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PMID: 2594752 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1).

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 23 ·1989-12-00 ·Pages 9089-93

Lux SE, John KM, Kopito RR, Lodish HF

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Anion Exchange Protein 1, Erythrocyte/genetics Base Sequence Chickens Cloning, Molecular/methods Erythrocyte Membrane/metabolism Gene Library Genes Humans Mice Molecular Sequence Data Protein Conformation RNA, Messenger/genetics Restriction Mapping Sequence Homology, Nucleic Acid
Chemicals
Anion Exchange Protein 1, Erythrocyte RNA, Messenger
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lux S E
Division of Hematology/Oncology, Children's Hospital, Boston, MA 02115.
John K M
Kopito R R
Lodish H F
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.86.23.9089
Published
1989-12-00
Pages
9089-93
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC298439
Subset
IM
Grants
NIDDK NIH HHS · DK34083 · United States
NHLBI NIH HHS · HL15157 · United States
NHLBI NIH HHS · HL32262 · United States
Databases
GENBANK
M27819
External Links
PubMed source DOI: 10.1073/pnas.86.23.9089 PMC Full Text View journal details
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