping
RNA, Messenger - genetics
Sequence Homology, Nucleic Acid
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Summary:The human erythrocyte anion-exchange protein (band 3 or AE1) was cloned from a fetal liver cDNA library. Three overlapping clones, encompassing 3637 nucleotides, were analyzed in detail. These encode a 911-amino acid protein (Mr 101,791) and detect a single 4.7-kilobase species in human reticulocyte RNA. The corresponding gene is located on chromosome 17. The protein is similar in structure to other anion exchangers and is divided into three regions: a hydrophilic, cytoplasmic domain that interacts with a variety of membrane and cytoplasmic proteins (residues 1-403); a hydrophobic, transmembrane domain that forms the anion antiporter (residues 404-882); and an acidic, C-terminal domain of unknown function (residues 883-911). The N-terminal domain contains several conserved sections (e.g., residues 57-86, 102-164, 219-347, and 375-403), some of which may contribute to binding sites for ankyrin, protein 4.1, or protein 4.2. The membrane domain is highly conserved with the exception of a single segment (residues 543-567) that contains several sites for cleavage of the protein by extracellular proteases. Based on hydropathy analyses and the wealth of available topographical and functional data, a model is proposed in which the protein crosses the membrane 14 times.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.86.23.9089