ID GRIA2_RAT Reviewed; 883 AA. AC P19491; Q9R174; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 243. DE RecName: Full=Glutamate receptor 2 {ECO:0000305}; DE Short=GluR-2; DE AltName: Full=AMPA-selective glutamate receptor 2; DE AltName: Full=GluR-B; DE AltName: Full=GluR-K2; DE AltName: Full=Glutamate receptor ionotropic, AMPA 2; DE Short=GluA2 {ECO:0000303|PubMed:20547133, ECO:0000303|PubMed:27756895}; DE Flags: Precursor; GN Name=Gria2 {ECO:0000312|RGD:61862}; Synonyms=Glur2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP). RC TISSUE=Brain; RX PubMed=2166337; DOI=10.1126/science.2166337; RA Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., RA Sakmann B., Seeburg P.H.; RT "A family of AMPA-selective glutamate receptors."; RL Science 249:556-560(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP). RX PubMed=2168579; DOI=10.1126/science.2168579; RA Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S., RA Maron C., Heinemann S.F.; RT "Molecular cloning and functional expression of glutamate receptor subunit RT genes."; RL Science 249:1033-1037(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP). RC TISSUE=Brain cortex, and Hippocampus; RX PubMed=1699567; DOI=10.1016/0896-6273(90)90212-x; RA Nakanishi N., Schneider N.A., Axel R.; RT "A family of glutamate receptor genes: evidence for the formation of RT heteromultimeric receptors with distinct channel properties."; RL Neuron 5:569-581(1990). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), AND FUNCTION. RC STRAIN=Sprague-Dawley; RX PubMed=9351977; DOI=10.1124/mol.52.5.861; RA Everts I., Villmann C., Hollmann M.; RT "N-glycosylation is not a prerequisite for glutamate receptor function but RT is essential for lectin modulation."; RL Mol. Pharmacol. 52:861-873(1997). RN [5] RP RNA EDITING OF POSITION 607. RX PubMed=1717158; DOI=10.1016/0092-8674(91)90568-j; RA Sommer B., Koehler M., Sprengel R., Seeburg P.H.; RT "RNA editing in brain controls a determinant of ion flow in glutamate-gated RT channels."; RL Cell 67:11-19(1991). RN [6] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NSF, RP IDENTIFICATION IN A COMPLEX WITH NSF; NAPA AND NAPB, AND MUTAGENESIS OF RP 851-ASN-PRO-852. RX PubMed=9697855; DOI=10.1016/s0896-6273(00)80518-8; RA Osten P., Srivastava S., Inman G.J., Vilim F.S., Khatri L., Lee L.M., RA States B.A., Einheber S., Milner T.A., Hanson P.I., Ziff E.B.; RT "The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent RT interaction with NSF and alpha- and beta-SNAPs."; RL Neuron 21:99-110(1998). RN [7] RP INTERACTION WITH PRKCABP. RX PubMed=10027300; DOI=10.1016/s0896-6273(00)80689-3; RA Xia J., Zhang X., Staudinger J., Huganir R.L.; RT "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein RT PICK1."; RL Neuron 22:179-187(1999). RN [8] RP ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP). RX PubMed=1699275; DOI=10.1126/science.1699275; RA Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., RA Koehler M., Takagi T., Sakmann B., Seeburg P.H.; RT "Flip and flop: a cell-specific functional switch in glutamate-operated RT channels of the CNS."; RL Science 249:1580-1585(1990). RN [9] RP PHOSPHORYLATION AT SER-683 AND SER-717. RX PubMed=8848293; DOI=10.1016/0168-0102(95)00977-9; RA Nakazawa K., Tadakuma T., Nokihara K., Ito M.; RT "Antibody specific for phosphorylated AMPA-type glutamate receptors at RT GluR2 Ser-696."; RL Neurosci. Res. 24:75-86(1995). RN [10] RP INTERACTION WITH GRIP1. RC TISSUE=Hippocampus; RX PubMed=9069286; DOI=10.1038/386279a0; RA Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F., Huganir R.L.; RT "GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA RT receptors."; RL Nature 386:279-284(1997). RN [11] RP INTERACTION WITH GRIP2. RX PubMed=10414981; DOI=10.1523/jneurosci.19-15-06528.1999; RA Wyszynski M., Valtschanoff J.G., Naisbitt S., Dunah A.W., Kim E., RA Standaert D.G., Weinberg R., Sheng M.; RT "Association of AMPA receptors with a subset of glutamate receptor- RT interacting protein in vivo."; RL J. Neurosci. 19:6528-6537(1999). RN [12] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=12657670; DOI=10.1523/jneurosci.23-06-02112.2003; RA Calderone A., Jover T., Noh K.M., Tanaka H., Yokota H., Lin Y., RA Grooms S.Y., Regis R., Bennett M.V., Zukin R.S.; RT "Ischemic insults derepress the gene silencer REST in neurons destined to RT die."; RL J. Neurosci. 23:2112-2121(2003). RN [13] RP IDENTIFICATION OF ISOFORM 3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RX PubMed=14687553; DOI=10.1016/s0896-6273(03)00722-0; RA Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., RA Koehr G., Malinow R., Seeburg P.H., Osten P.; RT "Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing RT AMPA receptors."; RL Neuron 40:1199-1212(2003). RN [14] RP PHOSPHORYLATION AT TYR-876, AND TISSUE SPECIFICITY. RX PubMed=15240807; DOI=10.1523/jneurosci.0799-04.2004; RA Hayashi T., Huganir R.L.; RT "Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family RT tyrosine kinases."; RL J. Neurosci. 24:6152-6160(2004). RN [15] RP COMPLEX FORMATION WITH GRIP1; NGS1 AND STX12, AND FUNCTION. RX PubMed=16037816; DOI=10.1038/sj.emboj.7600755; RA Steiner P., Alberi S., Kulangara K., Yersin A., Sarria J.C., Regulier E., RA Kasas S., Dietler G., Muller D., Catsicas S., Hirling H.; RT "Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and RT recycling of the glutamate receptor subunit GluR2."; RL EMBO J. 24:2873-2884(2005). RN [16] RP SUBCELLULAR LOCATION, AND INTERACTION WITH CACNG2. RX PubMed=16793768; DOI=10.1074/jbc.m600679200; RA Bedoukian M.A., Weeks A.M., Partin K.M.; RT "Different domains of the AMPA receptor direct stargazin-mediated RT trafficking and stargazin-mediated modulation of kinetics."; RL J. Biol. Chem. 281:23908-23921(2006). RN [17] RP INTERACTION WITH LRFN1. RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005; RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., RA Kim E.; RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of RT excitatory synapses."; RL Neuron 50:233-245(2006). RN [18] RP INTERACTION WITH CACNG5. RX PubMed=18817736; DOI=10.1016/j.neuron.2008.07.034; RA Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.; RT "AMPA receptor subunit-specific regulation by a distinct family of type II RT TARPs."; RL Neuron 59:986-996(2008). RN [19] RP INTERACTION WITH CACNG5. RX PubMed=19234459; DOI=10.1038/nn.2266; RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.; RT "Selective regulation of long-form calcium-permeable AMPA receptors by an RT atypical TARP, gamma-5."; RL Nat. Neurosci. 12:277-285(2009). RN [20] RP ERRATUM OF PUBMED:19234459. RX DOI=10.1038/nn0609-808c; RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.; RL Nat. Neurosci. 12:808-808(2009). RN [21] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=19265014; DOI=10.1126/science.1167852; RA Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B., RA Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.; RT "Functional proteomics identify cornichon proteins as auxiliary subunits of RT AMPA receptors."; RL Science 323:1313-1319(2009). RN [22] RP FUNCTION, INTERACTION WITH IQSEC1, MUTAGENESIS OF VAL-875 AND TYR-876, AND RP PHOSPHORYLATION AT TYR-876. RX PubMed=20547133; DOI=10.1016/j.neuron.2010.05.003; RA Scholz R., Berberich S., Rathgeber L., Kolleker A., Koehr G., Kornau H.C.; RT "AMPA receptor signaling through BRAG2 and Arf6 critical for long-term RT synaptic depression."; RL Neuron 66:768-780(2010). RN [23] RP FUNCTION. RX PubMed=21172611; DOI=10.1016/j.neuron.2010.11.026; RA Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H., RA Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.; RT "Hippocampal AMPA receptor gating controlled by both TARP and cornichon RT proteins."; RL Neuron 68:1082-1096(2010). RN [24] RP INTERACTION WITH ATAD1 AND GRIP1. RX PubMed=21496646; DOI=10.1016/j.cell.2011.03.016; RA Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H., RA Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M., RA Dawson V.L.; RT "The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic RT plasticity and behavior."; RL Cell 145:284-299(2011). RN [25] RP INTERACTION WITH CACNG2. RX PubMed=27756895; DOI=10.1038/srep35283; RA Rademacher N., Schmerl B., Lardong J.A., Wahl M.C., Shoichet S.A.; RT "MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell RT adhesion molecules to core components of the postsynaptic density."; RL Sci. Rep. 6:35283-35283(2016). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 404-796 IN COMPLEX WITH KAINATE. RX PubMed=9804426; DOI=10.1038/27692; RA Armstrong N., Sun Y., Chen G.Q., Gouaux E.; RT "Structure of a glutamate-receptor ligand-binding core in complex with RT kainate."; RL Nature 395:913-917(1998). RN [27] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 413-796 IN COMPLEXES WITH RP GLUTAMATE; AMPA; KAINATE; DNQX AND ZINC. RX PubMed=11086992; DOI=10.1016/s0896-6273(00)00094-5; RA Armstrong N., Gouaux E.; RT "Mechanisms for activation and antagonism of an AMPA-sensitive glutamate RT receptor: crystal structures of the GluR2 ligand binding core."; RL Neuron 28:165-181(2000). RN [28] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH RP QUISQUALATE, AND FUNCTION. RX PubMed=12501192; DOI=10.1021/bi020583k; RA Jin R., Horning M., Mayer M.L., Gouaux E.; RT "Mechanism of activation and selectivity in a ligand-gated ion channel: RT structural and functional studies of GluR2 and quisqualate."; RL Biochemistry 41:15635-15643(2002). RN [29] RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ACPA RP AND BR-HIBO. RX PubMed=12215417; DOI=10.1016/s0022-2836(02)00650-2; RA Hogner A., Kastrup J.S., Jin R., Liljefors T., Mayer M.L., Egebjerg J., RA Larsen I.K., Gouaux E.; RT "Structural basis for AMPA receptor activation and ligand selectivity: RT crystal structures of five agonist complexes with the GluR2 ligand-binding RT core."; RL J. Mol. Biol. 322:93-109(2002). RN [30] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; RP DNQX AND KAINATE, FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-504 AND RP ASN-775. RX PubMed=12015593; DOI=10.1038/417245a; RA Sun Y., Olson R., Horning M., Armstrong N., Mayer M., Gouaux E.; RT "Mechanism of glutamate receptor desensitization."; RL Nature 417:245-253(2002). RN [31] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 413-796 IN COMPLEXES WITH ATPA RP AND ZINC IONS. RX PubMed=12593667; DOI=10.1021/jm021020+; RA Lunn M.-L., Hogner A., Stensboel T.B., Gouaux E., Egebjerg J., RA Kastrup J.S.; RT "Three-dimensional structure of the ligand-binding core of GluR2 in complex RT with the agonist (S)-ATPA: implications for receptor subunit selectivity."; RL J. Med. Chem. 46:872-875(2003). RN [32] RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-796 IN COMPLEXES WITH RP WILLARDIINES, AND FUNCTION. RX PubMed=12872125; DOI=10.1038/nn1091; RA Jin R., Banke T.G., Mayer M.L., Traynelis S.F., Gouaux E.; RT "Structural basis for partial agonist action at ionotropic glutamate RT receptors."; RL Nat. Neurosci. 6:803-810(2003). RN [33] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 413-796 IN COMPLEXES WITH AMPA; RP KAINATE AND QUISQUALATE, AND FUNCTION. RX PubMed=12730367; DOI=10.1073/pnas.1037393100; RA Armstrong N., Mayer M., Gouaux E.; RT "Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic RT adjustment of agonist-induced conformational changes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5736-5741(2003). RN [34] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEXES WITH RP ANIRACETAM AND CX614, AND FUNCTION. RX PubMed=16192394; DOI=10.1523/jneurosci.2567-05.2005; RA Jin R., Clark S., Weeks A.M., Dudman J.T., Gouaux E., Partin K.M.; RT "Mechanism of positive allosteric modulators acting on AMPA receptors."; RL J. Neurosci. 25:9027-9036(2005). RN [35] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-796 IN COMPLEXES WITH CPW399 RP AND KAINATE, AND FUNCTION. RX PubMed=15591246; DOI=10.1124/mol.104.002931; RA Frandsen A., Pickering D.S., Vestergaard B., Kasper C., Nielsen B.B., RA Greenwood J.R., Campiani G., Fattorusso C., Gajhede M., Schousboe A., RA Kastrup J.S.; RT "Tyr702 is an important determinant of agonist binding and domain closure RT of the ligand-binding core of GluR2."; RL Mol. Pharmacol. 67:703-713(2005). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 413-794, FUNCTION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17018279; DOI=10.1016/j.cell.2006.08.037; RA Armstrong N., Jasti J., Beich-Frandsen M., Gouaux E.; RT "Measurement of conformational changes accompanying desensitization in an RT ionotropic glutamate receptor."; RL Cell 127:85-97(2006). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE RP AND S1209, AND FUNCTION. RX PubMed=16483599; DOI=10.1016/j.jmb.2006.01.024; RA Kasper C., Pickering D.S., Mirza O., Olsen L., Kristensen A.S., RA Greenwood J.R., Liljefors T., Schousboe A., Waetjen F., Gajhede M., RA Sigurskjold B.W., Kastrup J.S.; RT "The structure of a mixed GluR2 ligand-binding core dimer in complex with RT (S)-glutamate and the antagonist (S)-NS1209."; RL J. Mol. Biol. 357:1184-1201(2006). RN [38] RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 25-847 IN COMPLEX WITH GLUTAMATE RP ANALOG, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 413-796, FUNCTION, RP SUBUNIT, MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-370. RX PubMed=19946266; DOI=10.1038/nature08624; RA Sobolevsky A.I., Rosconi M.P., Gouaux E.; RT "X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate RT receptor."; RL Nature 462:745-756(2009). RN [39] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 25-400, FUNCTION, SUBUNIT, RP DISULFIDE BOND, AND GLYCOSYLATION AT ASN-256 AND ASN-370. RX PubMed=21317873; DOI=10.1038/emboj.2011.16; RA Rossmann M., Sukumaran M., Penn A.C., Veprintsev D.B., Babu M.M., RA Greger I.H.; RT "Subunit-selective N-terminal domain associations organize the formation of RT AMPA receptor heteromers."; RL EMBO J. 30:959-971(2011). RN [40] RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 414-794 IN COMPLEXES WITH RP GLUTAMATE; IODOWILLARDIINE AND KAINATE, FUNCTION, AND DISULFIDE BONDS. RX PubMed=21846932; DOI=10.1074/jbc.m111.269001; RA Ahmed A.H., Wang S., Chuang H.H., Oswald R.E.; RT "Mechanism of AMPA receptor activation by partial agonists: disulfide RT trapping of closed lobe conformations."; RL J. Biol. Chem. 286:35257-35266(2011). RN [41] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 25-850 IN COMPLEXES WITH KAINATE; RP FLUORAWILLARDINE AND THE CONE SNAIL TOXIN CON-IKOT-IKOT, DISULFIDE BOND, RP GLYCOSYLATION AT ASN-370, AND SITES ARG-474; ILE-654; ARG-681 AND LYS-773. RX PubMed=25103405; DOI=10.1126/science.1258409; RA Chen L., Durr K.L., Gouaux E.; RT "X-ray structures of AMPA receptor-cone snail toxin complexes illuminate RT activation mechanism."; RL Science 345:1021-1026(2014). CC -!- FUNCTION: Receptor for glutamate that functions as a ligand-gated ion CC channel in the central nervous system and plays an important role in CC excitatory synaptic transmission. L-glutamate acts as an excitatory CC neurotransmitter at many synapses in the central nervous system. CC Binding of the excitatory neurotransmitter L-glutamate induces a CC conformation change, leading to the opening of the cation channel, and CC thereby converts the chemical signal to an electrical impulse. The CC receptor then desensitizes rapidly and enters a transient inactive CC state, characterized by the presence of bound agonist. In the presence CC of CACNG4 or CACNG7 or CACNG8, shows resensitization which is CC characterized by a delayed accumulation of current flux upon continued CC application of glutamate. Through complex formation with NSG1, GRIP1 CC and STX12 controls the intracellular fate of AMPAR and the endosomal CC sorting of the GRIA2 subunit toward recycling and membrane targeting CC (PubMed:16037816). {ECO:0000269|PubMed:12015593, CC ECO:0000269|PubMed:12501192, ECO:0000269|PubMed:12730367, CC ECO:0000269|PubMed:12872125, ECO:0000269|PubMed:15591246, CC ECO:0000269|PubMed:16037816, ECO:0000269|PubMed:16192394, CC ECO:0000269|PubMed:16483599, ECO:0000269|PubMed:17018279, CC ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:19946266, CC ECO:0000269|PubMed:20547133, ECO:0000269|PubMed:21172611, CC ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:21846932, CC ECO:0000269|PubMed:9351977}. CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate CC receptor subunits. Tetramers may be formed by the dimerization of CC dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CC CSPG4 (By similarity). Interacts with ATAD1 in an ATP-dependent manner. CC ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 CC and leads to AMPAR complex disassembly. Interacts with NSF via its C- CC terminus. Interacts with CACNG2, PRKCABP and GRIP2 (PubMed:27756895). CC Part of a complex containing GRIA2, NSF and NAPA and/or NAPB. Interacts CC with PICK1 (via PDZ domain) (By similarity). Interacts with GRIA1 and CC SYNDIG1. Interacts with SNX27 (via PDZ domain); the interaction is CC required for recycling to the plasma membrane when endocytosed and CC prevent degradation in lysosomes (By similarity). Interacts with LRFN1. CC Found in a complex with GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CC CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5. Interacts CC with OLFM2 (By similarity). Interacts with AP4B1, AP4E1 and AP4M1; CC probably indirect it mediates the somatodendritic localization of GRIA2 CC in neurons (By similarity). Forms a complex with NSG1, GRIA2 and STX12; CC controls the intracellular fate of AMPAR and the endosomal sorting of CC the GRIA2 subunit toward recycling and membrane targeting CC (PubMed:16037816). Interacts with IQSEC1; the interaction is required CC for ARF6 activation (PubMed:20547133). {ECO:0000250|UniProtKB:P23819, CC ECO:0000269|PubMed:10027300, ECO:0000269|PubMed:10414981, CC ECO:0000269|PubMed:12015593, ECO:0000269|PubMed:12501192, CC ECO:0000269|PubMed:16037816, ECO:0000269|PubMed:16483599, CC ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:16793768, CC ECO:0000269|PubMed:18817736, ECO:0000269|PubMed:19234459, CC ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:19946266, CC ECO:0000269|PubMed:20547133, ECO:0000269|PubMed:21317873, CC ECO:0000269|PubMed:21496646, ECO:0000269|PubMed:27756895, CC ECO:0000269|PubMed:9069286, ECO:0000269|PubMed:9697855, CC ECO:0000269|PubMed:9804426}. CC -!- INTERACTION: CC P19491; Q8CGU4: Agap2; NbExp=4; IntAct=EBI-77718, EBI-4409108; CC P19491; P84092: Ap2m1; NbExp=2; IntAct=EBI-77718, EBI-297693; CC P19491; Q505J9: Atad1; NbExp=3; IntAct=EBI-77718, EBI-4280289; CC P19491; Q71RJ2: Cacng2; NbExp=2; IntAct=EBI-77718, EBI-8538384; CC P19491; P19490: Gria1; NbExp=3; IntAct=EBI-77718, EBI-371642; CC P19491; P19491: Gria2; NbExp=12; IntAct=EBI-77718, EBI-77718; CC P19491; P97879: Grip1; NbExp=15; IntAct=EBI-77718, EBI-936113; CC P19491; Q9WTW1-3: Grip2; NbExp=7; IntAct=EBI-77718, EBI-936068; CC P19491; Q9QUL6: Nsf; NbExp=5; IntAct=EBI-77718, EBI-925794; CC P19491; Q9EP80: Pick1; NbExp=13; IntAct=EBI-77718, EBI-77728; CC P19491; Q91Z80: Ppfia4; NbExp=3; IntAct=EBI-77718, EBI-8276907; CC P19491; P40748: Syt3; NbExp=3; IntAct=EBI-77718, EBI-458106; CC P19491; Q13136: PPFIA1; Xeno; NbExp=2; IntAct=EBI-77718, EBI-745426; CC P19491-2; P19490-2: Gria1; NbExp=2; IntAct=EBI-15817825, EBI-26900830; CC P19491-2; P19491-2: Gria2; NbExp=18; IntAct=EBI-15817825, EBI-15817825; CC P19491-2; P19492-2: Gria3; NbExp=6; IntAct=EBI-15817825, EBI-16201849; CC P19491-2; P19493-2: Gria4; NbExp=2; IntAct=EBI-15817825, EBI-15852899; CC P19491-2; P0CB20; Xeno; NbExp=2; IntAct=EBI-15817825, EBI-16116011; CC P19491-3; P49185: Mapk8; NbExp=2; IntAct=EBI-9118256, EBI-7456505; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23819}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P23819}. Endoplasmic CC reticulum membrane {ECO:0000250}; Multi-pass membrane protein CC {ECO:0000250}. Postsynaptic density membrane CC {ECO:0000250|UniProtKB:P23819}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P23819}. Note=Interaction with CACNG2, CNIH2 and CC CNIH3 promotes cell surface expression (By similarity). Displays a CC somatodendritic localization and is excluded from axons in neurons (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P23819}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Flop; CC IsoId=P19491-1; Sequence=Displayed; CC Name=Flip; CC IsoId=P19491-2; Sequence=VSP_000111, VSP_000112, VSP_000113, CC VSP_000114; CC Name=3; Synonyms=Long; CC IsoId=P19491-3; Sequence=VSP_029310; CC -!- TISSUE SPECIFICITY: Detected in forebrain. Detected in dendrites of CC neuronal cells. Expressed in the pyramidal cell layers of CA1 and CA3 CC and in the granule cell layer of the dentate gyrus (PubMed:12657670). CC {ECO:0000269|PubMed:12657670, ECO:0000269|PubMed:14687553, CC ECO:0000269|PubMed:15240807, ECO:0000269|PubMed:9697855}. CC -!- DEVELOPMENTAL STAGE: Detected at low levels in newborns. Levels CC increase strongly and are highest in hippocampus from 8 to 14 day old CC animals. Detected at intermediate levels at day 42 (at protein level). CC {ECO:0000269|PubMed:14687553}. CC -!- INDUCTION: Down-regulated in the pyramidal cell layer of CA1 in the CC hippocampus by global ischemia. {ECO:0000269|PubMed:12657670}. CC -!- DOMAIN: The M4 transmembrane segment mediates tetramerization and is CC required for cell surface expression. {ECO:0000250}. CC -!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610 CC palmitoylation leads to Golgi retention and decreased cell surface CC expression. In contrast, Cys-836 palmitoylation does not affect cell CC surface expression but regulates stimulation-dependent endocytosis (By CC similarity). {ECO:0000250|UniProtKB:P23819}. CC -!- PTM: Phosphorylation at Tyr-876 is required forc interaction with CC IQSEC1 and ARF6 activation. {ECO:0000269|PubMed:20547133}. CC -!- PTM: Ubiquitinated by RNF167, leading to its degradation. CC {ECO:0000250|UniProtKB:P42262}. CC -!- RNA EDITING: Modified_positions=607 {ECO:0000269|PubMed:1717158}; CC Note=Fully edited in the brain. Heteromerically expressed edited GLUR2 CC (R) receptor complexes are impermeable to calcium, whereas the unedited CC (Q) forms are highly permeable to divalent ions (By similarity). CC {ECO:0000250}; CC -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a CC variety of receptors that are named according to their selective CC agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate. CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) CC family. GRIA2 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M36419; AAA41244.1; -; mRNA. DR EMBL; M38061; AAC37652.1; -; mRNA. DR EMBL; M85035; AAA41240.1; -; mRNA. DR EMBL; X54655; CAA38465.1; -; mRNA. DR EMBL; AF164344; AAD51284.1; -; mRNA. DR PIR; S13677; S13677. DR RefSeq; NP_001077280.1; NM_001083811.1. DR RefSeq; NP_058957.1; NM_017261.2. DR PDB; 1FTJ; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1FTK; X-ray; 1.60 A; A=404-528, A=653-796. DR PDB; 1FTL; X-ray; 1.80 A; A/B=413-527, A/B=653-796. DR PDB; 1FTM; X-ray; 1.70 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1FTO; X-ray; 2.00 A; A/B=413-527, A/B=653-796. DR PDB; 1FW0; X-ray; 1.90 A; A=413-527, A=653-796. DR PDB; 1GR2; X-ray; 1.90 A; A=404-528, A=652-796. DR PDB; 1LB8; X-ray; 2.30 A; A/B=413-527, A/B=653-796. DR PDB; 1LB9; X-ray; 2.30 A; A/B=413-527, A/B=653-796. DR PDB; 1LBB; X-ray; 2.10 A; A=413-527, A=653-796. DR PDB; 1LBC; X-ray; 1.80 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1M5B; X-ray; 1.85 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1M5C; X-ray; 1.65 A; A=413-527, A=653-796. DR PDB; 1M5D; X-ray; 1.73 A; A=413-527, A=653-796. DR PDB; 1M5E; X-ray; 1.46 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1M5F; X-ray; 1.95 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MM6; X-ray; 2.15 A; A/B=413-527, A/B=653-796. DR PDB; 1MM7; X-ray; 1.65 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MQD; X-ray; 1.46 A; A/B/C/D=413-527, A/B/C/D=653-794. DR PDB; 1MQG; X-ray; 2.15 A; A/B=413-527, A/B=653-796. DR PDB; 1MQH; X-ray; 1.80 A; A=413-527, A=653-796. DR PDB; 1MQI; X-ray; 1.35 A; A=413-527, A=653-796. DR PDB; 1MQJ; X-ray; 1.65 A; A=413-527, A=653-796. DR PDB; 1MS7; X-ray; 1.97 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MXU; X-ray; 1.80 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MXV; X-ray; 1.95 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MXW; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MXX; X-ray; 2.00 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MXY; X-ray; 1.95 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MXZ; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MY0; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MY1; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MY2; X-ray; 1.80 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MY3; X-ray; 1.75 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1MY4; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1N0T; X-ray; 2.10 A; A/B/C/D=413-527, A/B/C/D=653-796. DR PDB; 1NNK; X-ray; 1.85 A; A=413-527, A=653-796. DR PDB; 1NNP; X-ray; 1.90 A; A/B=413-527, A/B=653-796. DR PDB; 1P1N; X-ray; 1.60 A; A=413-527, A=653-796. DR PDB; 1P1O; X-ray; 1.60 A; A=413-527, A=653-796. DR PDB; 1P1Q; X-ray; 2.00 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 1P1U; X-ray; 2.00 A; A/B=413-527, A/B=653-796. DR PDB; 1P1W; X-ray; 1.80 A; A/B=413-527, A/B=653-796. DR PDB; 1SYH; X-ray; 1.80 A; A=413-527, A=653-796. DR PDB; 1SYI; X-ray; 2.10 A; A/B=413-527, A/B=653-796. DR PDB; 1WVJ; X-ray; 1.75 A; A=413-527, A=653-796. DR PDB; 1XHY; X-ray; 1.85 A; A=413-527, A=653-796. DR PDB; 2AIX; X-ray; 2.17 A; A=413-527, A=653-796. DR PDB; 2AL4; X-ray; 1.70 A; A/B/C/D/E/F=413-527, A/B/C/D/E/F=653-796. DR PDB; 2AL5; X-ray; 1.65 A; A/B=413-527, A/B=653-796. DR PDB; 2ANJ; X-ray; 2.10 A; A=413-527, A=653-796. DR PDB; 2CMO; X-ray; 2.65 A; A/B=413-527, A/B=653-796. DR PDB; 2GFE; X-ray; 1.54 A; A/B/C=413-527, A/B/C=653-795. DR PDB; 2I3V; X-ray; 2.40 A; A/B/C/D=413-527, A/B/C/D=655-794. DR PDB; 2I3W; X-ray; 2.30 A; A/B=413-527, A/B=653-794. DR PDB; 2P2A; X-ray; 2.26 A; A/B=413-527, A/B=653-796. DR PDB; 2UXA; X-ray; 2.38 A; A/B/C=412-795. DR PDB; 2XX7; X-ray; 2.20 A; A/B/C=413-527, A/B/C=653-795. DR PDB; 2XX8; X-ray; 1.55 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 2XX9; X-ray; 1.97 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 2XXH; X-ray; 1.50 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 2XXI; X-ray; 1.60 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 3B6Q; X-ray; 2.00 A; A=413-527, A=653-796. DR PDB; 3B6T; X-ray; 2.10 A; A=413-527, A=653-796. DR PDB; 3B6W; X-ray; 1.70 A; A/B/C/D=413-527, A/B/C/D=653-796. DR PDB; 3B7D; X-ray; 2.50 A; A/B/C/D/E/F/G/H=413-527, A/B/C/D/E/F/G/H=653-794. DR PDB; 3BBR; X-ray; 2.25 A; A/B=413-527, A/B=653-796. DR PDB; 3BFT; X-ray; 2.27 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 3BFU; X-ray; 1.95 A; A/B/C/D=413-527, A/B/C/D=653-796. DR PDB; 3BKI; X-ray; 1.87 A; B/C/D/P=413-527, B/C/D/P=653-796. DR PDB; 3DP6; X-ray; 1.55 A; A/B/C=413-527, A/B/C=653-794. DR PDB; 3H03; X-ray; 1.90 A; A/B/D/G=414-527, A/B/D/G=653-794. DR PDB; 3H06; X-ray; 2.80 A; B/E/G/H/J/L/N/P=414-527, B/E/G/H/J/L/N/P=653-794. DR PDB; 3H5V; X-ray; 2.33 A; A/B/C=21-404. DR PDB; 3H5W; X-ray; 2.69 A; A/B=21-404. DR PDB; 3H6T; X-ray; 2.25 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 3H6U; X-ray; 1.85 A; A=413-527, A=653-796. DR PDB; 3H6V; X-ray; 2.10 A; A/B=413-527, A/B=653-796. DR PDB; 3H6W; X-ray; 1.49 A; A/B=413-527, A/B=653-796. DR PDB; 3HSY; X-ray; 1.75 A; A/B=25-400. DR PDB; 3IJO; X-ray; 2.00 A; B/E/H=414-527, B/E/H=653-794. DR PDB; 3IJX; X-ray; 2.88 A; B/D/H=414-527, B/D/H=653-794. DR PDB; 3IK6; X-ray; 2.10 A; B/E/H=414-527, B/E/H=653-794. DR PDB; 3IL1; X-ray; 2.00 A; B/E/H=414-527, B/E/H=653-794. DR PDB; 3ILT; X-ray; 2.11 A; B/E/H=414-527, B/E/H=653-794. DR PDB; 3ILU; X-ray; 2.00 A; B/E/H=414-527, B/E/H=653-794. DR PDB; 3KG2; X-ray; 3.60 A; A/B/C/D=25-412, A/B/C/D=414-847. DR PDB; 3KGC; X-ray; 1.55 A; A/B=414-527, A/B=654-795. DR PDB; 3LSF; X-ray; 1.85 A; B/E/H=414-527, B/E/H=653-794. DR PDB; 3LSL; X-ray; 2.12 A; A/D/G=414-527, A/D/G=653-794. DR PDB; 3M3L; X-ray; 1.85 A; A/D/G=414-794. DR PDB; 3N6V; X-ray; 3.20 A; A/B/C/D/E/F=27-400. DR PDB; 3O28; X-ray; 2.00 A; A=413-527, A=653-795. DR PDB; 3O29; X-ray; 2.02 A; A=413-527, A=653-795. DR PDB; 3O2A; X-ray; 1.90 A; A=413-527, A=653-795. DR PDB; 3O2J; X-ray; 1.95 A; A/B=22-400. DR PDB; 3O6G; X-ray; 1.80 A; A=413-527, A=653-795. DR PDB; 3O6H; X-ray; 2.10 A; A=413-527, A=653-795. DR PDB; 3O6I; X-ray; 1.80 A; A=413-527, A=653-795. DR PDB; 3PD8; X-ray; 2.48 A; A/B/C=413-527, A/B/C=653-795. DR PDB; 3PD9; X-ray; 2.10 A; A/B=413-527, A/B=653-795. DR PDB; 3PMV; X-ray; 1.80 A; A=413-527, A=653-795. DR PDB; 3PMW; X-ray; 2.20 A; A=413-527, A=653-795. DR PDB; 3PMX; X-ray; 1.87 A; A=413-527, A=653-795. DR PDB; 3RTF; X-ray; 1.70 A; B/D/F=414-527, B/D/F=653-794. DR PDB; 3RTW; X-ray; 2.10 A; B/D/F=414-527, B/D/F=653-794. DR PDB; 3T93; X-ray; 1.91 A; B/D/F=414-527, B/D/F=653-794. DR PDB; 3T96; X-ray; 1.87 A; B/D/F=414-527, B/D/F=653-794. DR PDB; 3T9H; X-ray; 2.02 A; B/D/F=414-527, B/D/F=653-794. DR PDB; 3T9U; X-ray; 1.97 A; A/B/C=414-527, A/B/C=653-794. DR PDB; 3T9V; X-ray; 1.98 A; A/B=414-527, A/B=653-794. DR PDB; 3T9X; X-ray; 1.82 A; B/D/F=414-527, B/D/F=653-794. DR PDB; 3TDJ; X-ray; 1.95 A; A/B=413-527, A/B=653-796. DR PDB; 3TKD; X-ray; 1.45 A; A/B=413-527, A/B=653-795. DR PDB; 3TZA; X-ray; 1.90 A; A/B=413-527, A/B=653-796. DR PDB; 4FAT; X-ray; 1.40 A; A=413-527, A=653-796. DR PDB; 4G8M; X-ray; 2.05 A; A/B=413-527, A/B=653-796. DR PDB; 4GXS; X-ray; 1.96 A; B/D=414-527, B/D=653-794. DR PDB; 4H8J; X-ray; 1.80 A; A/B/C/D=413-527, A/B/C/D=653-797. DR PDB; 4IGT; X-ray; 1.24 A; A=413-527, A=653-796. DR PDB; 4ISU; X-ray; 2.30 A; A/B/C/D=413-527, A/B/C/D=653-796. DR PDB; 4IY5; X-ray; 2.00 A; A/B=413-527, A/B=653-796. DR PDB; 4IY6; X-ray; 1.72 A; A=413-527, A=653-796. DR PDB; 4L17; X-ray; 2.80 A; A/C/E/G=413-527, A/C/E/G=653-796. DR PDB; 4LZ5; X-ray; 1.50 A; A/B/C=404-527, A/B/C=653-796. DR PDB; 4LZ7; X-ray; 2.10 A; A/B/C=404-527, A/B/C=653-796. DR PDB; 4LZ8; X-ray; 1.85 A; A/B/C=404-527, A/B/C=653-796. DR PDB; 4N07; X-ray; 1.87 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 4O3A; X-ray; 1.80 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 4O3B; X-ray; 1.91 A; A/B=413-527, A/B=653-796. DR PDB; 4O3C; X-ray; 1.50 A; A=413-527, A=653-796. DR PDB; 4Q30; X-ray; 2.03 A; B/D/F=414-527, B/D/F=653-794. DR PDB; 4U1O; X-ray; 1.85 A; A=413-527, A=653-796. DR PDB; 4U1W; X-ray; 3.25 A; A/B/C/D=25-412, A/B/C/D=414-622, A/B/C/D=624-847. DR PDB; 4U1X; X-ray; 3.30 A; A/B/C/D=25-412, A/B/C/D=414-555, A/B/C/D=557-602, A/B/C/D=604-622, A/B/C/D=624-847. DR PDB; 4U1Y; X-ray; 3.90 A; A/B/C/D=25-412, A/B/C/D=414-555, A/B/C/D=557-602, A/B/C/D=604-622, A/B/C/D=624-847. DR PDB; 4U1Z; X-ray; 1.94 A; A=413-527, A=653-796. DR PDB; 4U21; X-ray; 1.39 A; A/B=413-527, A/B=654-796. DR PDB; 4U22; X-ray; 1.44 A; A=413-527, A=653-796. DR PDB; 4U23; X-ray; 1.67 A; A=413-527, A=653-796. DR PDB; 4U2P; X-ray; 3.24 A; A/B/C/D=25-412, A/B/C/D=414-622, A/B/C/D=624-847. DR PDB; 4U2Q; X-ray; 3.52 A; A/B/C/D=25-412, A/B/C/D=414-622, A/B/C/D=624-847. DR PDB; 4U2R; X-ray; 1.41 A; A/B/C/D=413-527, A/B/C/D=653-796. DR PDB; 4U4F; X-ray; 4.79 A; A/B/C/D=25-412, A/B/C/D=414-847. DR PDB; 4U4G; X-ray; 4.49 A; A/B/C/D=25-412, A/B/C/D=414-847. DR PDB; 4U4S; X-ray; 1.90 A; A/B=413-527, A/B=653-796. DR PDB; 4U4X; X-ray; 1.56 A; A/B=413-527, A/B=653-796. DR PDB; 4U5B; X-ray; 3.50 A; A/B/C/D=25-412, A/B/C/D=414-555, A/B/C/D=557-602, A/B/C/D=604-622, A/B/C/D=624-850. DR PDB; 4U5C; X-ray; 3.69 A; A/B/C/D=25-412, A/B/C/D=414-555, A/B/C/D=557-602, A/B/C/D=604-622, A/B/C/D=624-850. DR PDB; 4U5D; X-ray; 3.58 A; A/B/C/D=25-412, A/B/C/D=414-555, A/B/C/D=557-602, A/B/C/D=604-622, A/B/C/D=624-850. DR PDB; 4U5E; X-ray; 3.51 A; A/B/C/D=25-412, A/B/C/D=414-555, A/B/C/D=557-602, A/B/C/D=604-622, A/B/C/D=624-850. DR PDB; 4U5F; X-ray; 3.70 A; A/B/C/D=25-412, A/B/C/D=414-850. DR PDB; 4UQ6; EM; 12.80 A; A/B/C/D=22-847. DR PDB; 4UQJ; EM; 10.40 A; A/B/C/D=22-847. DR PDB; 4UQK; EM; 16.40 A; A/B/C/D=22-847. DR PDB; 4X48; X-ray; 1.89 A; A/B/C=413-527, A/B/C=653-796. DR PDB; 4YMA; X-ray; 1.90 A; A/B=413-527, A/B=653-797. DR PDB; 4YU0; X-ray; 1.26 A; A/B=413-527, A/B=653-796. DR PDB; 4Z0I; X-ray; 1.45 A; A/B=413-527, A/B=653-796. DR PDB; 5BUU; X-ray; 2.07 A; A/B=413-527, A/B=653-796. DR PDB; 5CBR; X-ray; 2.00 A; A=413-527, A=653-797. DR PDB; 5CBS; X-ray; 1.80 A; A/B/C/D=413-527, A/B/C/D=653-797. DR PDB; 5ELV; X-ray; 1.92 A; A/B=413-527, A/B=653-797. DR PDB; 5FHM; X-ray; 1.55 A; A/B=413-527, A/B=653-797. DR PDB; 5FHN; X-ray; 1.60 A; A=413-527, A=653-797. DR PDB; 5FHO; X-ray; 2.30 A; A/B/C/D=413-527, A/B/C/D=653-797. DR PDB; 5FTH; X-ray; 2.90 A; A/B/C=404-527, A/B/C=653-795. DR PDB; 5FTI; X-ray; 1.35 A; A/B=404-527, A/B=653-795. DR PDB; 5FWX; X-ray; 2.50 A; A/C=25-400. DR PDB; 5FWY; X-ray; 2.12 A; A/C=25-400. DR PDB; 5IDE; EM; 8.25 A; A/C=23-883. DR PDB; 5IDF; EM; 10.31 A; A/C=23-883. DR PDB; 5JEI; X-ray; 1.23 A; A=413-527, A=653-797. DR PDB; 5KBS; EM; 8.70 A; A/B/C/D=25-847. DR PDB; 5KBT; EM; 6.40 A; A/B/C/D=25-847. DR PDB; 5KBU; EM; 7.80 A; A/B/C/D=25-847. DR PDB; 5KBV; EM; 6.80 A; A/B/C/D=25-412, A/B/C/D=414-847. DR PDB; 5KK2; EM; 7.30 A; A/B/C/D=1-883. DR PDB; 5L1B; X-ray; 4.00 A; A/B/C/D=25-412, A/B/C/D=414-565, A/B/C/D=588-847. DR PDB; 5L1E; X-ray; 4.37 A; A/B/C/D=25-412, A/B/C/D=414-565, A/B/C/D=588-847. DR PDB; 5L1F; X-ray; 4.00 A; A/B/C/D=25-412, A/B/C/D=414-565, A/B/C/D=588-847. DR PDB; 5L1G; X-ray; 4.51 A; A/B/C/D=25-412, A/B/C/D=414-565, A/B/C/D=588-847. DR PDB; 5L1H; X-ray; 3.80 A; A/B/C/D=25-412, A/B/C/D=414-565, A/B/C/D=588-847. DR PDB; 5N6P; X-ray; 2.80 A; A=25-400. DR PDB; 5NG9; X-ray; 1.15 A; A=413-527, A=653-797. DR PDB; 5NIH; X-ray; 1.30 A; A/B=413-527, A/B=653-797. DR PDB; 5NS9; X-ray; 1.44 A; A/B=413-527, A/B=653-797. DR PDB; 5O9A; X-ray; 1.78 A; A/B/C/D=413-527, A/B/C/D=653-797. DR PDB; 5OEW; X-ray; 2.00 A; A/B/C=413-527, A/B/C=653-797. DR PDB; 5VHW; EM; 7.80 A; A/B/C/D=25-847. DR PDB; 5VHX; EM; 8.30 A; A/B/C/D/E=25-847. DR PDB; 5VHY; EM; 4.60 A; A/B/C/D/E/F=25-847. DR PDB; 5VHZ; EM; 8.40 A; A/B/C/D/E/F=25-847. DR PDB; 5VOT; EM; 4.90 A; A/B/C/D=1-883. DR PDB; 5VOU; EM; 6.40 A; A/B/C/D=1-883. DR PDB; 5VOV; EM; 7.70 A; A/B/C/D=1-883. DR PDB; 5WEK; EM; 4.60 A; A/B/C/D=25-847. DR PDB; 5WEL; EM; 4.40 A; A/B/C/D=25-847. DR PDB; 5WEM; EM; 6.10 A; A/B/C/D=25-847. DR PDB; 5WEN; EM; 6.80 A; A/B/C/D=25-847. DR PDB; 5WEO; EM; 4.20 A; A/B/C/D=25-847. DR PDB; 6DLZ; EM; 3.90 A; A/B/C/D=25-847. DR PDB; 6DM0; EM; 4.40 A; A/B/C/D=25-847. DR PDB; 6DM1; EM; 4.20 A; A/B/C/D=25-847. DR PDB; 6FAZ; X-ray; 1.40 A; A/B=413-527, A/B=653-797. DR PDB; 6FQG; X-ray; 2.34 A; A/B=413-527, A/B=653-797. DR PDB; 6FQH; X-ray; 1.76 A; A/B=400-527, A/B=653-797. DR PDB; 6FQI; X-ray; 2.91 A; A/B=413-527, A/B=653-797. DR PDB; 6FQJ; X-ray; 2.50 A; A/B/C/D/E/F/G/H=413-527, A/B/C/D/E/F/G/H=653-797. DR PDB; 6FQK; X-ray; 1.98 A; A/B=400-527, A/B=653-797. DR PDB; 6GIV; X-ray; 1.75 A; A=413-527, A=653-797. DR PDB; 6GL4; X-ray; 1.95 A; A/B=413-527, A/B=653-797. DR PDB; 6HC9; X-ray; 2.40 A; A/B=413-527, A/B=653-797. DR PDB; 6HCA; X-ray; 1.88 A; A/B=413-527, A/B=653-797. DR PDB; 6HCB; X-ray; 1.90 A; A/B=413-527, A/B=653-797. DR PDB; 6HCC; X-ray; 1.62 A; A/B=413-527, A/B=653-797. DR PDB; 6HCH; X-ray; 1.60 A; A/B/C=413-527, A/B/C=653-797. DR PDB; 6NJL; EM; 6.70 A; B/D=1-883. DR PDB; 6NJM; EM; 6.50 A; B/D=1-883. DR PDB; 6NJN; EM; 6.50 A; B/D=1-883. DR PDB; 6O9G; EM; 4.80 A; A/B/C/D=25-847. DR PDB; 6PEQ; EM; 2.97 A; A/B/C/D=1-868. DR PDB; 6Q54; X-ray; 1.40 A; A/B=413-527, A/B=653-797. DR PDB; 6Q60; X-ray; 1.55 A; A/B=413-527, A/B=653-797. DR PDB; 6QKC; EM; 4.10 A; B/D=1-860. DR PDB; 6QKZ; EM; 6.30 A; B/D=22-860. DR PDB; 6RUQ; X-ray; 4.65 A; A/B/C/D=25-847. DR PDB; 6U5S; EM; 3.07 A; A/B/C/D=1-868. DR PDB; 6U6I; EM; 3.12 A; A/B/C/D=1-868. DR PDB; 6UCB; EM; 3.28 A; A/B/C/D=1-868. DR PDB; 6UD4; EM; 3.30 A; A/B/C/D=1-868. DR PDB; 6UD8; EM; 3.20 A; A/B/C/D=1-868. DR PDB; 6XSR; X-ray; 4.25 A; A/B/C/D=25-838. DR PDB; 6YK2; X-ray; 1.61 A; A=413-527, A=653-797. DR PDB; 6YK3; X-ray; 1.20 A; A=413-527, A=653-797. DR PDB; 6YK4; X-ray; 1.00 A; A=413-527, A=653-797. DR PDB; 6YK5; X-ray; 1.15 A; A=413-527, A=653-797. DR PDB; 6YK6; X-ray; 1.47 A; A=413-527, A=653-797. DR PDB; 6ZYU; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-797. DR PDB; 7OCA; EM; 3.40 A; B/D=1-860. DR PDB; 7OCC; EM; 3.40 A; B/D=1-860. DR PDB; 7OCD; EM; 3.50 A; B/D=1-860. DR PDB; 7OCE; EM; 3.10 A; B/D=1-860. DR PDB; 7OCF; EM; 3.60 A; B/D=1-860. DR PDB; 7QHB; EM; 3.50 A; B/D=1-860. DR PDB; 7QHH; EM; 3.60 A; B/D=1-860. DR PDB; 7RYY; EM; 4.40 A; A/B/C/D=25-847. DR PDB; 7RYZ; EM; 4.15 A; A/B/C/D=25-847. DR PDB; 7RZ4; EM; 3.60 A; A/B/C/D=25-847. DR PDB; 7RZ5; EM; 3.30 A; A/B/C/D=25-847. DR PDB; 7RZ6; EM; 4.40 A; A/B/C/D=25-847. DR PDB; 7RZ7; EM; 4.20 A; A/B/C/D=25-847. DR PDB; 7RZ8; EM; 4.10 A; A/B/C/D=25-847. DR PDB; 7RZ9; EM; 4.15 A; A/B/C/D=25-847. DR PDB; 7RZA; EM; 4.26 A; A/B/C/D=25-847. DR PDB; 7TNJ; EM; 4.02 A; A/B/C/D=25-847. DR PDB; 7TNK; EM; 4.50 A; A/B/C/D=25-847. DR PDB; 7TNL; EM; 3.59 A; A/B/C/D=25-847. DR PDB; 7TNM; EM; 4.74 A; A/B/C/D=25-847. DR PDB; 7TNN; EM; 3.91 A; A/B/C/D=25-847. DR PDB; 7TNO; EM; 4.02 A; A/B/C/D=25-847. DR PDB; 7TNP; EM; 3.96 A; A/B/C/D=25-847. DR PDB; 8AYL; EM; 3.20 A; B/D=1-860. DR PDB; 8AYM; EM; 3.30 A; B/D=1-860. DR PDB; 8AYN; EM; 2.80 A; B/D=1-860. DR PDB; 8AYO; EM; 3.30 A; B/D=1-860. DR PDB; 8C1R; EM; 3.20 A; A/B/C/D=1-883. DR PDB; 8C1S; EM; 3.00 A; A/B/C/D=1-883. DR PDB; 8P3Q; EM; 2.95 A; A/B/C/D=1-883. DR PDB; 8P3S; EM; 2.95 A; A/B/C/D=1-883. DR PDB; 8P3X; EM; 3.36 A; A/B/C/D=1-883. DR PDB; 8P3Y; EM; 3.55 A; A/B/C/D=1-883. DR PDB; 8P3Z; EM; 3.46 A; A/B/C/D=1-883. DR PDB; 8SS2; EM; 3.58 A; A/B/C/D=25-847. DR PDB; 8SS3; EM; 3.21 A; A/B/C/D=25-847. DR PDB; 8SS4; EM; 3.30 A; A/B/C/D=25-847. DR PDB; 8SS5; EM; 3.56 A; A/B/C/D=25-847. DR PDB; 8SS6; EM; 3.01 A; A/B/C/D=25-847. DR PDB; 8SS7; EM; 2.76 A; A/B/C/D=25-847. DR PDB; 8SS8; EM; 2.81 A; A/B/C/D=25-847. DR PDB; 8SS9; EM; 2.72 A; A/B/C/D=25-847. DR PDB; 8SSA; EM; 3.88 A; A/B/C/D=25-847. DR PDB; 8SSB; EM; 3.66 A; A/B/C/D=25-847. DR PDBsum; 1FTJ; -. DR PDBsum; 1FTK; -. DR PDBsum; 1FTL; -. DR PDBsum; 1FTM; -. DR PDBsum; 1FTO; -. DR PDBsum; 1FW0; -. DR PDBsum; 1GR2; -. DR PDBsum; 1LB8; -. DR PDBsum; 1LB9; -. DR PDBsum; 1LBB; -. DR PDBsum; 1LBC; -. DR PDBsum; 1M5B; -. DR PDBsum; 1M5C; -. DR PDBsum; 1M5D; -. DR PDBsum; 1M5E; -. DR PDBsum; 1M5F; -. DR PDBsum; 1MM6; -. DR PDBsum; 1MM7; -. DR PDBsum; 1MQD; -. DR PDBsum; 1MQG; -. DR PDBsum; 1MQH; -. DR PDBsum; 1MQI; -. DR PDBsum; 1MQJ; -. DR PDBsum; 1MS7; -. DR PDBsum; 1MXU; -. DR PDBsum; 1MXV; -. DR PDBsum; 1MXW; -. DR PDBsum; 1MXX; -. DR PDBsum; 1MXY; -. DR PDBsum; 1MXZ; -. DR PDBsum; 1MY0; -. DR PDBsum; 1MY1; -. DR PDBsum; 1MY2; -. DR PDBsum; 1MY3; -. DR PDBsum; 1MY4; -. DR PDBsum; 1N0T; -. DR PDBsum; 1NNK; -. DR PDBsum; 1NNP; -. DR PDBsum; 1P1N; -. DR PDBsum; 1P1O; -. DR PDBsum; 1P1Q; -. DR PDBsum; 1P1U; -. DR PDBsum; 1P1W; -. DR PDBsum; 1SYH; -. DR PDBsum; 1SYI; -. DR PDBsum; 1WVJ; -. DR PDBsum; 1XHY; -. DR PDBsum; 2AIX; -. DR PDBsum; 2AL4; -. DR PDBsum; 2AL5; -. DR PDBsum; 2ANJ; -. DR PDBsum; 2CMO; -. DR PDBsum; 2GFE; -. DR PDBsum; 2I3V; -. DR PDBsum; 2I3W; -. DR PDBsum; 2P2A; -. DR PDBsum; 2UXA; -. DR PDBsum; 2XX7; -. DR PDBsum; 2XX8; -. DR PDBsum; 2XX9; -. DR PDBsum; 2XXH; -. DR PDBsum; 2XXI; -. DR PDBsum; 3B6Q; -. DR PDBsum; 3B6T; -. DR PDBsum; 3B6W; -. DR PDBsum; 3B7D; -. DR PDBsum; 3BBR; -. DR PDBsum; 3BFT; -. DR PDBsum; 3BFU; -. DR PDBsum; 3BKI; -. DR PDBsum; 3DP6; -. DR PDBsum; 3H03; -. DR PDBsum; 3H06; -. DR PDBsum; 3H5V; -. DR PDBsum; 3H5W; -. DR PDBsum; 3H6T; -. DR PDBsum; 3H6U; -. DR PDBsum; 3H6V; -. DR PDBsum; 3H6W; -. DR PDBsum; 3HSY; -. DR PDBsum; 3IJO; -. DR PDBsum; 3IJX; -. DR PDBsum; 3IK6; -. DR PDBsum; 3IL1; -. DR PDBsum; 3ILT; -. DR PDBsum; 3ILU; -. DR PDBsum; 3KG2; -. DR PDBsum; 3KGC; -. DR PDBsum; 3LSF; -. DR PDBsum; 3LSL; -. DR PDBsum; 3M3L; -. DR PDBsum; 3N6V; -. DR PDBsum; 3O28; -. DR PDBsum; 3O29; -. DR PDBsum; 3O2A; -. DR PDBsum; 3O2J; -. DR PDBsum; 3O6G; -. DR PDBsum; 3O6H; -. DR PDBsum; 3O6I; -. DR PDBsum; 3PD8; -. DR PDBsum; 3PD9; -. DR PDBsum; 3PMV; -. DR PDBsum; 3PMW; -. DR PDBsum; 3PMX; -. DR PDBsum; 3RTF; -. DR PDBsum; 3RTW; -. DR PDBsum; 3T93; -. DR PDBsum; 3T96; -. DR PDBsum; 3T9H; -. DR PDBsum; 3T9U; -. DR PDBsum; 3T9V; -. DR PDBsum; 3T9X; -. DR PDBsum; 3TDJ; -. DR PDBsum; 3TKD; -. DR PDBsum; 3TZA; -. DR PDBsum; 4FAT; -. DR PDBsum; 4G8M; -. DR PDBsum; 4GXS; -. DR PDBsum; 4H8J; -. DR PDBsum; 4IGT; -. DR PDBsum; 4ISU; -. DR PDBsum; 4IY5; -. DR PDBsum; 4IY6; -. DR PDBsum; 4L17; -. DR PDBsum; 4LZ5; -. DR PDBsum; 4LZ7; -. DR PDBsum; 4LZ8; -. DR PDBsum; 4N07; -. DR PDBsum; 4O3A; -. DR PDBsum; 4O3B; -. DR PDBsum; 4O3C; -. DR PDBsum; 4Q30; -. DR PDBsum; 4U1O; -. DR PDBsum; 4U1W; -. DR PDBsum; 4U1X; -. DR PDBsum; 4U1Y; -. DR PDBsum; 4U1Z; -. DR PDBsum; 4U21; -. DR PDBsum; 4U22; -. DR PDBsum; 4U23; -. DR PDBsum; 4U2P; -. DR PDBsum; 4U2Q; -. DR PDBsum; 4U2R; -. DR PDBsum; 4U4F; -. DR PDBsum; 4U4G; -. DR PDBsum; 4U4S; -. DR PDBsum; 4U4X; -. DR PDBsum; 4U5B; -. DR PDBsum; 4U5C; -. DR PDBsum; 4U5D; -. DR PDBsum; 4U5E; -. DR PDBsum; 4U5F; -. DR PDBsum; 4UQ6; -. DR PDBsum; 4UQJ; -. DR PDBsum; 4UQK; -. DR PDBsum; 4X48; -. DR PDBsum; 4YMA; -. DR PDBsum; 4YU0; -. DR PDBsum; 4Z0I; -. DR PDBsum; 5BUU; -. DR PDBsum; 5CBR; -. DR PDBsum; 5CBS; -. DR PDBsum; 5ELV; -. DR PDBsum; 5FHM; -. DR PDBsum; 5FHN; -. DR PDBsum; 5FHO; -. DR PDBsum; 5FTH; -. DR PDBsum; 5FTI; -. DR PDBsum; 5FWX; -. DR PDBsum; 5FWY; -. DR PDBsum; 5IDE; -. DR PDBsum; 5IDF; -. DR PDBsum; 5JEI; -. DR PDBsum; 5KBS; -. DR PDBsum; 5KBT; -. DR PDBsum; 5KBU; -. DR PDBsum; 5KBV; -. DR PDBsum; 5KK2; -. DR PDBsum; 5L1B; -. DR PDBsum; 5L1E; -. DR PDBsum; 5L1F; -. DR PDBsum; 5L1G; -. DR PDBsum; 5L1H; -. DR PDBsum; 5N6P; -. DR PDBsum; 5NG9; -. DR PDBsum; 5NIH; -. DR PDBsum; 5NS9; -. DR PDBsum; 5O9A; -. DR PDBsum; 5OEW; -. DR PDBsum; 5VHW; -. DR PDBsum; 5VHX; -. DR PDBsum; 5VHY; -. DR PDBsum; 5VHZ; -. DR PDBsum; 5VOT; -. DR PDBsum; 5VOU; -. DR PDBsum; 5VOV; -. DR PDBsum; 5WEK; -. DR PDBsum; 5WEL; -. DR PDBsum; 5WEM; -. DR PDBsum; 5WEN; -. DR PDBsum; 5WEO; -. DR PDBsum; 6DLZ; -. DR PDBsum; 6DM0; -. DR PDBsum; 6DM1; -. DR PDBsum; 6FAZ; -. DR PDBsum; 6FQG; -. DR PDBsum; 6FQH; -. DR PDBsum; 6FQI; -. DR PDBsum; 6FQJ; -. DR PDBsum; 6FQK; -. DR PDBsum; 6GIV; -. DR PDBsum; 6GL4; -. DR PDBsum; 6HC9; -. DR PDBsum; 6HCA; -. DR PDBsum; 6HCB; -. DR PDBsum; 6HCC; -. DR PDBsum; 6HCH; -. DR PDBsum; 6NJL; -. DR PDBsum; 6NJM; -. DR PDBsum; 6NJN; -. DR PDBsum; 6O9G; -. DR PDBsum; 6PEQ; -. DR PDBsum; 6Q54; -. DR PDBsum; 6Q60; -. DR PDBsum; 6QKC; -. DR PDBsum; 6QKZ; -. DR PDBsum; 6RUQ; -. DR PDBsum; 6U5S; -. DR PDBsum; 6U6I; -. DR PDBsum; 6UCB; -. DR PDBsum; 6UD4; -. DR PDBsum; 6UD8; -. DR PDBsum; 6XSR; -. DR PDBsum; 6YK2; -. DR PDBsum; 6YK3; -. DR PDBsum; 6YK4; -. DR PDBsum; 6YK5; -. DR PDBsum; 6YK6; -. DR PDBsum; 6ZYU; -. DR PDBsum; 7OCA; -. DR PDBsum; 7OCC; -. DR PDBsum; 7OCD; -. DR PDBsum; 7OCE; -. DR PDBsum; 7OCF; -. DR PDBsum; 7QHB; -. DR PDBsum; 7QHH; -. DR PDBsum; 7RYY; -. DR PDBsum; 7RYZ; -. DR PDBsum; 7RZ4; -. DR PDBsum; 7RZ5; -. DR PDBsum; 7RZ6; -. DR PDBsum; 7RZ7; -. DR PDBsum; 7RZ8; -. DR PDBsum; 7RZ9; -. DR PDBsum; 7RZA; -. DR PDBsum; 7TNJ; -. DR PDBsum; 7TNK; -. DR PDBsum; 7TNL; -. DR PDBsum; 7TNM; -. DR PDBsum; 7TNN; -. DR PDBsum; 7TNO; -. DR PDBsum; 7TNP; -. DR PDBsum; 8AYL; -. DR PDBsum; 8AYM; -. DR PDBsum; 8AYN; -. DR PDBsum; 8AYO; -. DR PDBsum; 8C1R; -. DR PDBsum; 8C1S; -. DR PDBsum; 8P3Q; -. DR PDBsum; 8P3S; -. DR PDBsum; 8P3X; -. DR PDBsum; 8P3Y; -. DR PDBsum; 8P3Z; -. DR PDBsum; 8SS2; -. DR PDBsum; 8SS3; -. DR PDBsum; 8SS4; -. DR PDBsum; 8SS5; -. DR PDBsum; 8SS6; -. DR PDBsum; 8SS7; -. DR PDBsum; 8SS8; -. DR PDBsum; 8SS9; -. DR PDBsum; 8SSA; -. DR PDBsum; 8SSB; -. DR AlphaFoldDB; P19491; -. DR EMDB; EMD-12802; -. DR EMDB; EMD-12803; -. DR EMDB; EMD-12804; -. DR EMDB; EMD-12805; -. DR EMDB; EMD-12806; -. DR EMDB; EMD-13969; -. DR EMDB; EMD-13970; -. DR EMDB; EMD-13971; -. DR EMDB; EMD-13972; -. DR EMDB; EMD-13973; -. DR EMDB; EMD-13974; -. DR EMDB; EMD-15714; -. DR EMDB; EMD-15716; -. DR EMDB; EMD-15717; -. DR EMDB; EMD-15718; -. DR EMDB; EMD-16381; -. DR EMDB; EMD-16382; -. DR EMDB; EMD-17392; -. DR EMDB; EMD-17393; -. DR EMDB; EMD-17398; -. DR EMDB; EMD-17399; -. DR EMDB; EMD-17400; -. DR EMDB; EMD-20330; -. DR EMDB; EMD-20654; -. DR EMDB; EMD-20666; -. DR EMDB; EMD-20727; -. DR EMDB; EMD-20733; -. DR EMDB; EMD-20734; -. DR EMDB; EMD-24748; -. DR EMDB; EMD-24749; -. DR EMDB; EMD-24750; -. DR EMDB; EMD-24751; -. DR EMDB; EMD-24752; -. DR EMDB; EMD-24753; -. DR EMDB; EMD-24754; -. DR EMDB; EMD-24755; -. DR EMDB; EMD-24756; -. DR EMDB; EMD-2680; -. DR EMDB; EMD-2684; -. DR EMDB; EMD-2686; -. DR EMDB; EMD-2687; -. DR EMDB; EMD-2688; -. DR EMDB; EMD-2689; -. DR EMDB; EMD-4572; -. DR EMDB; EMD-4575; -. DR EMDB; EMD-8090; -. DR EMDB; EMD-8091; -. DR EMDB; EMD-8232; -. DR EMDB; EMD-8256; -. DR EMDB; EMD-8721; -. DR EMDB; EMD-8722; -. DR EMDB; EMD-8723; -. DR EMDB; EMD-9387; -. DR EMDB; EMD-9388; -. DR EMDB; EMD-9389; -. DR SASBDB; P19491; -. DR SMR; P19491; -. DR BioGRID; 248250; 12. DR CORUM; P19491; -. DR DIP; DIP-30952N; -. DR ELM; P19491; -. DR IntAct; P19491; 31. DR MINT; P19491; -. DR STRING; 10116.ENSRNOP00000069094; -. DR BindingDB; P19491; -. DR ChEMBL; CHEMBL3503; -. DR DrugCentral; P19491; -. DR GuidetoPHARMACOLOGY; 445; -. DR GlyCosmos; P19491; 4 sites, No reported glycans. DR GlyGen; P19491; 5 sites, 1 O-linked glycan (1 site). DR iPTMnet; P19491; -. DR PhosphoSitePlus; P19491; -. DR SwissPalm; P19491; -. DR PaxDb; 10116-ENSRNOP00000032937; -. DR ABCD; P19491; 2 sequenced antibodies. DR GeneID; 29627; -. DR KEGG; rno:29627; -. DR UCSC; RGD:61862; rat. [P19491-1] DR AGR; RGD:61862; -. DR CTD; 2891; -. DR RGD; 61862; Gria2. DR eggNOG; KOG1054; Eukaryota. DR InParanoid; P19491; -. DR OrthoDB; 511851at2759; -. DR PhylomeDB; P19491; -. DR Reactome; R-RNO-399710; Activation of AMPA receptors. DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors. DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR EvolutionaryTrace; P19491; -. DR PRO; PR:P19491; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB. DR GO; GO:0032279; C:asymmetric synapse; IDA:ARUK-UCL. DR GO; GO:0030424; C:axon; IDA:RGD. DR GO; GO:0009986; C:cell surface; IDA:RGD. DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL. DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD. DR GO; GO:0032590; C:dendrite membrane; IDA:RGD. DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB. DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB. DR GO; GO:0044327; C:dendritic spine head; IDA:RGD. DR GO; GO:0044326; C:dendritic spine neck; IDA:RGD. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0030426; C:growth cone; IDA:RGD. DR GO; GO:0008328; C:ionotropic glutamate receptor complex; TAS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB. DR GO; GO:0043204; C:perikaryon; IDA:RGD. DR GO; GO:0099544; C:perisynaptic space; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IDA:ARUK-UCL. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO. DR GO; GO:0098793; C:presynapse; IDA:RGD. DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO. DR GO; GO:0036477; C:somatodendritic compartment; ISO:RGD. DR GO; GO:0106033; C:spine synapse; IDA:RGD. DR GO; GO:0045202; C:synapse; IDA:UniProtKB. DR GO; GO:0097060; C:synaptic membrane; ISO:RGD. DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD. DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD. DR GO; GO:0043195; C:terminal bouton; IDA:RGD. DR GO; GO:0004971; F:AMPA glutamate receptor activity; IDA:UniProtKB. DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL. DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD. DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISO:RGD. DR GO; GO:0035254; F:glutamate receptor binding; IPI:UniProtKB. DR GO; GO:0004970; F:glutamate-gated receptor activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019865; F:immunoglobulin binding; IPI:UniProtKB. DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD. DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:UniProtKB. DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO. DR GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:RGD. DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD. DR GO; GO:0097110; F:scaffold protein binding; IPI:RGD. DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB. DR GO; GO:0000149; F:SNARE binding; IPI:UniProtKB. DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO. DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IDA:RGD. DR GO; GO:1905430; P:cellular response to glycine; IDA:RGD. DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD. DR GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD. DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB. DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB. DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB. DR GO; GO:0001919; P:regulation of receptor recycling; IMP:UniProtKB. DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:UniProtKB. DR GO; GO:0060992; P:response to fungicide; IEP:RGD. DR GO; GO:0010226; P:response to lithium ion; IEP:UniProtKB. DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central. DR CDD; cd06389; PBP1_iGluR_AMPA_GluR2; 1. DR CDD; cd13715; PBP2_iGluR_AMPA; 1. DR Gene3D; 1.10.287.70; -; 2. DR Gene3D; 3.40.50.2300; -; 2. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR InterPro; IPR001828; ANF_lig-bd_rcpt. DR InterPro; IPR019594; Glu/Gly-bd. DR InterPro; IPR001508; Iono_Glu_rcpt_met. DR InterPro; IPR015683; Ionotropic_Glu_rcpt. DR InterPro; IPR001320; Iontro_rcpt_C. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR PANTHER; PTHR18966:SF99; GLUTAMATE RECEPTOR 2; 1. DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00060; Lig_chan; 1. DR Pfam; PF10613; Lig_chan-Glu_bd; 1. DR Pfam; PF00497; SBP_bac_3; 1. DR PRINTS; PR00177; NMDARECEPTOR. DR SMART; SM00918; Lig_chan-Glu_bd; 1. DR SMART; SM00079; PBPe; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport; KW Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing; KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport; KW Ubl conjugation. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..883 FT /note="Glutamate receptor 2" FT /id="PRO_0000011535" FT TOPO_DOM 22..543 FT /note="Extracellular" FT TRANSMEM 544..564 FT /note="Helical" FT TOPO_DOM 565..591 FT /note="Cytoplasmic" FT INTRAMEM 592..607 FT /note="Helical; Pore-forming" FT INTRAMEM 608..610 FT TOPO_DOM 611..616 FT /note="Cytoplasmic" FT TRANSMEM 617..637 FT /note="Helical" FT TOPO_DOM 638..812 FT /note="Extracellular" FT TRANSMEM 813..833 FT /note="Helical; Name=M4" FT TOPO_DOM 834..883 FT /note="Cytoplasmic" FT REGION 867..877 FT /note="Required for interaction with IQSEC1" FT /evidence="ECO:0000269|PubMed:20547133" FT BINDING 471 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16483599" FT BINDING 499..501 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 501 FT /ligand="kainate" FT /ligand_id="ChEBI:CHEBI:156548" FT /evidence="ECO:0000269|PubMed:25103405" FT BINDING 506 FT /ligand="kainate" FT /ligand_id="ChEBI:CHEBI:156548" FT /evidence="ECO:0000269|PubMed:25103405" FT BINDING 506 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16483599" FT BINDING 675..676 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT BINDING 675 FT /ligand="kainate" FT /ligand_id="ChEBI:CHEBI:156548" FT /evidence="ECO:0000269|PubMed:25103405" FT BINDING 676 FT /ligand="kainate" FT /ligand_id="ChEBI:CHEBI:156548" FT /evidence="ECO:0000269|PubMed:25103405" FT BINDING 726 FT /ligand="kainate" FT /ligand_id="ChEBI:CHEBI:156548" FT /evidence="ECO:0000269|PubMed:25103405" FT BINDING 726 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000269|PubMed:16483599" FT SITE 474 FT /note="Interaction with the cone snail toxin Con-ikot-ikot" FT /evidence="ECO:0000269|PubMed:25103405" FT SITE 654 FT /note="Crucial to convey clamshell closure to channel FT opening" FT /evidence="ECO:0000269|PubMed:25103405" FT SITE 681 FT /note="Interaction with the cone snail toxin Con-ikot-ikot" FT /evidence="ECO:0000269|PubMed:25103405" FT SITE 773 FT /note="Interaction with the cone snail toxin Con-ikot-ikot" FT /evidence="ECO:0000269|PubMed:25103405" FT MOD_RES 683 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:8848293" FT MOD_RES 717 FT /note="Phosphoserine; by PKG" FT /evidence="ECO:0000269|PubMed:8848293" FT MOD_RES 860 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23819" FT MOD_RES 863 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23819" FT MOD_RES 876 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:15240807, FT ECO:0000269|PubMed:20547133" FT MOD_RES 880 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23819" FT LIPID 610 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 836 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 256 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21317873" FT CARBOHYD 370 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19946266, FT ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405" FT CARBOHYD 406 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 413 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 78..330 FT DISULFID 739..794 FT VAR_SEQ 765..766 FT /note="NA -> TP (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699567, FT ECO:0000303|PubMed:2166337, ECO:0000303|PubMed:9351977" FT /id="VSP_000111" FT VAR_SEQ 775 FT /note="N -> S (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699567, FT ECO:0000303|PubMed:2166337, ECO:0000303|PubMed:9351977" FT /id="VSP_000112" FT VAR_SEQ 779 FT /note="L -> V (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699567, FT ECO:0000303|PubMed:2166337, ECO:0000303|PubMed:9351977" FT /id="VSP_000113" FT VAR_SEQ 796..800 FT /note="SGGGD -> AKDSG (in isoform Flip)" FT /evidence="ECO:0000303|PubMed:1699567, FT ECO:0000303|PubMed:2166337, ECO:0000303|PubMed:9351977" FT /id="VSP_000114" FT VAR_SEQ 848..883 FT /note="VAKNPQNINPSSSQNSQNFATYKEGYNVYGIESVKI -> MTLSDVMRSKAR FT LSITGSTGENGRVMTPEFPKAVHAVPYVSPGMGMNVSVTDLS (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_029310" FT VARIANT 607 FT /note="Q -> R (in RNA edited version)" FT MUTAGEN 504 FT /note="L->Y: Promotes dimerization. Strongly reduced FT desensitization." FT /evidence="ECO:0000269|PubMed:12015593" FT MUTAGEN 775 FT /note="N->D: Increases rate of desensitization." FT /evidence="ECO:0000269|PubMed:12015593" FT MUTAGEN 851..852 FT /note="NP->AA: Strongly reduces interaction with NSF." FT /evidence="ECO:0000269|PubMed:9697855" FT MUTAGEN 875 FT /note="V->Y: Almost abolishes interaction with IQSEC1; when FT associated with V-876. Abolishes activation of ARF6 by FT IQSEC1; when associated with V-876." FT /evidence="ECO:0000269|PubMed:20547133" FT MUTAGEN 876 FT /note="Y->A: Strongly decreases interaction with IQSEC1. FT Abolishes activation of ARF6 by IQSEC1." FT /evidence="ECO:0000269|PubMed:20547133" FT MUTAGEN 876 FT /note="Y->F: No effect on interaction with IQSEC1." FT /evidence="ECO:0000269|PubMed:20547133" FT MUTAGEN 876 FT /note="Y->V: Almost abolishes interaction with IQSEC1; when FT associated with Y-875. Abolishes activation of ARF6 by FT IQSEC1; when associated with Y-875." FT /evidence="ECO:0000269|PubMed:20547133" FT STRAND 26..34 FT /evidence="ECO:0007829|PDB:3HSY" FT HELIX 38..50 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 57..65 FT /evidence="ECO:0007829|PDB:3HSY" FT HELIX 70..82 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 86..90 FT /evidence="ECO:0007829|PDB:3HSY" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:3HSY" FT HELIX 97..107 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:3HSY" FT HELIX 133..142 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:3HSY" FT TURN 154..156 FT /evidence="ECO:0007829|PDB:5FWY" FT HELIX 159..171 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 174..179 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 182..185 FT /evidence="ECO:0007829|PDB:3O2J" FT HELIX 188..199 FT /evidence="ECO:0007829|PDB:3HSY" FT TURN 201..203 FT /evidence="ECO:0007829|PDB:3H5V" FT STRAND 206..211 FT /evidence="ECO:0007829|PDB:3HSY" FT HELIX 213..226 FT /evidence="ECO:0007829|PDB:3HSY" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:6U5S" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 234..237 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:3HSY" FT HELIX 242..244 FT /evidence="ECO:0007829|PDB:5FWY" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:5FWY" FT STRAND 256..262 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:8SS6" FT HELIX 268..277 FT /evidence="ECO:0007829|PDB:3HSY" FT TURN 282..284 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:5FWY" FT HELIX 295..316 FT /evidence="ECO:0007829|PDB:3HSY" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:5N6P" FT HELIX 339..350 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 372..379 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 382..390 FT /evidence="ECO:0007829|PDB:3HSY" FT TURN 391..393 FT /evidence="ECO:0007829|PDB:3HSY" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:3HSY" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:8SS6" FT STRAND 416..420 FT /evidence="ECO:0007829|PDB:6YK4" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 433..435 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 438..441 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 442..444 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 445..457 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 461..465 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 467..469 FT /evidence="ECO:0007829|PDB:4U2P" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:2CMO" FT TURN 476..478 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 479..481 FT /evidence="ECO:0007829|PDB:6FQI" FT HELIX 483..489 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 504..507 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 510..512 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 516..519 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 521..526 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 537..539 FT /evidence="ECO:0007829|PDB:8SS9" FT STRAND 540..542 FT /evidence="ECO:0007829|PDB:6UCB" FT HELIX 544..566 FT /evidence="ECO:0007829|PDB:8SS9" FT HELIX 569..571 FT /evidence="ECO:0007829|PDB:8P3Q" FT STRAND 589..592 FT /evidence="ECO:0007829|PDB:7OCE" FT HELIX 594..605 FT /evidence="ECO:0007829|PDB:8SS9" FT HELIX 617..649 FT /evidence="ECO:0007829|PDB:8SS9" FT HELIX 653..655 FT /evidence="ECO:0007829|PDB:4U1W" FT HELIX 657..661 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 664..669 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 671..674 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 675..682 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 686..697 FT /evidence="ECO:0007829|PDB:6YK4" FT TURN 699..701 FT /evidence="ECO:0007829|PDB:8AYO" FT STRAND 704..706 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 707..716 FT /evidence="ECO:0007829|PDB:6YK4" FT TURN 717..719 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 720..726 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 727..734 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 736..738 FT /evidence="ECO:0007829|PDB:4YU0" FT STRAND 741..745 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 751..753 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 756..758 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 763..776 FT /evidence="ECO:0007829|PDB:6YK4" FT HELIX 779..788 FT /evidence="ECO:0007829|PDB:6YK4" FT TURN 789..791 FT /evidence="ECO:0007829|PDB:6YK4" FT STRAND 793..795 FT /evidence="ECO:0007829|PDB:6UD8" FT STRAND 800..803 FT /evidence="ECO:0007829|PDB:4U2P" FT TURN 810..812 FT /evidence="ECO:0007829|PDB:8SS9" FT HELIX 814..840 FT /evidence="ECO:0007829|PDB:8SS9" SQ SEQUENCE 883 AA; 98688 MW; DEFA817027C1CCD1 CRC64; MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI //