is a member of a family of plasma membrane amino acid transporters that mediate the Na(+)-independent transport of aromatic amino acids across the plasma membrane. The deduced 515-amino acid protein contains 12 transmembrane regions. It has phosphorylation sites for cAMP-dependent kinase and protein kinase C, and it has a leucine zipper motif on the ninth transmembrane domain. Human and rat SLC16A10 share 84% sequence identity. SLC16A10 also shares between 28 and 52% identity with the other monocarboxylic acid transporters. Northern blot analysis detected a 2.6-kb transcript expressed at high levels in kidney and skeletal muscle and at lower levels in placenta and heart. A faint message was detected in spleen and thymus.