NMDE2_MOUSE
ID NMDE2_MOUSE Reviewed; 1482 AA.
AC Q01097; Q9DCB2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 2B;
DE Short=GluN2B;
DE AltName: Full=Glutamate [NMDA] receptor subunit epsilon-2 {ECO:0000303|PubMed:1377365};
DE AltName: Full=N-methyl D-aspartate receptor subtype 2B;
DE Short=NMDAR2B;
DE Short=NR2B {ECO:0000303|PubMed:31424425};
DE Flags: Precursor;
GN Name=Grin2b;
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], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RX PubMed=1377365; DOI=10.1038/358036a0;
RA Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E., Araki K.,
RA Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.;
RT "Molecular diversity of the NMDA receptor channel.";
RL Nature 358:36-41(1992).
RN [2]
RP SEQUENCE REVISION.
RA Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E., Araki K.,
RA Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=8789948; DOI=10.1016/s0896-6273(00)80051-3;
RA Kutsuwada T., Sakimura K., Manabe T., Takayama C., Katakura N., Kushiya E.,
RA Natsume R., Watanabe M., Inoue Y., Yagi T., Aizawa S., Arakawa M.,
RA Takahashi T., Nakamura Y., Mori H., Mishina M.;
RT "Impairment of suckling response, trigeminal neuronal pattern formation,
RT and hippocampal LTD in NMDA receptor epsilon 2 subunit mutant mice.";
RL Neuron 16:333-344(1996).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=10846156; DOI=10.1126/science.288.5472.1796;
RA Setou M., Nakagawa T., Seog D.-H., Hirokawa N.;
RT "Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-
RT containing vesicle transport.";
RL Science 288:1796-1802(2000).
RN [6]
RP PHOSPHORYLATION AT TYR-1472.
RX PubMed=12451687;
RA Nakazawa T., Tezuka T., Yamamoto T.;
RT "Regulation of NMDA receptor function by Fyn-mediated tyrosine
RT phosphorylation.";
RL Nihon Shinkei Seishin Yakurigaku Zasshi 22:165-167(2002).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
RX PubMed=12008020; DOI=10.1016/s0169-328x(02)00173-0;
RA Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.;
RT "Cloning and characterization of a novel NMDA receptor subunit NR3B: a
RT dominant subunit that reduces calcium permeability.";
RL Brain Res. Mol. Brain Res. 100:43-52(2002).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
RX PubMed=14602821; DOI=10.1523/jneurosci.23-31-10064.2003;
RA Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
RT "Specific assembly with the NMDA receptor 3B subunit controls surface
RT expression and calcium permeability of NMDA receptors.";
RL J. Neurosci. 23:10064-10073(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP INTERACTION WITH HIP1.
RX PubMed=17329427; DOI=10.1523/jneurosci.5175-06.2007;
RA Metzler M., Gan L., Wong T.P., Liu L., Helm J., Liu L., Georgiou J.,
RA Wang Y., Bissada N., Cheng K., Roder J.C., Wang Y.T., Hayden M.R.;
RT "NMDA receptor function and NMDA receptor-dependent phosphorylation of
RT huntingtin is altered by the endocytic protein HIP1.";
RL J. Neurosci. 27:2298-2308(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-962; TYR-1039; TYR-1109;
RP TYR-1133 AND TYR-1155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [13]
RP INTERACTION WITH NETO1.
RX PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
RA Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M., Clapcote S.J.,
RA Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M., Roder J.C.,
RA Salter M.W., McInnes R.R.;
RT "Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for
RT synaptic plasticity and learning.";
RL PLoS Biol. 7:E41-E41(2009).
RN [14]
RP FUNCTION, PHOSPHORYLATION AT SER-1303, AND INTERACTION WITH DAPK1.
RX PubMed=20141836; DOI=10.1016/j.cell.2009.12.055;
RA Tu W., Xu X., Peng L., Zhong X., Zhang W., Soundarapandian M.M., Balel C.,
RA Wang M., Jia N., Zhang W., Lew F., Chan S.L., Chen Y., Lu Y.;
RT "DAPK1 interaction with NMDA receptor NR2B subunits mediates brain damage
RT in stroke.";
RL Cell 140:222-234(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-917; SER-920;
RP SER-1058; SER-1061; SER-1064; SER-1143; SER-1255; SER-1259 AND SER-1303,
RP AND 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 [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=26912815; DOI=10.1124/mol.115.103036;
RA Stroebel D., Buhl D.L., Knafels J.D., Chanda P.K., Green M., Sciabola S.,
RA Mony L., Paoletti P., Pandit J.;
RT "A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor GluN2B-
RT selective Antagonists.";
RL Mol. Pharmacol. 89:541-551(2016).
RN [17]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMEM25.
RX PubMed=31424425; DOI=10.1172/jci122599;
RA Zhang H., Tian X., Lu X., Xu D., Guo Y., Dong Z., Li Y., Ma Y., Chen C.,
RA Yang Y., Yang M., Yang Y., Liu F., Zhou R., He M., Xiao F., Wang X.;
RT "TMEM25 modulates neuronal excitability and NMDA receptor subunit NR2B
RT degradation.";
RL J. Clin. Invest. 129:3864-3876(2019).
CC -!- FUNCTION: Component of NMDA receptor complexes that function as
CC heterotetrameric, ligand-gated ion channels with high calcium
CC permeability and voltage-dependent sensitivity to magnesium. Channel
CC activation requires binding of the neurotransmitter glutamate to the
CC epsilon subunit, glycine binding to the zeta subunit, plus membrane
CC depolarization to eliminate channel inhibition by Mg(2+)
CC (PubMed:1377365, PubMed:26912815). Sensitivity to glutamate and channel
CC kinetics depend on the subunit composition (PubMed:1377365). In concert
CC with DAPK1 at extrasynaptic sites, acts as a central mediator for
CC stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances
CC synaptic NMDA receptor channel activity inducing injurious Ca2+ influx
CC through them, resulting in an irreversible neuronal death
CC (PubMed:20141836). Contributes to neural pattern formation in the
CC developing brain (PubMed:8789948). Plays a role in long-term depression
CC (LTD) of hippocampus membrane currents and in synaptic plasticity
CC (PubMed:8789948). {ECO:0000269|PubMed:1377365,
CC ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:26912815,
CC ECO:0000269|PubMed:8789948}.
CC -!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed of
CC two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A, GRIN2B,
CC GRIN2C or GRIN2D) (in vitro) (PubMed:1377365, PubMed:26912815). Can
CC also form heterotetrameric channels that contain at least one zeta
CC subunit (GRIN1), at least one epsilon subunit, plus GRIN3A or GRIN3B
CC (PubMed:12008020, PubMed:14602821). In vivo, the subunit composition
CC may depend on the expression levels of the different subunits
CC (Probable). Found in a complex with GRIN1, GRIN3A and PPP2CB (By
CC similarity). Found in a complex with GRIN1 and GRIN3B (PubMed:12008020,
CC PubMed:14602821). Interacts with MAGI3 (By similarity). Interacts with
CC HIP1 and NETO1 (PubMed:17329427, PubMed:19243221). Interacts with PDZ
CC domains of PATJ, DLG3 and DLG4. Interacts with DAPK1 (PubMed:20141836).
CC Found in a complex with GRIN1 and PRR7. Interacts with PRR7 (By
CC similarity). Interacts with CAMK2A (By similarity). Interacts with ARC;
CC preventing ARC oligomerization (By similarity). Interacts with TMEM25
CC (PubMed:31424425). {ECO:0000250|UniProtKB:Q00960,
CC ECO:0000250|UniProtKB:Q13224, ECO:0000269|PubMed:12008020,
CC ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:14602821,
CC ECO:0000269|PubMed:17329427, ECO:0000269|PubMed:19243221,
CC ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:26912815,
CC ECO:0000269|PubMed:31424425}.
CC -!- INTERACTION:
CC Q01097; Q9JI91: Actn2; NbExp=2; IntAct=EBI-400125, EBI-299169;
CC Q01097; P17426: Ap2a1; NbExp=2; IntAct=EBI-400125, EBI-775189;
CC Q01097; P11798: Camk2a; NbExp=5; IntAct=EBI-400125, EBI-400384;
CC Q01097; Q80YE7: Dapk1; NbExp=8; IntAct=EBI-400125, EBI-2584874;
CC Q01097; Q62108: Dlg4; NbExp=19; IntAct=EBI-400125, EBI-300895;
CC Q01097; P35438: Grin1; NbExp=11; IntAct=EBI-400125, EBI-400084;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1377365,
CC ECO:0000269|PubMed:26912815}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q00960}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q00960}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q00960}. Late endosome
CC {ECO:0000269|PubMed:31424425}. Lysosome {ECO:0000269|PubMed:31424425}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10846156}. Note=Co-
CC localizes with the motor protein KIF17 along microtubules.
CC {ECO:0000269|PubMed:10846156}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level)
CC (PubMed:8789948). Detected throughout the brain, and in brain stem
CC trigeminal nucleus (PubMed:8789948). Detected in forebrain
CC (PubMed:1377365). {ECO:0000269|PubMed:1377365,
CC ECO:0000269|PubMed:8789948}.
CC -!- DOMAIN: A hydrophobic region that gives rise to the prediction of a
CC transmembrane span does not cross the membrane, but is part of a
CC discontinuously helical region that dips into the membrane and is
CC probably part of the pore and of the selectivity filter.
CC {ECO:0000250|UniProtKB:Q00960}.
CC -!- PTM: Phosphorylated on tyrosine residues (PubMed:12451687).
CC Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor
CC channel activity (PubMed:20141836). {ECO:0000269|PubMed:12451687,
CC ECO:0000269|PubMed:20141836}.
CC -!- DISRUPTION PHENOTYPE: Mutant pups are born at the expected Mendelian
CC rate and appear grossly normal, but lack suckling behavior. As a
CC consequence, all die shortly after birth, except when they are fed
CC manually via a soft tube that delivers milk directly into the stomach.
CC While mutant neonate brain structures are grossly normal, the mutant
CC brain stem trigeminal complex lacks the neural repeating units called
CC barrelettes that correspond to whisker-associated nerve fibers. Primary
CC afferent nerve fibers from whiskers fail to show normal clustering in
CC the region where barrelette structures form in wild-type. In contrast,
CC nasolabial motor neurons appear normal. Contrary to wild-type neonates,
CC brain slices from the mutant neonate hippocampus CA1 region lack NMDA
CC receptor-type ion channel activity. Contrary to wild-type pups,
CC prolonged low frequency stimulation of afferent fibers does not induce
CC long-term depression (LTD) in the hippocampus.
CC {ECO:0000269|PubMed:8789948}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR2B/GRIN2B subfamily. {ECO:0000305}.
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DR EMBL; D10651; BAA01498.2; -; mRNA.
DR EMBL; AK002963; BAB22483.1; -; mRNA.
DR CCDS; CCDS20648.1; -.
DR PIR; I49704; I49704.
DR RefSeq; NP_032197.3; NM_008171.3.
DR AlphaFoldDB; Q01097; -.
DR SMR; Q01097; -.
DR BioGRID; 200069; 84.
DR ComplexPortal; CPX-291; NMDA receptor complex, GluN1-GluN2B.
DR ComplexPortal; CPX-296; NMDA receptor complex, GluN1-GluN2A-GluN2B.
DR CORUM; Q01097; -.
DR DIP; DIP-31568N; -.
DR IntAct; Q01097; 43.
DR MINT; Q01097; -.
DR STRING; 10090.ENSMUSP00000062284; -.
DR BindingDB; Q01097; -.
DR ChEMBL; CHEMBL3442; -.
DR GlyConnect; 2351; 11 N-Linked glycans (6 sites).
DR GlyGen; Q01097; 7 sites, 11 N-linked glycans (6 sites).
DR iPTMnet; Q01097; -.
DR PhosphoSitePlus; Q01097; -.
DR SwissPalm; Q01097; -.
DR CPTAC; non-CPTAC-4053; -.
DR MaxQB; Q01097; -.
DR PaxDb; Q01097; -.
DR PRIDE; Q01097; -.
DR ProteomicsDB; 293864; -.
DR ABCD; Q01097; 3 sequenced antibodies.
DR DNASU; 14812; -.
DR GeneID; 14812; -.
DR KEGG; mmu:14812; -.
DR CTD; 2904; -.
DR MGI; MGI:95821; Grin2b.
DR eggNOG; KOG1053; Eukaryota.
DR InParanoid; Q01097; -.
DR PhylomeDB; Q01097; -.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-MMU-9609736; Assembly and cell surface presentation of NMDA receptors.
DR BioGRID-ORCS; 14812; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Grin2b; mouse.
DR PRO; PR:Q01097; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q01097; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0044307; C:dendritic branch; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
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:0017146; C:NMDA selective glutamate receptor complex; IPI:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:ParkinsonsUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-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; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; IDA:ARUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IMP:MGI.
DR GO; GO:0005261; F:cation channel activity; IGI:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0031749; F:D2 dopamine receptor binding; ISO:MGI.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISO:MGI.
DR GO; GO:0016595; F:glutamate binding; ISS:UniProtKB.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
DR GO; GO:0016594; F:glycine binding; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0005149; F:interleukin-1 receptor binding; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0042165; F:neurotransmitter binding; ISO:MGI.
DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0099529; F:neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IMP: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; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0036094; F:small molecule binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0001508; P:action potential; ISO:MGI.
DR GO; GO:0008306; P:associative learning; ISO:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0098655; P:cation transmembrane transport; IC:ComplexPortal.
DR GO; GO:0006812; P:cation transport; IGI:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0042596; P:fear response; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0007612; P:learning; IDA:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0007613; P:memory; IDA:MGI.
DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IGI:ARUK-UCL.
DR GO; GO:0098989; P:NMDA selective glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISO:MGI.
DR GO; GO:1904062; P:regulation of cation transmembrane transport; IC:ComplexPortal.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; TAS:UniProtKB.
DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:MGI.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR GO; GO:0048511; P:rhythmic process; ISO:MGI.
DR GO; GO:0046960; P:sensitization; ISO:MGI.
DR GO; GO:0007423; P:sensory organ development; IMP:MGI.
DR GO; GO:0001964; P:startle response; IMP:MGI.
DR GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR DisProt; DP01492; -.
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; IPR018884; NMDAR2_C.
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 Pfam; PF10565; NMDAR2_C; 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 Calcium; Cell membrane; Cytoplasm; Cytoskeleton; Disulfide bond; Endosome;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Lysosome; Magnesium; Membrane; Metal-binding; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1482
FT /note="Glutamate receptor ionotropic, NMDA 2B"
FT /id="PRO_0000011578"
FT TOPO_DOM 27..557
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 558..576
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 577..603
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT INTRAMEM 604..623
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 624..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 631..646
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 647..817
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TRANSMEM 818..837
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT TOPO_DOM 838..1482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT REGION 604..623
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:A7XY94"
FT REGION 1074..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1304
FT /note="Interaction with DAPK1"
FT /evidence="ECO:0000269|PubMed:20141836"
FT MOTIF 1480..1482
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 1079..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT BINDING 514
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT BINDING 519
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT BINDING 690..691
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT BINDING 732
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT SITE 615
FT /note="Functional determinant of NMDA receptors"
FT /evidence="ECO:0000250"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 962
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1039
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1061
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1109
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1133
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1155
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1303
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000269|PubMed:20141836,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1472
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12451687"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 86..321
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT DISULFID 429..456
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT DISULFID 436..457
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT DISULFID 746..801
FT /evidence="ECO:0000250|UniProtKB:Q00960"
FT CONFLICT 99
FT /note="L -> F (in Ref. 3; BAB22483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1482 AA; 165959 MW; B8C3FA10E9A4B36D CRC64;
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SAPSIGIAVI LVGTSDEVAI KDAHEKDDFH
HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVLA DDTDQEAIAQ ILDFISAQTL
TPILGIHGGS SMIMADKDES SMFFQFGPSI EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ
DFVNKIRSTI ENSFVGWELE EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI
FEVANSVGLT GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS FSEDGYQMHP
KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE QEDDHLSIVT LEEAPFVIVE
SVDPLSGTCM RNTVPCQKRI ISENKTDEEP GYIKKCCKGF CIDILKKISK SVKFTYDLYL
VTNGKHGKKI NGTWNGMIGE VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR
SNGTVSPSAF LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL AAFMIQEEYV
DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA EMHAYMGKFN QRGVDDALLS
LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT IGSGKVFAST GYGIAIQKDS GWKRQVDLAI
LQLFGDGEME ELEALWLTGI CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH
LFYWQFRHCF MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN NPPCEENLFS
DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSTSSI DGLYDCDNPP FTTQPRSISK
KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS GHDDLIRSDV SDISTHTVTY GNIEGNAAKR
RKQQYKDSLK KRPASAKSRR EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK
ENSPHWEHVD LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGDKHGVV GGVPAPWEKN
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN LYDISEDNSL
QELDQPAAPV AVSSNASTTK YPQSPTNSKA QKKNRNKLRR QHSYDTFVDL QKEEAALAPR
SVSLKDKGRF MDGSPYAHMF EMPAGESSFA NKSSVTTAGH HHNNPGSGYM LSKSLYPDRV
TQNPFIPTFG DDQCLLHGSK SYFFRQPTVA GASKTRPDFR ALVTNKPVVS ALHGAVPGRF
QKDICIGNQS NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV
