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 27-MAR-2024, entry version 211. 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; RC 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 a ligand-gated ion CC channel in the central nervous system and plays an important role in CC excitatory synaptic transmission. L-glutamate acts as an excitatory CC neurotransmitter at many synapses in the central nervous system. CC Binding of the excitatory neurotransmitter L-glutamate induces a CC conformation change, leading to the opening of the cation channel, and CC thereby converts the chemical signal to an electrical impulse. The CC receptor then desensitizes rapidly and enters a transient inactive CC state, characterized by the presence of bound agonist. In the presence CC of CACNG4 or CACNG7 or CACNG8, shows resensitization which is CC characterized by a delayed accumulation of current flux upon continued CC application of glutamate (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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 EMDB; EMD-23285; -. DR EMDB; EMD-23286; -. DR EMDB; EMD-23287; -. DR EMDB; EMD-23288; -. DR EMDB; EMD-23292; -. DR SMR; P23819; -. DR BioGRID; 200059; 161. 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 GlyCosmos; P23819; 4 sites, 9 glycans. DR GlyGen; P23819; 5 sites, 9 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P23819; -. DR MetOSite; P23819; -. DR PhosphoSitePlus; P23819; -. DR SwissPalm; P23819; -. DR EPD; P23819; -. DR MaxQB; P23819; -. DR PaxDb; 10090-ENSMUSP00000074787; -. DR PeptideAtlas; 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 AGR; MGI:95809; -. 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 76 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:0032279; C:asymmetric synapse; ISO:MGI. DR GO; GO:0030424; C:axon; 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:0032590; C:dendrite membrane; ISO:MGI. DR GO; GO:0043198; C:dendritic shaft; ISO:MGI. DR GO; GO:0043197; C:dendritic spine; ISO:MGI. DR GO; GO:0044327; C:dendritic spine head; ISO:MGI. DR GO; GO:0044326; C:dendritic spine neck; 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: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:0098793; C:presynapse; ISO:MGI. DR GO; GO:0048787; C:presynaptic active zone membrane; ISO: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; IDA:SynGO. DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB. DR GO; GO:0106033; C:spine synapse; ISO:MGI. 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: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:0004970; F:glutamate-gated receptor activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0019865; F:immunoglobulin binding; ISO:MGI. DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI. DR GO; GO:0015277; F:kainate selective glutamate receptor activity; ISS:UniProtKB. DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI. DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0097110; F:scaffold protein 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 monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO. DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; ISO:MGI. DR GO; GO:1905430; P:cellular response to glycine; ISO:MGI. 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:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central. 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 GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central. DR CDD; cd06389; PBP1_iGluR_AMPA_GluR2; 1. DR CDD; cd13715; PBP2_iGluR_AMPA; 1. DR Gene3D; 1.10.287.70; -; 2. DR Gene3D; 3.40.50.2300; -; 2. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2. DR InterPro; IPR001828; ANF_lig-bd_rcpt. DR InterPro; IPR019594; Glu/Gly-bd. DR InterPro; IPR001508; Iono_Glu_rcpt_met. DR InterPro; IPR015683; Ionotropic_Glu_rcpt. DR InterPro; IPR001320; Iontro_rcpt_C. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR PANTHER; PTHR18966:SF99; GLUTAMATE RECEPTOR 2; 1. DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00060; Lig_chan; 1. DR Pfam; PF10613; Lig_chan-Glu_bd; 1. DR Pfam; PF00497; SBP_bac_3; 1. DR PRINTS; PR00177; NMDARECEPTOR. DR SMART; SM00918; Lig_chan-Glu_bd; 1. DR SMART; SM00079; PBPe; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport; KW Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing; KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport; KW Ubl conjugation. FT SIGNAL 1..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 FT F-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 FT F-876." FT /evidence="ECO:0000269|PubMed:15240807" FT MUTAGEN 876 FT /note="Y->F: Loss of tyrosine phosphorylation at the FT C-terminus. Reduced tyrosine phosphorylation; when FT associated with F-869 and F-873. Interferes with FT accumulation at synapses. Interferes with AMPA-mediated FT receptor 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 //