SLC4A1
SLC4A1, also known as band 3, AE1, EPB3 and CD233, is an anion exchanger of the erythrocyte plasma membrane. It works as a chloride/bicarbonate exchanger in carbon dioxide transport and carries the Diego blood group antigens. Browse Assay Genie's current range of SLC4A1 research reagents below, or read on for the biology behind the target.
SLC4A1 is part of the anion exchanger (AE) family and is expressed in the erythrocyte plasma membrane. There it acts as a chloride/bicarbonate exchanger and contributes to the transport of carbon dioxide from tissues to the lungs. The protein has two structurally and functionally distinct domains. The N-terminal cytoplasmic domain attaches the red cell skeleton to the membrane by binding ankyrin. The glycosylated C-terminal membrane domain contains 12-14 membrane-spanning segments and carries out stilbene disulphonate-sensitive anion exchange. The cytoplasmic tail at the extreme C-terminus binds carbonic anhydrase II.
The SLC4A1 protein is predominantly dimeric, but it forms tetramers in the presence of ankyrin. It associates with the red cell membrane protein glycophorin A, and this association promotes correct folding and translocation of the exchanger. UniProt records the protein as the Band 3 anion transport protein, and its subcellular locations include the cell membrane and the basolateral cell membrane. The mouse and rat orthologs are both named Slc4a1. The HGNC gene groups for the SLC4A1 gene are blood group antigens, CD molecules and solute carrier family 4.
Many SLC4A1 mutations are known in humans. Some destabilise the red cell membrane and cause hereditary spherocytosis, while others impair kidney acid secretion and cause distal renal tubular acidosis. Mutations that do not cause disease give rise to novel blood group antigens, which form the Diego blood group system. Southeast Asian ovalocytosis results from the heterozygous presence of a deletion in the protein and is common where Plasmodium falciparum malaria is endemic. One null mutation is known, resulting in very severe anaemia and nephrocalcinosis. UniProt also reports that the protein acts as a receptor for P. falciparum (isolate 3D7) MSP1 and MSP9, facilitating merozoite invasion of erythrocytes.
SLC4A1 links the red cell skeleton to the membrane by binding ankyrin, making it central to studies of erythrocyte membrane organisation.
As a chloride/bicarbonate exchanger that binds carbonic anhydrase II, SLC4A1 is studied in carbon dioxide transport from tissues to lungs.
Mutations in SLC4A1 cause hereditary spherocytosis and are linked to Southeast Asian ovalocytosis, so it features in research on red cell membrane stability.
SLC4A1 carries Diego blood group antigens and acts as a receptor for P. falciparum MSP1 and MSP9 in merozoite invasion of erythrocytes.
SLC4A1 is a chloride/bicarbonate exchanger in the erythrocyte plasma membrane that contributes to carbon dioxide transport from tissues to lungs. Its cytoplasmic domain binds ankyrin to anchor the red cell skeleton, and its C-terminal tail binds carbonic anhydrase II.
SLC4A1 is also called band 3, Band 3 anion transport protein, anion exchanger 1 (AE1), erythrocyte membrane protein band 3 (EPB3, EMPB3) and CD233. Other aliases include RTA1A, DI, WD, FR, SW and WR, reflecting its roles as a blood group antigen carrier and in renal tubular acidosis.
Yes. SLC4A1 mutations cause hereditary spherocytosis and distal renal tubular acidosis, and a deletion underlies Southeast Asian ovalocytosis. Orthologs exist in mouse and rat, both named Slc4a1. Check the datasheet of any product for its validated reactivity.
Other solute carrier transporters with products at Assay Genie, useful for comparative membrane transport research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P02730; product specifications from Assay Genie datasheets.