This family of 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, Ssu1 from 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, this family is 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]. 20981093. Homologue structure of the SLAC1 anion channel for closing stomata in leaves. Chen YH, Hu L, Punta M, Bruni R, Hillerich B, Kloss B, Rost B, Love J, Siegelbaum SA, Hendrickson WA;. Nature. 2010;467:1074-1080. [2]. 18305484. SLAC1 is required for plant guard cell S-type anion channel function in stomatal signalling. Vahisalu T, Kollist H, Wang YF, Nishimura N, Chan WY, Valerio G, Lamminmaki A, Brosche M, Moldau H, Desikan R, Schroeder JI, Kangasjarvi J;. Nature. 2008;452:487-491. (from Pfam)
GO Terms:- Date:
- 2024-10-16