The two-pore domain K+ (K2P) channels possess four transmembrane domains and two pore domains; they assemble as dimers. K2P channels have been implicated in a number of processes such as maintaining resting potential (leak K+ conductance), responding to volatile anesthetics, chemo- and mechanosensation. (Adapted from FBrf0188365 and PMID:11121510).
Notes on Group
FBrf0192007 states that although CG42340 has significant sequence similarity to K2P subunits it only has a single canonical pore signature, so may lack K[+] channel activity.