Excitatory Amino Acid Transporter 5 (EAAT5)

EAAT5-mediated L-glutamate uptake was sodium- and voltage-dependent and chloride-independent. Transporter currents elicited by glutamate were also sodium- and voltage-dependent, but ion substitution experiments suggested that this current was largely carried by chloride ions.Although EAAT5 shares the structural homologies of the EAAT family, 1 novel feature of the EAAT5 sequence is a C-terminal motif previously identified in N-methyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering. EAAT5 has 46% amino acid sequence identity with EAAT1 (SLC1A3), 43% identity with EAAT4 (SLC1A6), 37% identity with EAAT3 (SLC1A1), and 36% identity with EAAT2 (SLC1A2).