Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Glutamate receptor 2 (GluR-2) (AMPA-selective glutamate receptor 2) (GluR-B) (GluR-K2) (Glutamate receptor ionotropic, AMPA 2) (GluA2)

 GRIA2_RAT               Reviewed;         883 AA.
P19491; Q9R174;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
10-OCT-2018, entry version 211.
RecName: Full=Glutamate receptor 2 {ECO:0000305};
Short=GluR-2;
AltName: Full=AMPA-selective glutamate receptor 2;
AltName: Full=GluR-B;
AltName: Full=GluR-K2;
AltName: Full=Glutamate receptor ionotropic, AMPA 2;
Short=GluA2 {ECO:0000303|PubMed:27756895};
Flags: Precursor;
Name=Gria2 {ECO:0000312|RGD:61862}; Synonyms=Glur2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP).
TISSUE=Brain;
PubMed=2166337; DOI=10.1126/science.2166337;
Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A.,
Sakmann B., Seeburg P.H.;
"A family of AMPA-selective glutamate receptors.";
Science 249:556-560(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
PubMed=2168579; DOI=10.1126/science.2168579;
Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M.,
Deneris E.S., Maron C., Heinemann S.F.;
"Molecular cloning and functional expression of glutamate receptor
subunit genes.";
Science 249:1033-1037(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP).
TISSUE=Brain cortex, and Hippocampus;
PubMed=1699567; DOI=10.1016/0896-6273(90)90212-X;
Nakanishi N., Schneider N.A., Axel R.;
"A family of glutamate receptor genes: evidence for the formation of
heteromultimeric receptors with distinct channel properties.";
Neuron 5:569-581(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), AND FUNCTION.
STRAIN=Sprague-Dawley;
PubMed=9351977; DOI=10.1124/mol.52.5.861;
Everts I., Villmann C., Hollmann M.;
"N-glycosylation is not a prerequisite for glutamate receptor function
but is essential for lectin modulation.";
Mol. Pharmacol. 52:861-873(1997).
[5]
RNA EDITING OF POSITION 607.
PubMed=1717158; DOI=10.1016/0092-8674(91)90568-J;
Sommer B., Koehler M., Sprengel R., Seeburg P.H.;
"RNA editing in brain controls a determinant of ion flow in glutamate-
gated channels.";
Cell 67:11-19(1991).
[6]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NSF,
IDENTIFICATION IN A COMPLEX WITH NSF; NAPA AND NAPB, AND MUTAGENESIS
OF 851-ASN-PRO-852.
PubMed=9697855; DOI=10.1016/S0896-6273(00)80518-8;
Osten P., Srivastava S., Inman G.J., Vilim F.S., Khatri L., Lee L.M.,
States B.A., Einheber S., Milner T.A., Hanson P.I., Ziff E.B.;
"The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-
dependent interaction with NSF and alpha- and beta-SNAPs.";
Neuron 21:99-110(1998).
[7]
INTERACTION WITH PRKCABP.
PubMed=10027300; DOI=10.1016/S0896-6273(00)80689-3;
Xia J., Zhang X., Staudinger J., Huganir R.L.;
"Clustering of AMPA receptors by the synaptic PDZ domain-containing
protein PICK1.";
Neuron 22:179-187(1999).
[8]
ALTERNATIVE SPLICING (ISOFORMS FLIP AND FLOP).
PubMed=1699275; DOI=10.1126/science.1699275;
Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N.,
Herb A., Koehler M., Takagi T., Sakmann B., Seeburg P.H.;
"Flip and flop: a cell-specific functional switch in glutamate-
operated channels of the CNS.";
Science 249:1580-1585(1990).
[9]
PHOSPHORYLATION AT SER-683 AND SER-717.
PubMed=8848293; DOI=10.1016/0168-0102(95)00977-9;
Nakazawa K., Tadakuma T., Nokihara K., Ito M.;
"Antibody specific for phosphorylated AMPA-type glutamate receptors at
GluR2 Ser-696.";
Neurosci. Res. 24:75-86(1995).
[10]
INTERACTION WITH GRIP1.
TISSUE=Hippocampus;
PubMed=9069286; DOI=10.1038/386279a0;
Dong H., O'Brien R.J., Fung E.T., Lanahan A.A., Worley P.F.,
Huganir R.L.;
"GRIP: a synaptic PDZ domain-containing protein that interacts with
AMPA receptors.";
Nature 386:279-284(1997).
[11]
INTERACTION WITH GRIP2.
PubMed=10414981;
Wyszynski M., Valtschanoff J.G., Naisbitt S., Dunah A.W., Kim E.,
Standaert D.G., Weinberg R., Sheng M.;
"Association of AMPA receptors with a subset of glutamate receptor-
interacting protein in vivo.";
J. Neurosci. 19:6528-6537(1999).
[12]
IDENTIFICATION OF ISOFORM 3, SUBCELLULAR LOCATION, DEVELOPMENTAL
STAGE, AND TISSUE SPECIFICITY.
PubMed=14687553; DOI=10.1016/S0896-6273(03)00722-0;
Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T.,
Koehr G., Malinow R., Seeburg P.H., Osten P.;
"Glutamatergic plasticity by synaptic delivery of GluR-B(long)-
containing AMPA receptors.";
Neuron 40:1199-1212(2003).
[13]
PHOSPHORYLATION AT TYR-876, AND TISSUE SPECIFICITY.
PubMed=15240807; DOI=10.1523/JNEUROSCI.0799-04.2004;
Hayashi T., Huganir R.L.;
"Tyrosine phosphorylation and regulation of the AMPA receptor by SRC
family tyrosine kinases.";
J. Neurosci. 24:6152-6160(2004).
[14]
COMPLEX FORMATION WITH GRIP1; NGS1 AND STX12, AND FUNCTION.
PubMed=16037816; DOI=10.1038/sj.emboj.7600755;
Steiner P., Alberi S., Kulangara K., Yersin A., Sarria J.C.,
Regulier E., Kasas S., Dietler G., Muller D., Catsicas S., Hirling H.;
"Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and
recycling of the glutamate receptor subunit GluR2.";
EMBO J. 24:2873-2884(2005).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH CACNG2.
PubMed=16793768; DOI=10.1074/jbc.M600679200;
Bedoukian M.A., Weeks A.M., Partin K.M.;
"Different domains of the AMPA receptor direct stargazin-mediated
trafficking and stargazin-mediated modulation of kinetics.";
J. Biol. Chem. 281:23908-23921(2006).
[16]
INTERACTION WITH LRFN1.
PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H.,
Kaang B.-K., Kim E.;
"SALM synaptic cell adhesion-like molecules regulate the
differentiation of excitatory synapses.";
Neuron 50:233-245(2006).
[17]
INTERACTION WITH CACNG5.
PubMed=18817736; DOI=10.1016/j.neuron.2008.07.034;
Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.;
"AMPA receptor subunit-specific regulation by a distinct family of
type II TARPs.";
Neuron 59:986-996(2008).
[18]
INTERACTION WITH CACNG5.
PubMed=19234459; DOI=10.1038/nn.2266;
Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M.,
Cull-Candy S.G.;
"Selective regulation of long-form calcium-permeable AMPA receptors by
an atypical TARP, gamma-5.";
Nat. Neurosci. 12:277-285(2009).
[19]
ERRATUM.
DOI=10.1038/nn0609-808c;
Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M.,
Cull-Candy S.G.;
Nat. Neurosci. 12:808-808(2009).
[20]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=19265014; DOI=10.1126/science.1167852;
Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B.,
Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.;
"Functional proteomics identify cornichon proteins as auxiliary
subunits of AMPA receptors.";
Science 323:1313-1319(2009).
[21]
FUNCTION.
PubMed=21172611; DOI=10.1016/j.neuron.2010.11.026;
Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H.,
Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.;
"Hippocampal AMPA receptor gating controlled by both TARP and
cornichon proteins.";
Neuron 68:1082-1096(2010).
[22]
INTERACTION WITH ATAD1 AND GRIP1.
PubMed=21496646; DOI=10.1016/j.cell.2011.03.016;
Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H.,
Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P.,
Dawson T.M., Dawson V.L.;
"The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic
plasticity and behavior.";
Cell 145:284-299(2011).
[23]
INTERACTION WITH CACNG2.
PubMed=27756895; DOI=10.1038/srep35283;
Rademacher N., Schmerl B., Lardong J.A., Wahl M.C., Shoichet S.A.;
"MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell
adhesion molecules to core components of the postsynaptic density.";
Sci. Rep. 6:35283-35283(2016).
[24]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 404-796 IN COMPLEX WITH
KAINATE.
PubMed=9804426; DOI=10.1038/27692;
Armstrong N., Sun Y., Chen G.Q., Gouaux E.;
"Structure of a glutamate-receptor ligand-binding core in complex with
kainate.";
Nature 395:913-917(1998).
[25]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 413-796 IN COMPLEXES WITH
GLUTAMATE; AMPA; KAINATE; DNQX AND ZINC.
PubMed=11086992; DOI=10.1016/S0896-6273(00)00094-5;
Armstrong N., Gouaux E.;
"Mechanisms for activation and antagonism of an AMPA-sensitive
glutamate receptor: crystal structures of the GluR2 ligand binding
core.";
Neuron 28:165-181(2000).
[26]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH
QUISQUALATE, AND FUNCTION.
PubMed=12501192; DOI=10.1021/bi020583k;
Jin R., Horning M., Mayer M.L., Gouaux E.;
"Mechanism of activation and selectivity in a ligand-gated ion
channel: structural and functional studies of GluR2 and quisqualate.";
Biochemistry 41:15635-15643(2002).
[27]
X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 413-796 IN COMPLEXES WITH
ACPA AND BR-HIBO.
PubMed=12215417; DOI=10.1016/S0022-2836(02)00650-2;
Hogner A., Kastrup J.S., Jin R., Liljefors T., Mayer M.L.,
Egebjerg J., Larsen I.K., Gouaux E.;
"Structural basis for AMPA receptor activation and ligand selectivity:
crystal structures of five agonist complexes with the GluR2 ligand-
binding core.";
J. Mol. Biol. 322:93-109(2002).
[28]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 413-796 IN COMPLEXES WITH
AMPA; DNQX AND KAINATE, FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-504
AND ASN-775.
PubMed=12015593; DOI=10.1038/417245a;
Sun Y., Olson R., Horning M., Armstrong N., Mayer M., Gouaux E.;
"Mechanism of glutamate receptor desensitization.";
Nature 417:245-253(2002).
[29]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 413-796 IN COMPLEXES WITH
ATPA AND ZINC IONS.
PubMed=12593667; DOI=10.1021/jm021020+;
Lunn M.-L., Hogner A., Stensboel T.B., Gouaux E., Egebjerg J.,
Kastrup J.S.;
"Three-dimensional structure of the ligand-binding core of GluR2 in
complex with the agonist (S)-ATPA: implications for receptor subunit
selectivity.";
J. Med. Chem. 46:872-875(2003).
[30]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 413-796 IN COMPLEXES WITH
WILLARDIINES, AND FUNCTION.
PubMed=12872125; DOI=10.1038/nn1091;
Jin R., Banke T.G., Mayer M.L., Traynelis S.F., Gouaux E.;
"Structural basis for partial agonist action at ionotropic glutamate
receptors.";
Nat. Neurosci. 6:803-810(2003).
[31]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 413-796 IN COMPLEXES WITH
AMPA; KAINATE AND QUISQUALATE, AND FUNCTION.
PubMed=12730367; DOI=10.1073/pnas.1037393100;
Armstrong N., Mayer M., Gouaux E.;
"Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic
adjustment of agonist-induced conformational changes.";
Proc. Natl. Acad. Sci. U.S.A. 100:5736-5741(2003).
[32]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 413-796 IN COMPLEXES WITH
ANIRACETAM AND CX614, AND FUNCTION.
PubMed=16192394; DOI=10.1523/JNEUROSCI.2567-05.2005;
Jin R., Clark S., Weeks A.M., Dudman J.T., Gouaux E., Partin K.M.;
"Mechanism of positive allosteric modulators acting on AMPA
receptors.";
J. Neurosci. 25:9027-9036(2005).
[33]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-796 IN COMPLEXES WITH
CPW399 AND KAINATE, AND FUNCTION.
PubMed=15591246; DOI=10.1124/mol.104.002931;
Frandsen A., Pickering D.S., Vestergaard B., Kasper C., Nielsen B.B.,
Greenwood J.R., Campiani G., Fattorusso C., Gajhede M., Schousboe A.,
Kastrup J.S.;
"Tyr702 is an important determinant of agonist binding and domain
closure of the ligand-binding core of GluR2.";
Mol. Pharmacol. 67:703-713(2005).
[34]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 413-794, FUNCTION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17018279; DOI=10.1016/j.cell.2006.08.037;
Armstrong N., Jasti J., Beich-Frandsen M., Gouaux E.;
"Measurement of conformational changes accompanying desensitization in
an ionotropic glutamate receptor.";
Cell 127:85-97(2006).
[35]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 413-796 IN COMPLEX WITH
GLUTAMATE AND S1209, AND FUNCTION.
PubMed=16483599; DOI=10.1016/j.jmb.2006.01.024;
Kasper C., Pickering D.S., Mirza O., Olsen L., Kristensen A.S.,
Greenwood J.R., Liljefors T., Schousboe A., Waetjen F., Gajhede M.,
Sigurskjold B.W., Kastrup J.S.;
"The structure of a mixed GluR2 ligand-binding core dimer in complex
with (S)-glutamate and the antagonist (S)-NS1209.";
J. Mol. Biol. 357:1184-1201(2006).
[36]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 25-847 IN COMPLEX WITH
GLUTAMATE ANALOG, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 413-796,
FUNCTION, SUBUNIT, MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-370.
PubMed=19946266; DOI=10.1038/nature08624;
Sobolevsky A.I., Rosconi M.P., Gouaux E.;
"X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate
receptor.";
Nature 462:745-756(2009).
[37]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 25-400, FUNCTION, SUBUNIT,
DISULFIDE BOND, AND GLYCOSYLATION AT ASN-256 AND ASN-370.
PubMed=21317873; DOI=10.1038/emboj.2011.16;
Rossmann M., Sukumaran M., Penn A.C., Veprintsev D.B., Babu M.M.,
Greger I.H.;
"Subunit-selective N-terminal domain associations organize the
formation of AMPA receptor heteromers.";
EMBO J. 30:959-971(2011).
[38]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 414-794 IN COMPLEXES WITH
GLUTAMATE; IODOWILLARDIINE AND KAINATE, FUNCTION, AND DISULFIDE BONDS.
PubMed=21846932; DOI=10.1074/jbc.M111.269001;
Ahmed A.H., Wang S., Chuang H.H., Oswald R.E.;
"Mechanism of AMPA receptor activation by partial agonists: disulfide
trapping of closed lobe conformations.";
J. Biol. Chem. 286:35257-35266(2011).
[39]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 25-850 IN COMPLEXES WITH
KAINATE; FLUORAWILLARDINE AND THE CONE SNAIL TOXIN CON-IKOT-IKOT,
DISULFIDE BOND, GLYCOSYLATION AT ASN-370, AND SITES ARG-474; ILE-654;
ARG-681 AND LYS-773.
PubMed=25103405; DOI=10.1126/science.1258409;
Chen L., Durr K.L., Gouaux E.;
"X-ray structures of AMPA receptor-cone snail toxin complexes
illuminate activation mechanism.";
Science 345:1021-1026(2014).
-!- FUNCTION: Receptor for glutamate that functions as ligand-gated
ion channel in the central nervous system and plays an important
role in excitatory synaptic transmission. L-glutamate acts as an
excitatory neurotransmitter at many synapses in the central
nervous system. Binding of the excitatory neurotransmitter L-
glutamate induces a conformation change, leading to the opening of
the cation channel, and thereby converts the chemical signal to an
electrical impulse. The receptor then desensitizes rapidly and
enters a transient inactive state, characterized by the presence
of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8,
shows resensitization which is characterized by a delayed
accumulation of current flux upon continued application of
glutamate. Through complex formation with NSG1, GRIP1 and STX12
controls the intracellular fate of AMPAR and the endosomal sorting
of the GRIA2 subunit toward recycling and membrane targeting
(PubMed:16037816). {ECO:0000269|PubMed:12015593,
ECO:0000269|PubMed:12501192, ECO:0000269|PubMed:12730367,
ECO:0000269|PubMed:12872125, ECO:0000269|PubMed:15591246,
ECO:0000269|PubMed:16037816, ECO:0000269|PubMed:16192394,
ECO:0000269|PubMed:16483599, ECO:0000269|PubMed:17018279,
ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:19946266,
ECO:0000269|PubMed:21172611, ECO:0000269|PubMed:21317873,
ECO:0000269|PubMed:21846932, ECO:0000269|PubMed:9351977}.
-!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
receptor subunits. Tetramers may be formed by the dimerization of
dimers. May interact with MPP4. Forms a ternary complex with GRIP1
and CSPG4 (By similarity). Interacts with ATAD1 in an ATP-
dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding
to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly.
Interacts with NSF via its C-terminus. Interacts with CACNG2,
PRKCABP and GRIP2 (PubMed:27756895). Part of a complex containing
GRIA2, NSF and NAPA and/or NAPB. Interacts with PICK1 (via PDZ
domain) (By similarity). Interacts with GRIA1 and SYNDIG1.
Interacts with SNX27 (via PDZ domain); the interaction is required
for recycling to the plasma membrane when endocytosed and prevent
degradation in lysosomes (By similarity). Interacts with LRFN1.
Found in a complex with GRIA3, GRIA4, CNIH2, CNIH3, CACNG2,
CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5.
Interacts with OLFM2 (By similarity). Interacts with AP4B1, AP4E1
and AP4M1; probably indirect it mediates the somatodendritic
localization of GRIA2 in neurons (By similarity). Forms a complex
with NSG1, GRIA2 and STX12; controls the intracellular fate of
AMPAR and the endosomal sorting of the GRIA2 subunit toward
recycling and membrane targeting (PubMed:16037816).
{ECO:0000250|UniProtKB:P23819, ECO:0000269|PubMed:10027300,
ECO:0000269|PubMed:10414981, ECO:0000269|PubMed:12015593,
ECO:0000269|PubMed:12501192, ECO:0000269|PubMed:16037816,
ECO:0000269|PubMed:16483599, ECO:0000269|PubMed:16630835,
ECO:0000269|PubMed:16793768, ECO:0000269|PubMed:18817736,
ECO:0000269|PubMed:19234459, ECO:0000269|PubMed:19265014,
ECO:0000269|PubMed:19946266, ECO:0000269|PubMed:21317873,
ECO:0000269|PubMed:21496646, ECO:0000269|PubMed:27756895,
ECO:0000269|PubMed:9069286, ECO:0000269|PubMed:9697855,
ECO:0000269|PubMed:9804426}.
-!- INTERACTION:
Self; NbExp=11; IntAct=EBI-77718, EBI-77718;
P0CB20:- (xeno); NbExp=2; IntAct=EBI-15817825, EBI-16116011;
Q8CGU4:Agap2; NbExp=4; IntAct=EBI-77718, EBI-4409108;
P84092:Ap2m1; NbExp=2; IntAct=EBI-77718, EBI-297693;
Q505J9:Atad1; NbExp=3; IntAct=EBI-77718, EBI-4280289;
Q71RJ2:Cacng2; NbExp=2; IntAct=EBI-77718, EBI-8538384;
P19490:Gria1; NbExp=3; IntAct=EBI-77718, EBI-371642;
P19492-2:Gria3; NbExp=4; IntAct=EBI-15817825, EBI-16201849;
P19493-2:Gria4; NbExp=2; IntAct=EBI-15817825, EBI-15852899;
P97879:Grip1; NbExp=15; IntAct=EBI-77718, EBI-936113;
Q9WTW1-3:Grip2; NbExp=7; IntAct=EBI-77718, EBI-936068;
P49185:Mapk8; NbExp=2; IntAct=EBI-9118256, EBI-7456505;
Q9QUL6:Nsf; NbExp=5; IntAct=EBI-77718, EBI-925794;
Q9EP80:Pick1; NbExp=13; IntAct=EBI-77718, EBI-77728;
Q13136:PPFIA1 (xeno); NbExp=2; IntAct=EBI-77718, EBI-745426;
Q91Z80:Ppfia4; NbExp=3; IntAct=EBI-77718, EBI-8276907;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P23819}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P23819}. Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
junction, synapse, postsynaptic cell membrane
{ECO:0000250|UniProtKB:P23819}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P23819}. Note=Interaction with CACNG2,
CNIH2 and CNIH3 promotes cell surface expression (By similarity).
Displays a somatodendritic localization and is excluded from axons
in neurons (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P23819}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Flop;
IsoId=P19491-1; Sequence=Displayed;
Name=Flip;
IsoId=P19491-2; Sequence=VSP_000111, VSP_000112, VSP_000113,
VSP_000114;
Name=3; Synonyms=Long;
IsoId=P19491-3; Sequence=VSP_029310;
-!- TISSUE SPECIFICITY: Detected in forebrain. Detected in dendrites
of neuronal cells. {ECO:0000269|PubMed:14687553,
ECO:0000269|PubMed:15240807, ECO:0000269|PubMed:9697855}.
-!- DEVELOPMENTAL STAGE: Detected at low levels in newborns. Levels
increase strongly and are highest in hippocampus from 8 to 14 day
old animals. Detected at intermediate levels at day 42 (at protein
level). {ECO:0000269|PubMed:14687553}.
-!- DOMAIN: The M4 transmembrane segment mediates tetramerization and
is required for cell surface expression. {ECO:0000250}.
-!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation.
Cys-610 palmitoylation leads to Golgi retention and decreased cell
surface expression. In contrast, Cys-836 palmitoylation does not
affect cell surface expression but regulates stimulation-dependent
endocytosis (By similarity). {ECO:0000250}.
-!- RNA EDITING: Modified_positions=607 {ECO:0000269|PubMed:1717158};
Note=Fully edited in the brain. Heteromerically expressed edited
GLUR2 (R) receptor complexes are impermeable to calcium, whereas
the unedited (Q) forms are highly permeable to divalent ions (By
similarity). {ECO:0000250};
-!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
variety of receptors that are named according to their selective
agonists. This receptor binds AMPA (quisqualate) > glutamate >
kainate.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. GRIA2 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M36419; AAA41244.1; -; mRNA.
EMBL; M38061; AAC37652.1; -; mRNA.
EMBL; M85035; AAA41240.1; -; mRNA.
EMBL; X54655; CAA38465.1; -; mRNA.
EMBL; AF164344; AAD51284.1; -; mRNA.
PIR; S13677; S13677.
RefSeq; NP_001077280.1; NM_001083811.1.
RefSeq; NP_058957.1; NM_017261.2.
UniGene; Rn.91361; -.
PDB; 1FTJ; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1FTK; X-ray; 1.60 A; A=404-528, A=653-796.
PDB; 1FTL; X-ray; 1.80 A; A/B=413-527, A/B=653-796.
PDB; 1FTM; X-ray; 1.70 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1FTO; X-ray; 2.00 A; A/B=413-527, A/B=653-796.
PDB; 1FW0; X-ray; 1.90 A; A=413-527, A=653-796.
PDB; 1GR2; X-ray; 1.90 A; A=404-528, A=652-796.
PDB; 1LB8; X-ray; 2.30 A; A/B=413-527, A/B=653-796.
PDB; 1LB9; X-ray; 2.30 A; A/B=413-527, A/B=653-796.
PDB; 1LBB; X-ray; 2.10 A; A=413-527, A=653-796.
PDB; 1LBC; X-ray; 1.80 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1M5B; X-ray; 1.85 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1M5C; X-ray; 1.65 A; A=413-527, A=653-796.
PDB; 1M5D; X-ray; 1.73 A; A=413-527, A=653-796.
PDB; 1M5E; X-ray; 1.46 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1M5F; X-ray; 1.95 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MM6; X-ray; 2.15 A; A/B=413-527, A/B=653-796.
PDB; 1MM7; X-ray; 1.65 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MQD; X-ray; 1.46 A; A/B/C/D=413-527, A/B/C/D=653-794.
PDB; 1MQG; X-ray; 2.15 A; A/B=413-527, A/B=653-796.
PDB; 1MQH; X-ray; 1.80 A; A=413-527, A=653-796.
PDB; 1MQI; X-ray; 1.35 A; A=413-527, A=653-796.
PDB; 1MQJ; X-ray; 1.65 A; A=413-527, A=653-796.
PDB; 1MS7; X-ray; 1.97 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MXU; X-ray; 1.80 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MXV; X-ray; 1.95 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MXW; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MXX; X-ray; 2.00 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MXY; X-ray; 1.95 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MXZ; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MY0; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MY1; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MY2; X-ray; 1.80 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MY3; X-ray; 1.75 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1MY4; X-ray; 1.90 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1N0T; X-ray; 2.10 A; A/B/C/D=413-527, A/B/C/D=653-796.
PDB; 1NNK; X-ray; 1.85 A; A=413-527, A=653-796.
PDB; 1NNP; X-ray; 1.90 A; A/B=413-527, A/B=653-796.
PDB; 1P1N; X-ray; 1.60 A; A=413-527, A=653-796.
PDB; 1P1O; X-ray; 1.60 A; A=413-527, A=653-796.
PDB; 1P1Q; X-ray; 2.00 A; A/B/C=413-527, A/B/C=653-796.
PDB; 1P1U; X-ray; 2.00 A; A/B=413-527, A/B=653-796.
PDB; 1P1W; X-ray; 1.80 A; A/B=413-527, A/B=653-796.
PDB; 1SYH; X-ray; 1.80 A; A=413-527, A=653-796.
PDB; 1SYI; X-ray; 2.10 A; A/B=413-527, A/B=653-796.
PDB; 1WVJ; X-ray; 1.75 A; A=413-527, A=653-796.
PDB; 1XHY; X-ray; 1.85 A; A=413-527, A=653-796.
PDB; 2AIX; X-ray; 2.17 A; A=413-527, A=653-796.
PDB; 2AL4; X-ray; 1.70 A; A/B/C/D/E/F=413-527, A/B/C/D/E/F=653-796.
PDB; 2AL5; X-ray; 1.65 A; A/B=413-527, A/B=653-796.
PDB; 2ANJ; X-ray; 2.10 A; A=413-527, A=653-796.
PDB; 2CMO; X-ray; 2.65 A; A/B=413-527, A/B=653-796.
PDB; 2GFE; X-ray; 1.54 A; A/B/C=413-527, A/B/C=653-795.
PDB; 2I3V; X-ray; 2.40 A; A/B/C/D=413-527, A/B/C/D=655-794.
PDB; 2I3W; X-ray; 2.30 A; A/B=413-527, A/B=653-794.
PDB; 2P2A; X-ray; 2.26 A; A/B=413-527, A/B=653-796.
PDB; 2UXA; X-ray; 2.38 A; A/B/C=412-795.
PDB; 2XX7; X-ray; 2.20 A; A/B/C=413-527, A/B/C=653-795.
PDB; 2XX8; X-ray; 1.55 A; A/B/C=413-527, A/B/C=653-796.
PDB; 2XX9; X-ray; 1.97 A; A/B/C=413-527, A/B/C=653-796.
PDB; 2XXH; X-ray; 1.50 A; A/B/C=413-527, A/B/C=653-796.
PDB; 2XXI; X-ray; 1.60 A; A/B/C=413-527, A/B/C=653-796.
PDB; 3B6Q; X-ray; 2.00 A; A=413-527, A=653-796.
PDB; 3B6T; X-ray; 2.10 A; A=413-527, A=653-796.
PDB; 3B6W; X-ray; 1.70 A; A/B/C/D=413-527, A/B/C/D=653-796.
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.
PDB; 3BBR; X-ray; 2.25 A; A/B=413-527, A/B=653-796.
PDB; 3BFT; X-ray; 2.27 A; A/B/C=413-527, A/B/C=653-796.
PDB; 3BFU; X-ray; 1.95 A; A/B/C/D=413-527, A/B/C/D=653-796.
PDB; 3BKI; X-ray; 1.87 A; B/C/D/P=413-527, B/C/D/P=653-796.
PDB; 3DP6; X-ray; 1.55 A; A/B/C=413-527, A/B/C=653-794.
PDB; 3H03; X-ray; 1.90 A; A/B/D/G=414-527, A/B/D/G=653-794.
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.
PDB; 3H5V; X-ray; 2.33 A; A/B/C=21-404.
PDB; 3H5W; X-ray; 2.69 A; A/B=21-404.
PDB; 3H6T; X-ray; 2.25 A; A/B/C=413-527, A/B/C=653-796.
PDB; 3H6U; X-ray; 1.85 A; A=413-527, A=653-796.
PDB; 3H6V; X-ray; 2.10 A; A/B=413-527, A/B=653-796.
PDB; 3H6W; X-ray; 1.49 A; A/B=413-527, A/B=653-796.
PDB; 3HSY; X-ray; 1.75 A; A/B=25-400.
PDB; 3IJO; X-ray; 2.00 A; B/E/H=414-527, B/E/H=653-794.
PDB; 3IJX; X-ray; 2.88 A; B/D/H=414-527, B/D/H=653-794.
PDB; 3IK6; X-ray; 2.10 A; B/E/H=414-527, B/E/H=653-794.
PDB; 3IL1; X-ray; 2.00 A; B/E/H=414-527, B/E/H=653-794.
PDB; 3ILT; X-ray; 2.11 A; B/E/H=414-527, B/E/H=653-794.
PDB; 3ILU; X-ray; 2.00 A; B/E/H=414-527, B/E/H=653-794.
PDB; 3KG2; X-ray; 3.60 A; A/B/C/D=25-412, A/B/C/D=414-847.
PDB; 3KGC; X-ray; 1.55 A; A/B=414-527, A/B=654-795.
PDB; 3LSF; X-ray; 1.85 A; B/E/H=414-527, B/E/H=653-794.
PDB; 3LSL; X-ray; 2.12 A; A/D/G=414-527, A/D/G=653-794.
PDB; 3M3L; X-ray; 1.85 A; A/D/G=414-794.
PDB; 3N6V; X-ray; 3.20 A; A/B/C/D/E/F=27-400.
PDB; 3O28; X-ray; 2.00 A; A=413-527, A=653-795.
PDB; 3O29; X-ray; 2.02 A; A=413-527, A=653-795.
PDB; 3O2A; X-ray; 1.90 A; A=413-527, A=653-795.
PDB; 3O2J; X-ray; 1.95 A; A/B=22-400.
PDB; 3O6G; X-ray; 1.80 A; A=413-527, A=653-795.
PDB; 3O6H; X-ray; 2.10 A; A=413-527, A=653-795.
PDB; 3O6I; X-ray; 1.80 A; A=413-527, A=653-795.
PDB; 3PD8; X-ray; 2.48 A; A/B/C=413-527, A/B/C=653-795.
PDB; 3PD9; X-ray; 2.10 A; A/B=413-527, A/B=653-795.
PDB; 3PMV; X-ray; 1.80 A; A=413-527, A=653-795.
PDB; 3PMW; X-ray; 2.20 A; A=413-527, A=653-795.
PDB; 3PMX; X-ray; 1.87 A; A=413-527, A=653-795.
PDB; 3RTF; X-ray; 1.70 A; B/D/F=414-527, B/D/F=653-794.
PDB; 3RTW; X-ray; 2.10 A; B/D/F=414-527, B/D/F=653-794.
PDB; 3T93; X-ray; 1.91 A; B/D/F=414-527, B/D/F=653-794.
PDB; 3T96; X-ray; 1.87 A; B/D/F=414-527, B/D/F=653-794.
PDB; 3T9H; X-ray; 2.02 A; B/D/F=414-527, B/D/F=653-794.
PDB; 3T9U; X-ray; 1.97 A; A/B/C=414-527, A/B/C=653-794.
PDB; 3T9V; X-ray; 1.98 A; A/B=414-527, A/B=653-794.
PDB; 3T9X; X-ray; 1.82 A; B/D/F=414-527, B/D/F=653-794.
PDB; 3TDJ; X-ray; 1.95 A; A/B=413-527, A/B=653-796.
PDB; 3TKD; X-ray; 1.45 A; A/B=413-527, A/B=653-795.
PDB; 3TZA; X-ray; 1.90 A; A/B=413-527, A/B=653-796.
PDB; 4FAT; X-ray; 1.40 A; A=413-527, A=653-796.
PDB; 4G8M; X-ray; 2.05 A; A/B=413-527, A/B=653-796.
PDB; 4GXS; X-ray; 1.96 A; B/D=414-527, B/D=653-794.
PDB; 4H8J; X-ray; 1.80 A; A/B/C/D=413-527, A/B/C/D=653-797.
PDB; 4IGT; X-ray; 1.24 A; A=413-527, A=653-796.
PDB; 4ISU; X-ray; 2.30 A; A/B/C/D=413-527, A/B/C/D=653-796.
PDB; 4IY5; X-ray; 2.00 A; A/B=413-527, A/B=653-796.
PDB; 4IY6; X-ray; 1.72 A; A=413-527, A=653-796.
PDB; 4L17; X-ray; 2.80 A; A/C/E/G=413-527, A/C/E/G=653-796.
PDB; 4LZ5; X-ray; 1.50 A; A/B/C=404-527, A/B/C=653-796.
PDB; 4LZ7; X-ray; 2.10 A; A/B/C=404-527, A/B/C=653-796.
PDB; 4LZ8; X-ray; 1.85 A; A/B/C=404-527, A/B/C=653-796.
PDB; 4N07; X-ray; 1.87 A; A/B/C=413-527, A/B/C=653-796.
PDB; 4O3A; X-ray; 1.80 A; A/B/C=413-527, A/B/C=653-796.
PDB; 4O3B; X-ray; 1.91 A; A/B=413-527, A/B=653-796.
PDB; 4O3C; X-ray; 1.50 A; A=413-527, A=653-796.
PDB; 4Q30; X-ray; 2.03 A; B/D/F=414-527, B/D/F=653-794.
PDB; 4U1O; X-ray; 1.85 A; A=413-527, A=653-796.
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.
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.
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.
PDB; 4U1Z; X-ray; 1.94 A; A=413-527, A=653-796.
PDB; 4U21; X-ray; 1.39 A; A/B=413-527, A/B=654-796.
PDB; 4U22; X-ray; 1.44 A; A=413-527, A=653-796.
PDB; 4U23; X-ray; 1.67 A; A=413-527, A=653-796.
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.
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.
PDB; 4U2R; X-ray; 1.41 A; A/B/C/D=413-527, A/B/C/D=653-796.
PDB; 4U4F; X-ray; 4.79 A; A/B/C/D=25-412, A/B/C/D=414-847.
PDB; 4U4G; X-ray; 4.49 A; A/B/C/D=25-412, A/B/C/D=414-847.
PDB; 4U4S; X-ray; 1.90 A; A/B=413-527, A/B=653-796.
PDB; 4U4X; X-ray; 1.56 A; A/B=413-527, A/B=653-796.
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.
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.
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.
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.
PDB; 4U5F; X-ray; 3.70 A; A/B/C/D=25-412, A/B/C/D=414-850.
PDB; 4UQ6; EM; 12.80 A; A/B/C/D=22-847.
PDB; 4UQJ; EM; 10.40 A; A/B/C/D=22-847.
PDB; 4UQK; EM; 16.40 A; A/B/C/D=22-847.
PDB; 4X48; X-ray; 1.89 A; A/B/C=413-527, A/B/C=653-796.
PDB; 4YMA; X-ray; 1.90 A; A/B=413-527, A/B=653-797.
PDB; 4YU0; X-ray; 1.26 A; A/B=413-527, A/B=653-796.
PDB; 4Z0I; X-ray; 1.45 A; A/B=413-527, A/B=653-796.
PDB; 5BUU; X-ray; 2.07 A; A/B=413-527, A/B=653-796.
PDB; 5CBR; X-ray; 2.00 A; A=413-527, A=653-797.
PDB; 5CBS; X-ray; 1.80 A; A/B/C/D=413-527, A/B/C/D=653-797.
PDB; 5ELV; X-ray; 1.92 A; A/B=413-527, A/B=653-797.
PDB; 5FHM; X-ray; 1.55 A; A/B=413-527, A/B=653-797.
PDB; 5FHN; X-ray; 1.60 A; A=413-527, A=653-797.
PDB; 5FHO; X-ray; 2.30 A; A/B/C/D=413-527, A/B/C/D=653-797.
PDB; 5FTH; X-ray; 2.90 A; A/B/C=404-527, A/B/C=653-795.
PDB; 5FTI; X-ray; 1.35 A; A/B=404-527, A/B=653-795.
PDB; 5FWX; X-ray; 2.50 A; A/C=25-400.
PDB; 5FWY; X-ray; 2.12 A; A/C=25-400.
PDB; 5IDE; EM; 8.25 A; A/C=23-883.
PDB; 5IDF; EM; 10.31 A; A/C=23-883.
PDB; 5JEI; X-ray; 1.23 A; A=413-527, A=653-797.
PDB; 5KBS; EM; 8.70 A; A/B/C/D=25-847.
PDB; 5KBT; EM; 6.40 A; A/B/C/D=25-847.
PDB; 5KBU; EM; 7.80 A; A/B/C/D=25-847.
PDB; 5KBV; EM; 6.80 A; A/B/C/D=25-412, A/B/C/D=414-847.
PDB; 5KK2; EM; 7.30 A; A/B/C/D=1-883.
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.
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.
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.
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.
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.
PDB; 5N6P; X-ray; 2.80 A; A=25-400.
PDB; 5NG9; X-ray; 1.15 A; A=413-527, A=653-797.
PDB; 5NIH; X-ray; 1.30 A; A/B=413-527, A/B=653-797.
PDB; 5NS9; X-ray; 1.44 A; A/B=413-527, A/B=653-797.
PDB; 5O9A; X-ray; 1.78 A; A/B/C/D=413-527, A/B/C/D=653-797.
PDB; 5OEW; X-ray; 2.00 A; A/B/C=413-527, A/B/C=653-797.
PDB; 5VHW; EM; 7.80 A; A/B/C/D=25-847.
PDB; 5VHX; EM; 8.30 A; A/B/C/D/E=25-847.
PDB; 5VHY; EM; 4.60 A; A/B/C/D/E/F=25-847.
PDB; 5VHZ; EM; 8.40 A; A/B/C/D/E/F=25-847.
PDB; 5VOT; EM; 4.90 A; A/B/C/D=1-883.
PDB; 5VOU; EM; 6.40 A; A/B/C/D=1-883.
PDB; 5VOV; EM; 7.70 A; A/B/C/D=1-883.
PDB; 5WEK; EM; 4.60 A; A/B/C/D=25-847.
PDB; 5WEL; EM; 4.40 A; A/B/C/D=25-847.
PDB; 5WEM; EM; 6.10 A; A/B/C/D=25-847.
PDB; 5WEN; EM; 6.80 A; A/B/C/D=25-847.
PDB; 5WEO; EM; 4.20 A; A/B/C/D=25-847.
PDB; 6DLZ; EM; 3.90 A; A/B/C/D=25-847.
PDB; 6DM0; EM; 4.40 A; A/B/C/D=25-847.
PDB; 6DM1; EM; 4.20 A; A/B/C/D=25-847.
PDB; 6DM2; EM; 4.60 A; A/B/C/D=25-847.
PDBsum; 1FTJ; -.
PDBsum; 1FTK; -.
PDBsum; 1FTL; -.
PDBsum; 1FTM; -.
PDBsum; 1FTO; -.
PDBsum; 1FW0; -.
PDBsum; 1GR2; -.
PDBsum; 1LB8; -.
PDBsum; 1LB9; -.
PDBsum; 1LBB; -.
PDBsum; 1LBC; -.
PDBsum; 1M5B; -.
PDBsum; 1M5C; -.
PDBsum; 1M5D; -.
PDBsum; 1M5E; -.
PDBsum; 1M5F; -.
PDBsum; 1MM6; -.
PDBsum; 1MM7; -.
PDBsum; 1MQD; -.
PDBsum; 1MQG; -.
PDBsum; 1MQH; -.
PDBsum; 1MQI; -.
PDBsum; 1MQJ; -.
PDBsum; 1MS7; -.
PDBsum; 1MXU; -.
PDBsum; 1MXV; -.
PDBsum; 1MXW; -.
PDBsum; 1MXX; -.
PDBsum; 1MXY; -.
PDBsum; 1MXZ; -.
PDBsum; 1MY0; -.
PDBsum; 1MY1; -.
PDBsum; 1MY2; -.
PDBsum; 1MY3; -.
PDBsum; 1MY4; -.
PDBsum; 1N0T; -.
PDBsum; 1NNK; -.
PDBsum; 1NNP; -.
PDBsum; 1P1N; -.
PDBsum; 1P1O; -.
PDBsum; 1P1Q; -.
PDBsum; 1P1U; -.
PDBsum; 1P1W; -.
PDBsum; 1SYH; -.
PDBsum; 1SYI; -.
PDBsum; 1WVJ; -.
PDBsum; 1XHY; -.
PDBsum; 2AIX; -.
PDBsum; 2AL4; -.
PDBsum; 2AL5; -.
PDBsum; 2ANJ; -.
PDBsum; 2CMO; -.
PDBsum; 2GFE; -.
PDBsum; 2I3V; -.
PDBsum; 2I3W; -.
PDBsum; 2P2A; -.
PDBsum; 2UXA; -.
PDBsum; 2XX7; -.
PDBsum; 2XX8; -.
PDBsum; 2XX9; -.
PDBsum; 2XXH; -.
PDBsum; 2XXI; -.
PDBsum; 3B6Q; -.
PDBsum; 3B6T; -.
PDBsum; 3B6W; -.
PDBsum; 3B7D; -.
PDBsum; 3BBR; -.
PDBsum; 3BFT; -.
PDBsum; 3BFU; -.
PDBsum; 3BKI; -.
PDBsum; 3DP6; -.
PDBsum; 3H03; -.
PDBsum; 3H06; -.
PDBsum; 3H5V; -.
PDBsum; 3H5W; -.
PDBsum; 3H6T; -.
PDBsum; 3H6U; -.
PDBsum; 3H6V; -.
PDBsum; 3H6W; -.
PDBsum; 3HSY; -.
PDBsum; 3IJO; -.
PDBsum; 3IJX; -.
PDBsum; 3IK6; -.
PDBsum; 3IL1; -.
PDBsum; 3ILT; -.
PDBsum; 3ILU; -.
PDBsum; 3KG2; -.
PDBsum; 3KGC; -.
PDBsum; 3LSF; -.
PDBsum; 3LSL; -.
PDBsum; 3M3L; -.
PDBsum; 3N6V; -.
PDBsum; 3O28; -.
PDBsum; 3O29; -.
PDBsum; 3O2A; -.
PDBsum; 3O2J; -.
PDBsum; 3O6G; -.
PDBsum; 3O6H; -.
PDBsum; 3O6I; -.
PDBsum; 3PD8; -.
PDBsum; 3PD9; -.
PDBsum; 3PMV; -.
PDBsum; 3PMW; -.
PDBsum; 3PMX; -.
PDBsum; 3RTF; -.
PDBsum; 3RTW; -.
PDBsum; 3T93; -.
PDBsum; 3T96; -.
PDBsum; 3T9H; -.
PDBsum; 3T9U; -.
PDBsum; 3T9V; -.
PDBsum; 3T9X; -.
PDBsum; 3TDJ; -.
PDBsum; 3TKD; -.
PDBsum; 3TZA; -.
PDBsum; 4FAT; -.
PDBsum; 4G8M; -.
PDBsum; 4GXS; -.
PDBsum; 4H8J; -.
PDBsum; 4IGT; -.
PDBsum; 4ISU; -.
PDBsum; 4IY5; -.
PDBsum; 4IY6; -.
PDBsum; 4L17; -.
PDBsum; 4LZ5; -.
PDBsum; 4LZ7; -.
PDBsum; 4LZ8; -.
PDBsum; 4N07; -.
PDBsum; 4O3A; -.
PDBsum; 4O3B; -.
PDBsum; 4O3C; -.
PDBsum; 4Q30; -.
PDBsum; 4U1O; -.
PDBsum; 4U1W; -.
PDBsum; 4U1X; -.
PDBsum; 4U1Y; -.
PDBsum; 4U1Z; -.
PDBsum; 4U21; -.
PDBsum; 4U22; -.
PDBsum; 4U23; -.
PDBsum; 4U2P; -.
PDBsum; 4U2Q; -.
PDBsum; 4U2R; -.
PDBsum; 4U4F; -.
PDBsum; 4U4G; -.
PDBsum; 4U4S; -.
PDBsum; 4U4X; -.
PDBsum; 4U5B; -.
PDBsum; 4U5C; -.
PDBsum; 4U5D; -.
PDBsum; 4U5E; -.
PDBsum; 4U5F; -.
PDBsum; 4UQ6; -.
PDBsum; 4UQJ; -.
PDBsum; 4UQK; -.
PDBsum; 4X48; -.
PDBsum; 4YMA; -.
PDBsum; 4YU0; -.
PDBsum; 4Z0I; -.
PDBsum; 5BUU; -.
PDBsum; 5CBR; -.
PDBsum; 5CBS; -.
PDBsum; 5ELV; -.
PDBsum; 5FHM; -.
PDBsum; 5FHN; -.
PDBsum; 5FHO; -.
PDBsum; 5FTH; -.
PDBsum; 5FTI; -.
PDBsum; 5FWX; -.
PDBsum; 5FWY; -.
PDBsum; 5IDE; -.
PDBsum; 5IDF; -.
PDBsum; 5JEI; -.
PDBsum; 5KBS; -.
PDBsum; 5KBT; -.
PDBsum; 5KBU; -.
PDBsum; 5KBV; -.
PDBsum; 5KK2; -.
PDBsum; 5L1B; -.
PDBsum; 5L1E; -.
PDBsum; 5L1F; -.
PDBsum; 5L1G; -.
PDBsum; 5L1H; -.
PDBsum; 5N6P; -.
PDBsum; 5NG9; -.
PDBsum; 5NIH; -.
PDBsum; 5NS9; -.
PDBsum; 5O9A; -.
PDBsum; 5OEW; -.
PDBsum; 5VHW; -.
PDBsum; 5VHX; -.
PDBsum; 5VHY; -.
PDBsum; 5VHZ; -.
PDBsum; 5VOT; -.
PDBsum; 5VOU; -.
PDBsum; 5VOV; -.
PDBsum; 5WEK; -.
PDBsum; 5WEL; -.
PDBsum; 5WEM; -.
PDBsum; 5WEN; -.
PDBsum; 5WEO; -.
PDBsum; 6DLZ; -.
PDBsum; 6DM0; -.
PDBsum; 6DM1; -.
PDBsum; 6DM2; -.
ProteinModelPortal; P19491; -.
SMR; P19491; -.
BioGrid; 248250; 9.
CORUM; P19491; -.
DIP; DIP-30952N; -.
ELM; P19491; -.
IntAct; P19491; 27.
MINT; P19491; -.
STRING; 10116.ENSRNOP00000062152; -.
BindingDB; P19491; -.
ChEMBL; CHEMBL3503; -.
GuidetoPHARMACOLOGY; 445; -.
iPTMnet; P19491; -.
PhosphoSitePlus; P19491; -.
SwissPalm; P19491; -.
PaxDb; P19491; -.
PRIDE; P19491; -.
GeneID; 29627; -.
KEGG; rno:29627; -.
UCSC; RGD:61862; rat. [P19491-1]
CTD; 2891; -.
RGD; 61862; Gria2.
eggNOG; KOG1054; Eukaryota.
eggNOG; ENOG410XPSH; LUCA.
HOGENOM; HOG000234372; -.
HOVERGEN; HBG051839; -.
InParanoid; P19491; -.
KO; K05198; -.
PhylomeDB; P19491; -.
EvolutionaryTrace; P19491; -.
PRO; PR:P19491; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0008328; C:ionotropic glutamate receptor complex; TAS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0004971; F:AMPA glutamate receptor activity; IDA:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:UniProtKB.
GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
GO; GO:0000149; F:SNARE binding; IPI:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD.
GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0001919; P:regulation of receptor recycling; IMP:UniProtKB.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
GO; GO:0060992; P:response to fungicide; IEP:RGD.
GO; GO:0010226; P:response to lithium ion; IEP:UniProtKB.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Complete proteome; Disulfide bond; Endoplasmic reticulum;
Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing;
Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 883 Glutamate receptor 2.
/FTId=PRO_0000011535.
TOPO_DOM 22 543 Extracellular.
TRANSMEM 544 564 Helical.
TOPO_DOM 565 591 Cytoplasmic.
INTRAMEM 592 607 Helical; Pore-forming.
INTRAMEM 608 610
TOPO_DOM 611 616 Cytoplasmic.
TRANSMEM 617 637 Helical.
TOPO_DOM 638 812 Extracellular.
TRANSMEM 813 833 Helical; Name=M4.
TOPO_DOM 834 883 Cytoplasmic.
REGION 499 501 Glutamate binding.
REGION 675 676 Glutamate binding.
BINDING 471 471 Glutamate. {ECO:0000269|PubMed:16483599}.
BINDING 501 501 Kainate; via amide nitrogen.
{ECO:0000269|PubMed:25103405}.
BINDING 506 506 Glutamate. {ECO:0000269|PubMed:16483599}.
BINDING 506 506 Kainate. {ECO:0000269|PubMed:25103405}.
BINDING 675 675 Kainate; via amide nitrogen.
{ECO:0000269|PubMed:25103405}.
BINDING 676 676 Kainate; via amide nitrogen.
{ECO:0000269|PubMed:25103405}.
BINDING 726 726 Glutamate. {ECO:0000269|PubMed:16483599}.
BINDING 726 726 Kainate. {ECO:0000269|PubMed:25103405}.
SITE 474 474 Interaction with the cone snail toxin
Con-ikot-ikot.
{ECO:0000269|PubMed:25103405}.
SITE 654 654 Crucial to convey clamshell closure to
channel opening.
{ECO:0000269|PubMed:25103405}.
SITE 681 681 Interaction with the cone snail toxin
Con-ikot-ikot.
{ECO:0000269|PubMed:25103405}.
SITE 773 773 Interaction with the cone snail toxin
Con-ikot-ikot.
{ECO:0000269|PubMed:25103405}.
MOD_RES 683 683 Phosphoserine; by PKC.
{ECO:0000269|PubMed:8848293}.
MOD_RES 717 717 Phosphoserine; by PKG.
{ECO:0000269|PubMed:8848293}.
MOD_RES 860 860 Phosphoserine.
{ECO:0000250|UniProtKB:P23819}.
MOD_RES 863 863 Phosphoserine.
{ECO:0000250|UniProtKB:P23819}.
MOD_RES 876 876 Phosphotyrosine.
{ECO:0000269|PubMed:15240807}.
MOD_RES 880 880 Phosphoserine.
{ECO:0000250|UniProtKB:P23819}.
LIPID 610 610 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 836 836 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21317873}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19946266,
ECO:0000269|PubMed:21317873,
ECO:0000269|PubMed:25103405}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 330
DISULFID 739 794
VAR_SEQ 765 766 NA -> TP (in isoform Flip).
{ECO:0000303|PubMed:1699567,
ECO:0000303|PubMed:2166337,
ECO:0000303|PubMed:9351977}.
/FTId=VSP_000111.
VAR_SEQ 775 775 N -> S (in isoform Flip).
{ECO:0000303|PubMed:1699567,
ECO:0000303|PubMed:2166337,
ECO:0000303|PubMed:9351977}.
/FTId=VSP_000112.
VAR_SEQ 779 779 L -> V (in isoform Flip).
{ECO:0000303|PubMed:1699567,
ECO:0000303|PubMed:2166337,
ECO:0000303|PubMed:9351977}.
/FTId=VSP_000113.
VAR_SEQ 796 800 SGGGD -> AKDSG (in isoform Flip).
{ECO:0000303|PubMed:1699567,
ECO:0000303|PubMed:2166337,
ECO:0000303|PubMed:9351977}.
/FTId=VSP_000114.
VAR_SEQ 848 883 VAKNPQNINPSSSQNSQNFATYKEGYNVYGIESVKI -> M
TLSDVMRSKARLSITGSTGENGRVMTPEFPKAVHAVPYVSP
GMGMNVSVTDLS (in isoform 3).
{ECO:0000305}.
/FTId=VSP_029310.
VARIANT 607 607 Q -> R (in RNA edited version).
MUTAGEN 504 504 L->Y: Promotes dimerization. Strongly
reduced desensitization.
{ECO:0000269|PubMed:12015593}.
MUTAGEN 775 775 N->D: Increases rate of desensitization.
{ECO:0000269|PubMed:12015593}.
MUTAGEN 851 852 NP->AA: Strongly reduces interaction with
NSF. {ECO:0000269|PubMed:9697855}.
STRAND 26 34 {ECO:0000244|PDB:3HSY}.
HELIX 38 50 {ECO:0000244|PDB:3HSY}.
STRAND 57 65 {ECO:0000244|PDB:3HSY}.
HELIX 70 82 {ECO:0000244|PDB:3HSY}.
STRAND 86 90 {ECO:0000244|PDB:3HSY}.
TURN 94 96 {ECO:0000244|PDB:3HSY}.
HELIX 97 107 {ECO:0000244|PDB:3HSY}.
STRAND 110 113 {ECO:0000244|PDB:3HSY}.
STRAND 125 127 {ECO:0000244|PDB:3HSY}.
HELIX 133 142 {ECO:0000244|PDB:3HSY}.
STRAND 147 152 {ECO:0000244|PDB:3HSY}.
TURN 154 156 {ECO:0000244|PDB:5FWY}.
HELIX 159 171 {ECO:0000244|PDB:3HSY}.
STRAND 174 179 {ECO:0000244|PDB:3HSY}.
STRAND 182 185 {ECO:0000244|PDB:3O2J}.
HELIX 188 199 {ECO:0000244|PDB:3HSY}.
TURN 201 203 {ECO:0000244|PDB:3H5V}.
STRAND 206 211 {ECO:0000244|PDB:3HSY}.
HELIX 213 226 {ECO:0000244|PDB:3HSY}.
TURN 227 229 {ECO:0000244|PDB:4U1X}.
HELIX 230 232 {ECO:0000244|PDB:3HSY}.
STRAND 234 237 {ECO:0000244|PDB:3HSY}.
STRAND 239 241 {ECO:0000244|PDB:3HSY}.
HELIX 242 244 {ECO:0000244|PDB:5FWY}.
HELIX 247 249 {ECO:0000244|PDB:3HSY}.
STRAND 251 254 {ECO:0000244|PDB:5FWY}.
STRAND 256 262 {ECO:0000244|PDB:3HSY}.
STRAND 265 267 {ECO:0000244|PDB:4U1X}.
HELIX 268 277 {ECO:0000244|PDB:3HSY}.
TURN 282 284 {ECO:0000244|PDB:3HSY}.
STRAND 289 291 {ECO:0000244|PDB:5FWY}.
HELIX 295 316 {ECO:0000244|PDB:3HSY}.
TURN 330 332 {ECO:0000244|PDB:5N6P}.
HELIX 339 350 {ECO:0000244|PDB:3HSY}.
STRAND 353 355 {ECO:0000244|PDB:3HSY}.
STRAND 358 360 {ECO:0000244|PDB:3HSY}.
STRAND 366 368 {ECO:0000244|PDB:3HSY}.
STRAND 372 379 {ECO:0000244|PDB:3HSY}.
STRAND 382 390 {ECO:0000244|PDB:3HSY}.
TURN 391 393 {ECO:0000244|PDB:3HSY}.
STRAND 394 397 {ECO:0000244|PDB:3HSY}.
STRAND 416 420 {ECO:0000244|PDB:5NG9}.
TURN 424 426 {ECO:0000244|PDB:5NG9}.
STRAND 427 429 {ECO:0000244|PDB:5NG9}.
HELIX 433 435 {ECO:0000244|PDB:5NG9}.
HELIX 438 441 {ECO:0000244|PDB:5NG9}.
STRAND 442 444 {ECO:0000244|PDB:5NG9}.
HELIX 445 457 {ECO:0000244|PDB:5NG9}.
STRAND 461 465 {ECO:0000244|PDB:5NG9}.
STRAND 467 469 {ECO:0000244|PDB:4U2P}.
STRAND 472 474 {ECO:0000244|PDB:2CMO}.
TURN 476 478 {ECO:0000244|PDB:5NG9}.
HELIX 483 489 {ECO:0000244|PDB:5NG9}.
STRAND 494 496 {ECO:0000244|PDB:5NG9}.
HELIX 504 507 {ECO:0000244|PDB:5NG9}.
STRAND 510 512 {ECO:0000244|PDB:5NG9}.
STRAND 516 519 {ECO:0000244|PDB:5NG9}.
STRAND 521 526 {ECO:0000244|PDB:5NG9}.
TURN 534 538 {ECO:0000244|PDB:4U1W}.
STRAND 539 542 {ECO:0000244|PDB:4U1W}.
HELIX 544 565 {ECO:0000244|PDB:4U2P}.
HELIX 617 650 {ECO:0000244|PDB:4U2P}.
HELIX 653 655 {ECO:0000244|PDB:4U1W}.
HELIX 657 661 {ECO:0000244|PDB:5NG9}.
STRAND 664 674 {ECO:0000244|PDB:5NG9}.
HELIX 675 682 {ECO:0000244|PDB:5NG9}.
HELIX 686 697 {ECO:0000244|PDB:5NG9}.
STRAND 704 706 {ECO:0000244|PDB:5NG9}.
HELIX 707 716 {ECO:0000244|PDB:5NG9}.
TURN 717 719 {ECO:0000244|PDB:5NG9}.
STRAND 720 726 {ECO:0000244|PDB:5NG9}.
HELIX 727 734 {ECO:0000244|PDB:5NG9}.
STRAND 736 738 {ECO:0000244|PDB:4YU0}.
STRAND 741 745 {ECO:0000244|PDB:5NG9}.
STRAND 751 753 {ECO:0000244|PDB:5NG9}.
STRAND 756 758 {ECO:0000244|PDB:5NG9}.
HELIX 764 776 {ECO:0000244|PDB:5NG9}.
HELIX 779 788 {ECO:0000244|PDB:5NG9}.
TURN 789 791 {ECO:0000244|PDB:5NG9}.
STRAND 800 803 {ECO:0000244|PDB:4U2P}.
HELIX 810 813 {ECO:0000244|PDB:4U2P}.
HELIX 815 831 {ECO:0000244|PDB:4U2P}.
HELIX 833 836 {ECO:0000244|PDB:4U2P}.
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


Related products :

Catalog number Product name Quantity
18-783-77674 SHEEP ANTI GLUTAMATE RECEPTOR 2 - GLUTAMATE RECEPTOR 2; GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.02 mg
10-783-79552 SYNTHETIC HUMAN GLUTAMATE RECEPTOR 2 (aa831-842) - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 0.05 mg
18-662-20066 Glutamate receptor 1 - GluR-1; GluR-A; GluR-K1; Glutamate receptor ionotropic. AMPA 1; AMPA-selective glutamate receptor 1 Polyclonal 0.1 ml
18-003-42968 Glutamate receptor 2 - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.1 mg Protein A
18-662-20051 Glutamate receptor 2 - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.1 ml
18-662-20050 Glutamate receptor 2 - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.1 ml
18-662-20065 Glutamate receptor 1 - GluR-1; GluR-A; GluR-K1; Glutamate receptor ionotropic. AMPA 1; AMPA-selective glutamate receptor 1 Polyclonal 0.1 ml
18-003-43297 Glutamate receptor 2 - GluR-2; GluR-B; GluR-K2; Glutamate receptor ionotropic. AMPA 2; AMPA-selective glutamate receptor 2 Polyclonal 0.1 mg Protein A
18-003-42646 Glutamate receptor. ionotropic kainate 2 - Glutamate receptor 6; GluR-6; GluR6; Excitatory amino acid receptor 4; EAA4 Polyclonal 0.05 mg Aff Pur
18-003-42645 Glutamate receptor. ionotropic kainate 2 - Glutamate receptor 6; GluR-6; GluR6; Excitatory amino acid receptor 4; EAA4 Polyclonal 0.1 mg Protein A
201-11-1567 Rat Glutamate Receptor, Ionotropic, AMPA 1(GRIA1)ELISA Kit 96T
E11295h Human Glutamate Receptor, Ionotropic, AMPA 3 ELISA 96T
E11294h Human Glutamate Receptor, Ionotropic, AMPA 2 ELISA 96T
E11296h Human Glutamate Receptor, Ionotropic, AMPA 4 ELISA 96T
201-20-2385 GRIA2{glutamate receptor, ionotropic, AMPA 2}rabbit.pAb 0.2ml
E94801Ra ELISA Kit for Glutamate Receptor, Ionotropic, AMPA 1 (GRIA1) 96T/Kit
UB-E10079 Rat Glutamate Receptor, Ionotropic, AMPA 1(GRIA1)ELISA Kit 96T
E11293h Human Glutamate Receptor, Ionotropic, AMPA 1 ELISA 96T
GRIA3 GRIA1 Gene glutamate receptor, ionotropic, AMPA 1
GRIA4 GRIA2 Gene glutamate receptor, ionotropic, AMPA 2
QY-E10079 Rat Glutamate Receptor, Ionotropic, AMPA 1(GRIA1)ELISA Kit 96T
UB-E05158 Human Glutamate Receptor, Ionotropic, AMPA 3(GRIA3)ELISA Kit 96T
UB-E20662 Mouse Glutamate Receptor, Ionotropic, AMPA 1(GRIA1)ELISA Kit 96T
GWB-245BF1 Anti- GRIA2 (glutamate receptor. ionotropic. AMPA 2) Antibody
GWB-98DB8F Anti- GRIA2 (glutamate receptor. ionotropic. AMPA 2) Antibody


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur