Description
Product Characteristics:
Band 3, also designated AE1, is an erythrocyte membrane glycoprotein that contributes to cell stuctural integrity and mediates exchange of chloride and bicarbonate across the phospholipid bilayer. The diverse functions of the approximately 900 amino acid protein are mediated by two distinct domains. The amino terminal domain, also known as cdb3 for cytoplasmic domain of erthrocyte membrane band 3, acts as an attachment site for the erythrocyte skeleton by binding ankyrin. The carboxy-terminal, membrane-associated domain carries out exchange transport of anions. Degradation of band 3 can generate an aging antigen known as senescent cell antigen, or SCA, which is expressed on old cells and marks them for removal by the immune system. An isoform of band 3, which lacks the first 65 amino acids and does not bind ankryin, is expressed in kidney.
Subcellular location: Cell membrane
Synonyms: SLC4A1, Band 3 phospho Y21, p-Band 3 phospho Y21, Solute carrier family 4 anion exchanger member 1, Solute carrier family 4 member 1, AE 1, AE1, Anion exchange protein 1, Anion exchanger 1, B3AT_HUMAN, Band 3, Band 3 anion transport protein, BND3, CD233, DI, Diego blood group, EMPB3, EPB3, Erythrocyte membrane protein band 3, Erythroid anion exchange protein, FR antibod, Froese blood group, RTA1A, Solute carrier family 4 member 1, SW antibody, Swann blood group, Waldner blood group, WD antibody, WD1, WR antibody, Wright blood group.
Target Information: The protein encoded by this gene is part of the anion exchanger (AE) family and is expressed in the erythrocyte plasma membrane, where it functions as a chloride/bicarbonate exchanger involved in carbon dioxide transport from tissues to lungs. The protein comprises two domains that are structurally and functionally distinct. The N-terminal 40kDa domain is located in the cytoplasm and acts as an attachment site for the red cell skeleton by binding ankyrin. The glycosylated C-terminal membrane-associated domain contains 12-14 membrane spanning segments and carries out the stilbene disulphonate-sensitive exchange transport of anions. The cytoplasmic tail at the extreme C-terminus of the membrane domain binds carbonic anhydrase II. The encoded protein associates with the red cell membrane protein glycophorin A and this association promotes the correct folding and translocation of the exchanger. This protein is predominantly dimeric but forms tetramers in the presence of ankyrin. Many mutations in this gene are known in man, and these mutations can lead to two types of disease: destabilization of red cell membrane leading to hereditary spherocytosis, and defective kidney acid secretion leading to distal renal tubular acidosis. Other mutations that do not give rise to disease result in novel blood group antigens, which form the Diego blood group system. Southeast Asian ovalocytosis (SAO, Melanesian ovalocytosis) results from the heterozygous presence of a deletion in the encoded protein and is common in areas where Plasmodium falciparum malaria is endemic. One null mutation in this gene is known, resulting in very severe anemia and nephrocalcinosis. [provided by RefSeq, Jul 2008]