Structural highlights
Disease
EAA2_HUMAN Non-specific early-onset epileptic encephalopathy. The disease is caused by variants affecting the gene represented in this entry.
Function
EAA2_HUMAN Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:14506254, PubMed:15265858, PubMed:26690923, PubMed:7521911). 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 (PubMed:14506254). Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (PubMed:14506254). Essential for the rapid removal of released glutamate from the synaptic cleft, and for terminating the postsynaptic action of glutamate (By similarity).[UniProtKB:P43006][1] [2] [3]
References
- ↑ Gendreau S, Voswinkel S, Torres-Salazar D, Lang N, Heidtmann H, Detro-Dassen S, Schmalzing G, Hidalgo P, Fahlke C. A trimeric quaternary structure is conserved in bacterial and human glutamate transporters. J Biol Chem. 2004 Sep 17;279(38):39505-12. Epub 2004 Jul 20. PMID:15265858 doi:http://dx.doi.org/10.1074/jbc.M408038200
- ↑ Abousaab A, Warsi J, Elvira B, Lang F. Caveolin-1 Sensitivity of Excitatory Amino Acid Transporters EAAT1, EAAT2, EAAT3, and EAAT4. J Membr Biol. 2016 Jun;249(3):239-49. doi: 10.1007/s00232-015-9863-0. Epub 2015, Dec 21. PMID:26690923 doi:http://dx.doi.org/10.1007/s00232-015-9863-0
- ↑ Arriza JL, Fairman WA, Wadiche JI, Murdoch GH, Kavanaugh MP, Amara SG. Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. J Neurosci. 1994 Sep;14(9):5559-69. PMID:7521911
