GRIA2_RAT
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 03-AUG-2022, entry version 236.
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 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}.
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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 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 AlphaFoldDB; P19491; -.
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.ENSRNOP00000032937; -.
DR BindingDB; P19491; -.
DR ChEMBL; CHEMBL3503; -.
DR DrugCentral; P19491; -.
DR GuidetoPHARMACOLOGY; 445; -.
DR GlyGen; P19491; 4 sites.
DR iPTMnet; P19491; -.
DR PhosphoSitePlus; P19491; -.
DR SwissPalm; P19491; -.
DR PaxDb; P19491; -.
DR PRIDE; P19491; -.
DR ABCD; P19491; 2 sequenced antibodies.
DR GeneID; 29627; -.
DR KEGG; rno:29627; -.
DR UCSC; RGD:61862; rat. [P19491-1]
DR CTD; 2891; -.
DR RGD; 61862; Gria2.
DR eggNOG; KOG1054; Eukaryota.
DR InParanoid; P19491; -.
DR OrthoDB; 188544at2759; -.
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:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032279; C:asymmetric synapse; IDA:ARUK-UCL.
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:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
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:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
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; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:ARUK-UCL.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
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: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:0051117; F:ATPase binding; IPI:UniProtKB.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019865; F:immunoglobulin binding; IPI:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase 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 ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
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: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 InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 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:4U1X"
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 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:6PEQ"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:6UCB"
FT HELIX 544..567
FT /evidence="ECO:0007829|PDB:6PEQ"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 594..605
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 617..649
FT /evidence="ECO:0007829|PDB:6PEQ"
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 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 HELIX 810..812
FT /evidence="ECO:0007829|PDB:6PEQ"
FT HELIX 814..843
FT /evidence="ECO:0007829|PDB:6PEQ"
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
