Abstract
A Xenopus oocyte heterologous expression system was used to characterise iron transport properties of two members of the solute carrier 11 (slc11) protein family isolated from rainbow trout gills. One cDNA clone differed from the trout Slc11α containing an additional 52 bp in the exon between transmembrane domains (TM) 10 and 11. The 52 bp contained a stop codon, resulting in a novel isoform lacking the last two TM (termed slc11γ). Slc11γ and another isoform slc11β, import Fe 2+ at external pHs ⩽ to 7.4. Trout slc11β Fe 2+ import was more sensitive to inhibition by divalent metals. The novel vertebrate slc11γ isoform functions without TM11 and 12.
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