description
The ATP-binding cassette (ABC) transporters form one of the largest known protein families, and are widespread in bacteria, archaea, and eukaryotes. They couple ATP hydrolysis to active transport of a wide variety of substrates such as ions, sugars, lipids, sterols, peptides, proteins, and drugs. The structure of a prokaryotic ABC transporter usually consists of three components; typically two integral membrane proteins each having six transmembrane segments, two peripheral proteins that bind and hydrolyze ATP, and a periplasmic (or lipoprotein) substrate-binding protein. Many of the genes for the three components form operons as in fact observed in many bacterial and archaeal genomes. On the other hand, in a typical eukaryotic ABC transporter, the membrane spanning protein and the ATP-binding protein are fused, forming a multi-domain protein with the membrane-spanning domain (MSD) and the nucleotide-binding domain (NBD)

external resources
NCBI:83035
KEGG:hsa02010
PUBMED:10557362
PUBMED:18424520
PUBMED:9799792
PUBMED:18375759
PUBMED:16135226
PUBMED:18326572
PUBMED:18805970
PUBMED:17214741
PUBMED:11929526
PUBMED:11731493
PUBMED:16109926
PUBMED:17873039

genes
ABCA1 , ABCA2 , ABCA3 , ABCB7 , ABCA4 , ABCD1 , ABCD2 , ABCC6 , CFTR , ABCC2 , ABCC1 , ABCB1 , ABCB4 , ABCD3 , ABCD4 , ABCC8 , TAP1 , TAP2 , ABCB11 , ABCC3 , ABCG2 , ABCG1 , ABCC5 , ABCB6 , ABCC9 , ABCC4 , ABCA7 , ABCA10 , ABCA9 , ABCA8 , ABCB8 , ABCB10 , ABCB9 , ABCA6 , ABCA5 , ABCA12 , ABCG4 , ABCG5 , ABCG8 , ABCC11 , ABCC10 , ABCC12 , ABCA13 , ABCB5 ,