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

 GRIA2_MOUSE             Reviewed;         883 AA.
P23819; Q61604; Q61605; Q8BG69; Q8BXU3; Q9D6D3;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
02-AUG-2002, sequence version 3.
23-MAY-2018, entry version 183.
RecName: Full=Glutamate receptor 2;
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;
Flags: Precursor;
Name=Gria2; Synonyms=Glur2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1699805; DOI=10.1016/0014-5793(90)80452-O;
Sakimura K., Bujo H., Kushiya E., Araki K., Yamazaki M., Yamazaki M.,
Meguro H., Warashina A., Numa S., Mishina M.;
"Functional expression from cloned cDNAs of glutamate receptor species
responsive to kainate and quisqualate.";
FEBS Lett. 272:73-80(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4).
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=7545935;
Koehler M., Kornau H.-C., Seeburg P.H.;
"The organization of the gene for the functionally dominant alpha-
amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit
GluR-B.";
J. Biol. Chem. 269:17367-17370(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J;
TISSUE=Brain, Cerebellum, Medulla oblongata, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
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).
[5]
INTERACTION WITH MPP4.
PubMed=10558890; DOI=10.1006/bbrc.1999.1723;
Inagaki H., Maeda S., Lin K.H., Shimizu N., Saito T.;
"rDLG6: a novel homolog of Drosophila DLG expressed in rat brain.";
Biochem. Biophys. Res. Commun. 265:462-468(1999).
[6]
PHOSPHORYLATION AT SER-880.
PubMed=10501226; DOI=10.1046/j.1471-4159.1999.731765.x;
Matsuda S., Mikawa S., Hirai H.;
"Phosphorylation of serine-880 in GluR2 by protein kinase C prevents
its C terminus from binding with glutamate receptor-interacting
protein.";
J. Neurochem. 73:1765-1768(1999).
[7]
INTERACTION WITH PRKCABP (ISOFORM 1).
PubMed=10340301; DOI=10.1016/S0028-3908(98)00230-5;
Dev K.K., Nishimune A., Henley J.M., Nakanishi S.;
"The protein kinase C alpha binding protein PICK1 interacts with short
but not long form alternative splice variants of AMPA receptor
subunits.";
Neuropharmacology 38:635-644(1999).
[8]
INTERACTION WITH GRIP1 AND CSPG4.
PubMed=12458226; DOI=10.1074/jbc.M210010200;
Stegmueller J., Werner H., Nave K.-A., Trotter J.;
"The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-
methyl-4-isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate
receptor interaction protein (GRIP) in glial progenitor cells.
Implications for glial-neuronal signaling.";
J. Biol. Chem. 278:3590-3598(2003).
[9]
PALMITOYLATION AT CYS-610 AND CYS-836.
PubMed=16129400; DOI=10.1016/j.neuron.2005.06.035;
Hayashi T., Rumbaugh G., Huganir R.L.;
"Differential regulation of AMPA receptor subunit trafficking by
palmitoylation of two distinct sites.";
Neuron 47:709-723(2005).
[10]
IDENTIFICATION OF ISOFORM 3, GLYCOSYLATION, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
[11]
PHOSPHORYLATION AT TYR-876, MUTAGENESIS OF TYR-869; TYR-873 AND
TYR-876, SUBCELLULAR LOCATION, INTERACTION WITH GRIP1; GRIP2 AND
PICK1, 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).
[12]
INTERACTION WITH AP4B1; AP4E1 AND AP4M1, AND SUBCELLULAR LOCATION.
PubMed=18341993; DOI=10.1016/j.neuron.2008.02.012;
Matsuda S., Miura E., Matsuda K., Kakegawa W., Kohda K., Watanabe M.,
Yuzaki M.;
"Accumulation of AMPA receptors in autophagosomes in neuronal axons
lacking adaptor protein AP-4.";
Neuron 57:730-745(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-860 AND SER-863, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
INTERACTION WITH GRIA1 AND SYNDIG1.
PubMed=20152115; DOI=10.1016/j.neuron.2009.12.021;
Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B.,
Ishimaru T., Trimmer J.S., Mohapatra D.P., Diaz E.;
"SynDIG1: an activity-regulated, AMPA- receptor-interacting
transmembrane protein that regulates excitatory synapse development.";
Neuron 65:80-93(2010).
[15]
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).
[16]
INTERACTION WITH SNX27.
PubMed=23524343; DOI=10.1038/nm.3117;
Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y., Loo L.S.,
Cai L., Thompson R.C., Yang B., Chen Y., Johnson P.F., Wu C., Bu G.,
Mobley W.C., Zhang D., Gage F.H., Ranscht B., Zhang Y.W., Lipton S.A.,
Hong W., Xu H.;
"Loss of sorting nexin 27 contributes to excitatory synaptic
dysfunction by modulating glutamate receptor recycling in Down's
syndrome.";
Nat. Med. 19:473-480(2013).
[17]
INTERACTION WITH OLFM2.
PubMed=25218043; DOI=10.1016/j.expneurol.2014.09.002;
Sultana A., Nakaya N., Dong L., Abu-Asab M., Qian H., Tomarev S.I.;
"Deletion of olfactomedin 2 induces changes in the AMPA receptor
complex and impairs visual, olfactory, and motor functions in mice.";
Exp. Neurol. 261:802-811(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 (By similarity). 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 (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P19491}.
-!- 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. 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 GRIP2.
Isoform 1, but not isoform 3, interacts with PICK1/PRKCABP.
Interacts with GRIA1 and SYNDIG1. Interacts with LRFN1 (By
similarity). Found in a complex with GRIA1, GRIA3, GRIA4, CNIH2,
CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8.
Interacts with CACNG5 (By similarity). Interacts with SNX27 (via
PDZ domain); the interaction is required for recycling to the
plasma membrane when endocytosed and prevent degradation in
lysosomes. Interacts with OLFM2 (PubMed:25218043). Interacts with
AP4B1, AP4E1 and AP4M1; probably indirect it mediates the
somatodendritic localization of GRIA2 in neurons
(PubMed:18341993). Forms a complex with NSG1, GRIP1 and STX12;
controls the intracellular fate of AMPAR and the endosomal sorting
of the GRIA2 subunit toward recycling and membrane targeting (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P19491,
ECO:0000269|PubMed:10558890, ECO:0000269|PubMed:12458226,
ECO:0000269|PubMed:15240807, ECO:0000269|PubMed:18341993,
ECO:0000269|PubMed:20152115, ECO:0000269|PubMed:21496646,
ECO:0000269|PubMed:23524343, ECO:0000269|PubMed:25218043}.
-!- INTERACTION:
Q8VHY0:Cspg4; NbExp=2; IntAct=EBI-77538, EBI-8327479;
P23818:Gria1; NbExp=5; IntAct=EBI-77538, EBI-445486;
Q925T6:Grip1; NbExp=5; IntAct=EBI-77538, EBI-537752;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell
membrane; Multi-pass membrane protein. Note=Interaction with
CACNG2, CNIH2 and CNIH3 promotes cell surface expression (By
similarity). Displays a somatodendritic localization and is
excluded from axons in neurons (PubMed:18341993). {ECO:0000250,
ECO:0000269|PubMed:18341993}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P23819-1; Sequence=Displayed;
Name=2;
IsoId=P23819-2; Sequence=VSP_000106, VSP_000107, VSP_000108;
Name=3;
IsoId=P23819-3; Sequence=VSP_000109, VSP_000110;
Name=4;
IsoId=P23819-4; Sequence=VSP_000109;
-!- TISSUE SPECIFICITY: Detected in brain cortex, hippocampus and
cerebellum (at protein level). Detected in hippocampus.
{ECO:0000269|PubMed:14687553, ECO:0000269|PubMed:15240807}.
-!- DEVELOPMENTAL STAGE: Detected at low levels in newborns. Levels
increase strongly and are highest in hippocampus from 7 day olds.
Detected at low levels in hippocampus and olfactory bulb of 3
month olds (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.
ZDHHC3/GODZ specifically palmitoylates Cys-610, which 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.
{ECO:0000269|PubMed:16129400}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:14687553}.
-!- 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.;
-!- 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}.
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EMBL; X57498; CAA40735.1; -; mRNA.
EMBL; L32204; AAC37653.1; -; Genomic_DNA.
EMBL; L32189; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32190; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32192; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32194; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32196; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32198; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32200; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32202; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32203; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32201; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32199; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32197; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32195; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32193; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32191; AAC37653.1; JOINED; Genomic_DNA.
EMBL; L32372; AAC37654.1; -; Genomic_DNA.
EMBL; L32189; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32190; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32191; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32192; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32193; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32194; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32195; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32196; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32197; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32198; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32199; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32200; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32201; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32202; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32203; AAC37654.1; JOINED; Genomic_DNA.
EMBL; L32204; AAC37654.1; JOINED; Genomic_DNA.
EMBL; AK014389; BAB29316.1; -; mRNA.
EMBL; AK043490; BAC31557.1; -; mRNA.
EMBL; AK044574; BAC31986.1; -; mRNA.
EMBL; AK046861; BAC32899.1; -; mRNA.
CCDS; CCDS17423.1; -. [P23819-1]
PIR; I49695; I49695.
PIR; I49696; I49696.
UniGene; Mm.220224; -.
UniGene; Mm.426957; -.
ProteinModelPortal; P23819; -.
SMR; P23819; -.
BioGrid; 200059; 14.
CORUM; P23819; -.
IntAct; P23819; 35.
MINT; P23819; -.
STRING; 10090.ENSMUSP00000074787; -.
ChEMBL; CHEMBL2096617; -.
iPTMnet; P23819; -.
PhosphoSitePlus; P23819; -.
SwissPalm; P23819; -.
EPD; P23819; -.
MaxQB; P23819; -.
PaxDb; P23819; -.
PeptideAtlas; P23819; -.
PRIDE; P23819; -.
KEGG; mmu:14800; -.
UCSC; uc008pof.1; mouse. [P23819-1]
MGI; MGI:95809; Gria2.
eggNOG; KOG1054; Eukaryota.
eggNOG; ENOG410XPSH; LUCA.
HOGENOM; HOG000234372; -.
HOVERGEN; HBG051839; -.
InParanoid; P23819; -.
KO; K05198; -.
PhylomeDB; P23819; -.
PRO; PR:P23819; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_GRIA2; -.
GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0097060; C:synaptic membrane; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0004971; F:AMPA glutamate receptor activity; ISS:UniProtKB.
GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IDA:MGI.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:MGI.
GO; GO:0015277; F:kainate selective glutamate receptor activity; ISS:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IDA:MGI.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:MGI.
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;
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 24 {ECO:0000255}.
CHAIN 25 883 Glutamate receptor 2.
/FTId=PRO_0000011533.
TOPO_DOM 25 543 Extracellular. {ECO:0000250}.
TRANSMEM 544 564 Helical. {ECO:0000250}.
TOPO_DOM 565 591 Cytoplasmic. {ECO:0000250}.
INTRAMEM 592 607 Helical; Pore-forming. {ECO:0000250}.
INTRAMEM 608 610 {ECO:0000250}.
TOPO_DOM 611 616 Cytoplasmic. {ECO:0000250}.
TRANSMEM 617 637 Helical. {ECO:0000250}.
TOPO_DOM 638 812 Extracellular. {ECO:0000250}.
TRANSMEM 813 833 Helical; Name=M4. {ECO:0000250}.
TOPO_DOM 834 883 Cytoplasmic. {ECO:0000250}.
BINDING 471 471 Glutamate. {ECO:0000250}.
BINDING 506 506 Glutamate. {ECO:0000250}.
BINDING 726 726 Glutamate. {ECO:0000250}.
MOD_RES 683 683 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P19491}.
MOD_RES 717 717 Phosphoserine; by PKG.
{ECO:0000250|UniProtKB:P19491}.
MOD_RES 860 860 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 863 863 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 876 876 Phosphotyrosine.
{ECO:0000269|PubMed:15240807}.
MOD_RES 880 880 Phosphoserine.
{ECO:0000269|PubMed:10501226}.
LIPID 610 610 S-palmitoyl cysteine.
{ECO:0000269|PubMed:16129400}.
LIPID 836 836 S-palmitoyl cysteine.
{ECO:0000269|PubMed:16129400}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 330 {ECO:0000250}.
DISULFID 739 794 {ECO:0000250}.
VAR_SEQ 761 761 S -> T (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_000106.
VAR_SEQ 765 767 NAV -> WVE (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_000107.
VAR_SEQ 768 883 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_000108.
VAR_SEQ 802 802 K -> KTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDS
GSK (in isoform 3 and isoform 4).
{ECO:0000305}.
/FTId=VSP_000109.
VAR_SEQ 848 883 VAKNAQNINPSSSQNSQNFATYKEGYNVYGIESVKI -> M
TLSAATRNKARLSITGSTGENGRVMTPEFPKAVHAVPYVSP
GMGMNVSVTDLS (in isoform 3).
{ECO:0000305}.
/FTId=VSP_000110.
VARIANT 607 607 Q -> R (in RNA edited version).
MUTAGEN 869 869 Y->F: No effect on tyrosine
phosphorylation. Reduced tyrosine
phosphorylation; when associated with F-
873 and F-876.
{ECO:0000269|PubMed:15240807}.
MUTAGEN 873 873 Y->F: No effect on tyrosine
phosphorylation. Reduced tyrosine
phosphorylation; when associated with F-
869 and F-876.
{ECO:0000269|PubMed:15240807}.
MUTAGEN 876 876 Y->F: Loss of tyrosine phosphorylation at
the C-terminus. Reduced tyrosine
phosphorylation; when associated with F-
869 and F-873. Interferes with
accumulation at synapses. Interferes with
AMPA-mediated receptor internalization.
{ECO:0000269|PubMed:15240807}.
CONFLICT 264 264 D -> V (in Ref. 1; CAA40735).
{ECO:0000305}.
CONFLICT 270 270 V -> A (in Ref. 1; CAA40735).
{ECO:0000305}.
CONFLICT 282 282 E -> G (in Ref. 1; CAA40735).
{ECO:0000305}.
CONFLICT 374 374 N -> H (in Ref. 3; BAB29316).
{ECO:0000305}.
CONFLICT 482 482 N -> K (in Ref. 3; BAC31557).
{ECO:0000305}.
CONFLICT 552 552 F -> L (in Ref. 3; BAB29316).
{ECO:0000305}.
CONFLICT 764 764 G -> R (in Ref. 2; AAC37653).
{ECO:0000305}.
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


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