Main pageKEGG pathway → ABC transporters

KEGG pathway: ABC transporters

Pathway hsa02010
Name ABC transporters
Members ABCC3 ABCA1 TAP1 ABCB7 ABCB4 ABCC4 ABCD3 ABCD4 ABCD1 ABCC1 ABCA13 ABCB10 ABCG1 ABCC10 ABCB6 ABCA12 ABCC2 ABCB8 ABCA8 ABCC6 ABCB5 ABCB11 ABCA7 ABCA4 ABCC11 CFTR ABCG8 ABCC12 ABCG2 ABCG5 ABCB1 ABCC9 ABCB9 ABCC5 ABCA3 ABCD2 ABCA6 ABCA5 ABCA10 ABCA9 ABCA2 ABCC8 ABCG4 TAP2
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).