Anti-SLC1A6

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering. Protein function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:7791878). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport, this avoids the accumulation of negative charges due to aspartate and Na(+) symport. Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (Probable). [The UniProt Consortium]