The sulfate permease (SulP) family (TC# 2.A.53) is a member of the large APC superfamily of secondary carriers.
Many organisms including Bacillus subtilis, Synechocystis sp, Saccharomyces cerevisiae, Arabidopsis thaliana and Caenorhabditis elegans possess multiple SulP family paralogues.
For example, the mouse homologue, SLC26A6 (TC# 2.A.53.2.7), can transport sulfate, formate, oxalate, chloride and bicarbonate, exchanging any one of these anions for another.
[4] In these porters, mutating a glutamate, also involved in transport in the CIC family (TC# 2.A.49), (E357A in SLC26A6) created a channel out of the carrier.
[5] A low-resolution structure of a bacterial SulP transporter revealed a dimeric stoichiometry, stabilized via its transmembrane core and mobile intracellular domains.
The structure suggests that large movements of the STAS domain underlie the conformational changes that occur during transport.
[9] Apical membrane chloride/base exchange activity was sharply reduced, and the luminal content was more acidic in SLC26A3-null mouse colon.
MOT1 from Arabidopsis thaliana (TC# 2.A.53.11.1, 456aas; 8-10 TMSs), a distant homologue of the SulP and BenE (2.A.46) families, is expressed in both roots and shoots, and is localized to plasma membranes and intracellular vesicles.
Thus, SLC26A9 and CFTR behave differentially in polarized and non-polarized cells, explaining earlier conflicting data.
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