is a transmembrane receptor that mediates the sodium-independent uptake of numerous endogenous compounds including bilirubin, 17-beta-glucuronosyl estradiol and leukotriene C4. This protein is also involved in the removal of drug compounds such as statins, bromosulfophthalein and rifampin from the blood into the hepatocytes. Polymorphisms in the gene encoding this protein are associated with impaired transporter function. The SLC21A6 gene encodes a deduced 691-amino acid protein containing 12 transmembrane domains, 7 putative N-glycosylation sites in the extracellular loops, and 2 potential phosphorylation sites. Northern blot analysis detected major 3.0- and minor 4.8-kb SLC21A6 transcripts exclusively in liver, in contrast to the more widely expressed SLC21A3.