InterPro domain: IPR038665

Each of these transporters has ten alpha helical transmembrane segments [ 1 ]. The structure of a bacterial homologue of SLAC1 shows it to have a trimeric arrangement. The pore is composed of five helices with a conserved Phe residue involved in gating. One homologue, Mae1 from the yeast Schizosaccharomyces pombe, functions as a malate uptake transporter; another, Ssu1from Saccharomyces cerevisiae and other fungi including Aspergillus fumigatus, is characterised as a sulfite efflux pump; and TehA from Escherichia coli is identified as a tellurite resistance protein by virtue of its association in the tehA/tehB operon. In plants, homologues are found in the stomatal guard cells functioning as an anion-transporting pore [ 2 ]. Many homologues are incorrectly annotated as tellurite resistance or dicarboxylate transporter (TDT) proteins.

1. Homologue structure of the SLAC1 anion channel for closing stomata in leaves. Nature 467, 1074-80
2. SLAC1 is required for plant guard cell S-type anion channel function in stomatal signalling. Nature 452, 487-91