GRIA2_MOUSE
ID GRIA2_MOUSE Reviewed; 883 AA.
AC P23819; Q61604; Q61605; Q8BG69; Q8BXU3; Q9D6D3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 204.
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;
DE Flags: Precursor;
GN Name=Gria2 {ECO:0000312|MGI:MGI:95809}; Synonyms=Glur2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1699805; DOI=10.1016/0014-5793(90)80452-o;
RA Sakimura K., Bujo H., Kushiya E., Araki K., Yamazaki M., Yamazaki M.,
RA Meguro H., Warashina A., Numa S., Mishina M.;
RT "Functional expression from cloned cDNAs of glutamate receptor species
RT responsive to kainate and quisqualate.";
RL FEBS Lett. 272:73-80(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7545935; DOI=10.1016/s0021-9258(17)32444-4;
RA Koehler M., Kornau H.-C., Seeburg P.H.;
RT "The organization of the gene for the functionally dominant alpha-amino-3-
RT hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B.";
RL J. Biol. Chem. 269:17367-17370(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, Medulla oblongata, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
RP INTERACTION WITH MPP4.
RX PubMed=10558890; DOI=10.1006/bbrc.1999.1723;
RA Inagaki H., Maeda S., Lin K.H., Shimizu N., Saito T.;
RT "rDLG6: a novel homolog of Drosophila DLG expressed in rat brain.";
RL Biochem. Biophys. Res. Commun. 265:462-468(1999).
RN [6]
RP PHOSPHORYLATION AT SER-880.
RX PubMed=10501226; DOI=10.1046/j.1471-4159.1999.731765.x;
RA Matsuda S., Mikawa S., Hirai H.;
RT "Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C
RT terminus from binding with glutamate receptor-interacting protein.";
RL J. Neurochem. 73:1765-1768(1999).
RN [7]
RP INTERACTION WITH PRKCABP (ISOFORM 1).
RX PubMed=10340301; DOI=10.1016/s0028-3908(98)00230-5;
RA Dev K.K., Nishimune A., Henley J.M., Nakanishi S.;
RT "The protein kinase C alpha binding protein PICK1 interacts with short but
RT not long form alternative splice variants of AMPA receptor subunits.";
RL Neuropharmacology 38:635-644(1999).
RN [8]
RP INTERACTION WITH GRIP1 AND CSPG4.
RX PubMed=12458226; DOI=10.1074/jbc.m210010200;
RA Stegmueller J., Werner H., Nave K.-A., Trotter J.;
RT "The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4-
RT isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate receptor
RT interaction protein (GRIP) in glial progenitor cells. Implications for
RT glial-neuronal signaling.";
RL J. Biol. Chem. 278:3590-3598(2003).
RN [9]
RP PALMITOYLATION AT CYS-610 AND CYS-836.
RX PubMed=16129400; DOI=10.1016/j.neuron.2005.06.035;
RA Hayashi T., Rumbaugh G., Huganir R.L.;
RT "Differential regulation of AMPA receptor subunit trafficking by
RT palmitoylation of two distinct sites.";
RL Neuron 47:709-723(2005).
RN [10]
RP IDENTIFICATION OF ISOFORM 3, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [11]
RP PHOSPHORYLATION AT TYR-876, MUTAGENESIS OF TYR-869; TYR-873 AND TYR-876,
RP SUBCELLULAR LOCATION, INTERACTION WITH GRIP1; GRIP2 AND PICK1, AND TISSUE
RP 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 [12]
RP INTERACTION WITH AP4B1; AP4E1 AND AP4M1, AND SUBCELLULAR LOCATION.
RX PubMed=18341993; DOI=10.1016/j.neuron.2008.02.012;
RA Matsuda S., Miura E., Matsuda K., Kakegawa W., Kohda K., Watanabe M.,
RA Yuzaki M.;
RT "Accumulation of AMPA receptors in autophagosomes in neuronal axons lacking
RT adaptor protein AP-4.";
RL Neuron 57:730-745(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860 AND SER-863, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP INTERACTION WITH GRIA1 AND SYNDIG1.
RX PubMed=20152115; DOI=10.1016/j.neuron.2009.12.021;
RA Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B., Ishimaru T.,
RA Trimmer J.S., Mohapatra D.P., Diaz E.;
RT "SynDIG1: an activity-regulated, AMPA- receptor-interacting transmembrane
RT protein that regulates excitatory synapse development.";
RL Neuron 65:80-93(2010).
RN [15]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [16]
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 [17]
RP INTERACTION WITH SNX27.
RX PubMed=23524343; DOI=10.1038/nm.3117;
RA Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y., Loo L.S., Cai L.,
RA Thompson R.C., Yang B., Chen Y., Johnson P.F., Wu C., Bu G., Mobley W.C.,
RA Zhang D., Gage F.H., Ranscht B., Zhang Y.W., Lipton S.A., Hong W., Xu H.;
RT "Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by
RT modulating glutamate receptor recycling in Down's syndrome.";
RL Nat. Med. 19:473-480(2013).
RN [18]
RP INTERACTION WITH OLFM2.
RX PubMed=25218043; DOI=10.1016/j.expneurol.2014.09.002;
RA Sultana A., Nakaya N., Dong L., Abu-Asab M., Qian H., Tomarev S.I.;
RT "Deletion of olfactomedin 2 induces changes in the AMPA receptor complex
RT and impairs visual, olfactory, and motor functions in mice.";
RL Exp. Neurol. 261:802-811(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 (By similarity). Through complex formation
CC with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and
CC the endosomal sorting of the GRIA2 subunit toward recycling and
CC membrane targeting (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P19491}.
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. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed
CC ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to
CC AMPAR complex disassembly. Interacts with GRIP2. Isoform 1, but not
CC isoform 3, interacts with PICK1/PRKCABP. Interacts with GRIA1 and
CC SYNDIG1. Interacts with LRFN1 (By similarity). Found in a complex with
CC GRIA1, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5,
CC CACNG7 and CACNG8. Interacts with CACNG5 (By similarity). Interacts
CC with SNX27 (via PDZ domain); the interaction is required for recycling
CC to the plasma membrane when endocytosed and prevent degradation in
CC lysosomes. Interacts with OLFM2 (PubMed:25218043). Interacts with
CC AP4B1, AP4E1 and AP4M1; probably indirect it mediates the
CC somatodendritic localization of GRIA2 in neurons (PubMed:18341993).
CC Forms a complex with NSG1, GRIP1 and STX12; controls the intracellular
CC fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward
CC recycling and membrane targeting (By similarity). Interacts with
CC IQSEC1; the interaction is required for ARF6 activation (By
CC similarity). {ECO:0000250|UniProtKB:P19491,
CC ECO:0000269|PubMed:10558890, ECO:0000269|PubMed:12458226,
CC ECO:0000269|PubMed:15240807, ECO:0000269|PubMed:18341993,
CC ECO:0000269|PubMed:20152115, ECO:0000269|PubMed:21496646,
CC ECO:0000269|PubMed:23524343, ECO:0000269|PubMed:25218043}.
CC -!- INTERACTION:
CC P23819; Q8VHY0: Cspg4; NbExp=2; IntAct=EBI-77538, EBI-8327479;
CC P23819; P16858: Gapdh; NbExp=2; IntAct=EBI-77538, EBI-444871;
CC P23819; P23818: Gria1; NbExp=4; IntAct=EBI-77538, EBI-445486;
CC P23819; Q925T6: Grip1; NbExp=5; IntAct=EBI-77538, EBI-537752;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:20547133}; Multi-pass membrane protein
CC {ECO:0000255}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:20547133}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes
CC cell surface expression (By similarity). Displays a somatodendritic
CC localization and is excluded from axons in neurons (PubMed:18341993).
CC {ECO:0000250, ECO:0000269|PubMed:18341993}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P23819-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23819-2; Sequence=VSP_000106, VSP_000107, VSP_000108;
CC Name=3;
CC IsoId=P23819-3; Sequence=VSP_000109, VSP_000110;
CC Name=4;
CC IsoId=P23819-4; Sequence=VSP_000109;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, hippocampus and
CC cerebellum (at protein level). Detected in hippocampus.
CC {ECO:0000269|PubMed:14687553, ECO:0000269|PubMed:15240807,
CC ECO:0000269|PubMed:20547133}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in newborns. Levels
CC increase strongly and are highest in hippocampus from 7 day olds.
CC Detected at low levels in hippocampus and olfactory bulb of 3 month
CC olds (at protein level). {ECO:0000269|PubMed:14687553,
CC ECO:0000269|PubMed:20547133}.
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.
CC ZDHHC3/GODZ specifically palmitoylates Cys-610, which leads to Golgi
CC retention and decreased cell surface expression. In contrast, Cys-836
CC palmitoylation does not affect cell surface expression but regulates
CC stimulation-dependent endocytosis. {ECO:0000269|PubMed:16129400}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:14687553}.
CC -!- PTM: Phosphorylation at Tyr-876 is required forc interaction with
CC IQSEC1 and ARF6 activation. {ECO:0000250|UniProtKB:P19491}.
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.;
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; X57498; CAA40735.1; -; mRNA.
DR EMBL; L32204; AAC37653.1; -; Genomic_DNA.
DR EMBL; L32189; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32190; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32192; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32194; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32196; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32198; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32200; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32202; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32203; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32201; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32199; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32197; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32195; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32193; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32191; AAC37653.1; JOINED; Genomic_DNA.
DR EMBL; L32372; AAC37654.1; -; Genomic_DNA.
DR EMBL; L32189; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32190; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32191; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32192; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32193; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32194; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32195; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32196; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32197; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32198; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32199; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32200; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32201; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32202; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32203; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; L32204; AAC37654.1; JOINED; Genomic_DNA.
DR EMBL; AK014389; BAB29316.1; -; mRNA.
DR EMBL; AK043490; BAC31557.1; -; mRNA.
DR EMBL; AK044574; BAC31986.1; -; mRNA.
DR EMBL; AK046861; BAC32899.1; -; mRNA.
DR CCDS; CCDS17423.1; -. [P23819-1]
DR PIR; I49695; I49695.
DR PIR; I49696; I49696.
DR PDB; 7LDD; EM; 3.40 A; B/D=1-883.
DR PDB; 7LDE; EM; 3.90 A; B/D=1-883.
DR PDB; 7LEP; EM; 3.25 A; B/D=417-840.
DR PDBsum; 7LDD; -.
DR PDBsum; 7LDE; -.
DR PDBsum; 7LEP; -.
DR AlphaFoldDB; P23819; -.
DR SMR; P23819; -.
DR BioGRID; 200059; 23.
DR CORUM; P23819; -.
DR IntAct; P23819; 36.
DR MINT; P23819; -.
DR STRING; 10090.ENSMUSP00000074787; -.
DR ChEMBL; CHEMBL2096617; -.
DR GlyConnect; 2342; 9 N-Linked glycans (3 sites).
DR GlyGen; P23819; 4 sites, 9 N-linked glycans (3 sites).
DR iPTMnet; P23819; -.
DR PhosphoSitePlus; P23819; -.
DR SwissPalm; P23819; -.
DR EPD; P23819; -.
DR MaxQB; P23819; -.
DR PaxDb; P23819; -.
DR PeptideAtlas; P23819; -.
DR PRIDE; P23819; -.
DR ProteomicsDB; 271299; -. [P23819-1]
DR ProteomicsDB; 271300; -. [P23819-2]
DR ProteomicsDB; 271301; -. [P23819-3]
DR ProteomicsDB; 271302; -. [P23819-4]
DR ABCD; P23819; 1 sequenced antibody.
DR UCSC; uc008pof.1; mouse. [P23819-1]
DR MGI; MGI:95809; Gria2.
DR eggNOG; KOG1054; Eukaryota.
DR InParanoid; P23819; -.
DR PhylomeDB; P23819; -.
DR Reactome; R-MMU-399710; Activation of AMPA receptors.
DR Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR BioGRID-ORCS; 14800; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Gria2; mouse.
DR PRO; PR:P23819; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P23819; protein.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0099544; C:perisynaptic space; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:ARUK-UCL.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IDA:MGI.
DR GO; GO:0035254; F:glutamate receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019865; F:immunoglobulin binding; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:MGI.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:MGI.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0051262; P:protein tetramerization; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0001919; P:regulation of receptor recycling; ISO:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISO:MGI.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..883
FT /note="Glutamate receptor 2"
FT /id="PRO_0000011533"
FT TOPO_DOM 25..543
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 565..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 592..607
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 608..610
FT /evidence="ECO:0000250"
FT TOPO_DOM 611..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 638..812
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 813..833
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 834..883
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 867..877
FT /note="Required for interaction with IQSEC1"
FT /evidence="ECO:0000250|UniProtKB:P19491"
FT BINDING 471
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 726
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 683
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P19491"
FT MOD_RES 717
FT /note="Phosphoserine; by PKG"
FT /evidence="ECO:0000250|UniProtKB:P19491"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 876
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:15240807"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10501226"
FT LIPID 610
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:16129400"
FT LIPID 836
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:16129400"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 /evidence="ECO:0000250"
FT DISULFID 739..794
FT /evidence="ECO:0000250"
FT VAR_SEQ 761
FT /note="S -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000106"
FT VAR_SEQ 765..767
FT /note="NAV -> WVE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000107"
FT VAR_SEQ 768..883
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000108"
FT VAR_SEQ 802
FT /note="K -> KTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGSK (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_000109"
FT VAR_SEQ 848..883
FT /note="VAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI -> MTLSAATRNKAR
FT LSITGSTGENGRVMTPEFPKAVHAVPYVSPGMGMNVSVTDLS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_000110"
FT VARIANT 607
FT /note="Q -> R (in RNA edited version)"
FT MUTAGEN 869
FT /note="Y->F: No effect on tyrosine phosphorylation. Reduced
FT tyrosine phosphorylation; when associated with F-873 and F-
FT 876."
FT /evidence="ECO:0000269|PubMed:15240807"
FT MUTAGEN 873
FT /note="Y->F: No effect on tyrosine phosphorylation. Reduced
FT tyrosine phosphorylation; when associated with F-869 and F-
FT 876."
FT /evidence="ECO:0000269|PubMed:15240807"
FT MUTAGEN 876
FT /note="Y->F: Loss of tyrosine phosphorylation at the C-
FT terminus. Reduced tyrosine phosphorylation; when associated
FT with F-869 and F-873. Interferes with accumulation at
FT synapses. Interferes with AMPA-mediated receptor
FT internalization."
FT /evidence="ECO:0000269|PubMed:15240807"
FT CONFLICT 264
FT /note="D -> V (in Ref. 1; CAA40735)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="V -> A (in Ref. 1; CAA40735)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="E -> G (in Ref. 1; CAA40735)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="N -> H (in Ref. 3; BAB29316)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="N -> K (in Ref. 3; BAC31557)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="F -> L (in Ref. 3; BAB29316)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="G -> R (in Ref. 2; AAC37653)"
FT /evidence="ECO:0000305"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 248..253
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 295..316
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:7LEP"
FT TURN 431..435
FT /evidence="ECO:0007829|PDB:7LEP"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:7LEP"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:7LEP"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 544..565
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 594..605
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 618..646
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 657..663
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 665..669
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 675..681
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 686..696
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 707..716
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 717..723
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 727..733
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 765..776
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 779..789
FT /evidence="ECO:0007829|PDB:7LEP"
FT STRAND 798..801
FT /evidence="ECO:0007829|PDB:7LEP"
FT HELIX 810..838
FT /evidence="ECO:0007829|PDB:7LEP"
SQ SEQUENCE 883 AA; 98662 MW; C44B317027C1CCC1 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 NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI
