The ATP binding cassette (ABC) superfamily of membrane transporters is one of the largest protein classes known, and counts for numerous proteins involved in trafficking of biological molecules across membranes, host-defense mechanism to xenobiotics. The first known members were P-glycoprotein (P-gp) and multidrug resistant protein (MRP), cause multidrug resistance when transfected into drug-sensitive cells. In addition, increasing numbers of ABC proteins have recently been identified. The human ABCG1 (ABC, subfamily G, member 1) gene encodes a member of ABC superfamily that mediates the ATP-dependent translocation of variety of amphiphilic and lipophilic molecules. ABCG2 has been identified as a candidate protein responsible for cancer multidrug resistance, the overexpression of ABCG2 was found in several drug-selective cell lines. Search made of EST databases with BLAST program led to identification of several mouse and rat sequences that had high homology to ABCG2 but that appeared to encode a unique gene. ABCG3 is the most closely related to ABCG2 with 54% amino acid identity overall. The gene, ABCG4, produces several transcripts that differ at the 5’ end and encode proteins of various lengths, the ABCG4 protein is closely related to the Drosophila’s white and human ABCG1 genes, and belongs to the ABCG subfamily which are involved in cholesterol transport. ABCG5 and ABCG8 are members of the G subfamily of ABC transporters, which are predicted to contain a single magnesium-dependent ATP catalytic domain N-terminal to six transmembrane segments, mutations in either of them cause an identical phenotype which is consistent with these two gene products functioning as heterodimer. ABCG6 and ABCG7 exist in Dictyostelium species of eukaryotes.
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