Anion exchange protein 1 (AE1) (AE1)

Anion exchange protein 1 (AE1), commonly known as Band 3, is a multi-pass membrane protein that serves as the primary anion transporter in erythrocytes and the alpha-intercalated cells of the renal collecting duct [UniProt: P02730]. In red blood cells, it mediates the electroneutral exchange of chloride for bicarbonate, which is vital for the chloride shift that facilitates CO2 transport from tissues to the lungs [PubMed: 21518806]. Structurally, Band 3 acts as a central hub for the erythrocyte metabolon, anchoring the cytoskeleton to the plasma membrane via interactions with ankyrin, protein 4.2, and various glycolytic enzymes [PubMed: 15731161]. Mutations in the SLC4A1 gene, which encodes Band 3, are associated with clinical conditions such as hereditary spherocytosis, Southeast Asian ovalocytosis, and distal renal tubular acidosis [StatPearls: NBK541079]. While it is not a traditional target for many approved drugs, its function can be inhibited by stilbene derivatives like DIDS, and it plays a significant role in the pathogenesis of malaria, as it is used by Plasmodium falciparum for erythrocyte invasion and remodeling [PubMed: 29358495].

Other names

Band 3 anion transporterSolute carrier family 4 member 1SLC4A1Erythrocyte membrane protein band 3CD233Anion exchanger 1

Inhibition of the anion exchange pore by binding to the transport site or inducing conformational changes that block the passage of chloride and bicarbonate ions [PubMed: 10940054].