NMDE1_MOUSE
ID NMDE1_MOUSE Reviewed; 1464 AA.
AC P35436;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 2A;
DE Short=GluN2A;
DE AltName: Full=Glutamate [NMDA] receptor subunit epsilon-1 {ECO:0000303|PubMed:1374164};
DE AltName: Full=N-methyl D-aspartate receptor subtype 2A;
DE Short=NMDAR2A;
DE Short=NR2A {ECO:0000303|PubMed:8987814};
DE Flags: Precursor;
GN Name=Grin2a;
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=1374164; DOI=10.1038/357070a0;
RA Meguro H., Mori H., Araki K., Kushiya E., Kutsuwada T., Yamazaki M.,
RA Kumanishi T., Arakawa M., Sakimura K., Mishina M.;
RT "Functional characterization of a heteromeric NMDA receptor channel
RT expressed from cloned cDNAs.";
RL Nature 357:70-74(1992).
RN [2]
RP SEQUENCE REVISION TO 384.
RA Meguro H., Mori H., Araki K., Kushiya E., Kutsuwada T., Yamazaki M.,
RA Kumanishi T., Arakawa M., Sakimura K., Mishina M.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7816096; DOI=10.1038/373151a0;
RA Sakimura K., Kutsuwada T., Ito I., Manabe T., Takayama C., Kushiya E.,
RA Yagi T., Aizawa S., Inoue Y., Sugiyama H.;
RT "Reduced hippocampal LTP and spatial learning in mice lacking NMDA receptor
RT epsilon 1 subunit.";
RL Nature 373:151-155(1995).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8987814; DOI=10.1523/jneurosci.16-24-07859.1996;
RA Kadotani H., Hirano T., Masugi M., Nakamura K., Nakao K., Katsuki M.,
RA Nakanishi S.;
RT "Motor discoordination results from combined gene disruption of the NMDA
RT receptor NR2A and NR2C subunits, but not from single disruption of the NR2A
RT or NR2C subunit.";
RL J. Neurosci. 16:7859-7867(1996).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929 AND
RP SER-1059, 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 [10]
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 [11]
RP INTERACTION WITH SORCS2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28469074; DOI=10.1172/jci.insight.88995;
RA Ma Q., Yang J., Milner T.A., Vonsattel J.G., Palko M.E., Tessarollo L.,
RA Hempstead B.L.;
RT "SorCS2-mediated NR2A trafficking regulates motor deficits in Huntington's
RT disease.";
RL JCI Insight 2:0-0(2017).
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
CC (PubMed:1374164). Channel activation requires binding of the
CC neurotransmitter glutamate to the epsilon subunit, glycine binding to
CC the zeta subunit, plus membrane depolarization to eliminate channel
CC inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics
CC depend on the subunit composition; channels containing GRIN1 and GRIN2A
CC have lower sensitivity to glutamate and faster deactivation kinetics
CC than channels formed by GRIN1 and GRIN2B (By similarity). Contributes
CC to the slow phase of excitatory postsynaptic current, long-term
CC synaptic potentiation, and learning (PubMed:7816096, PubMed:8987814).
CC {ECO:0000250|UniProtKB:Q00959, ECO:0000269|PubMed:1374164,
CC ECO:0000269|PubMed:7816096, ECO:0000269|PubMed:8987814}.
CC -!- SUBUNIT: Heterotetramer (By similarity). Forms heterotetrameric
CC channels composed of two zeta subunits (GRIN1), and two epsilon
CC subunits (GRIN2A, GRIN2B, GRIN2C or GRIN2D) (in vitro)
CC (PubMed:1374164). Can also form heterotetrameric channels that contain
CC at least one zeta subunit (GRIN1), at least one epsilon subunit, plus
CC GRIN3A or GRIN3B (PubMed:12008020). In vivo, the subunit composition
CC may depend on the expression levels of the different subunits. Found in
CC a complex with GRIN1, GRIN3A and PPP2CB (By similarity). Found in a
CC complex with GRIN1 and GRIN3B (PubMed:12008020). Interacts with AIP1
CC (By similarity). Interacts with HIP1 and NETO1 (PubMed:17329427,
CC PubMed:19243221). Interacts with SNX27 (via PDZ domain); the
CC interaction is required for recycling to the plasma membrane when
CC endocytosed and prevent degradation in lysosomes (PubMed:23524343).
CC Interacts with PDZ domains of PATJ and DLG4. Interacts with LRFN2 (By
CC similarity). Interacts with RPH3A and DLG4; this ternary complex
CC regulates NMDA receptor composition at postsynaptic membranes (By
CC similarity). Interacts with SORCS2 (PubMed:28469074). Interacts with
CC ARC; preventing ARC oligomerization (By similarity).
CC {ECO:0000250|UniProtKB:Q00959, ECO:0000269|PubMed:12008020,
CC ECO:0000269|PubMed:1374164, ECO:0000269|PubMed:17329427,
CC ECO:0000269|PubMed:19243221, ECO:0000269|PubMed:23524343,
CC ECO:0000269|PubMed:28469074}.
CC -!- INTERACTION:
CC P35436; Q62108: Dlg4; NbExp=15; IntAct=EBI-400115, EBI-300895;
CC P35436; Q9D415: Dlgap1; NbExp=2; IntAct=EBI-400115, EBI-400152;
CC P35436; Q63ZW7: Patj; NbExp=4; IntAct=EBI-400115, EBI-8366894;
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000269|PubMed:28469074}. Cell membrane
CC {ECO:0000269|PubMed:1374164, ECO:0000269|PubMed:28469074}; Multi-pass
CC membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:28469074}.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00959}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:Q00959}. Cytoplasmic vesicle
CC membrane {ECO:0000269|PubMed:28469074}. Note=Expression at the dendrite
CC cell membrane and at synapses is regulated by SORCS2 and the retromer
CC complex. {ECO:0000269|PubMed:28469074}.
CC -!- TISSUE SPECIFICITY: Detected in striatum (PubMed:28469074). Detected in
CC forbrain (PubMed:7816096). Detected in cerebellum (at protein level)
CC (PubMed:8987814). Detected in brain cortex, piriform cortex,
CC hippocampus, caudate-putamen, dentate gyrus and granule cell layer
CC (PubMed:1374164, PubMed:7816096). {ECO:0000269|PubMed:1374164,
CC ECO:0000269|PubMed:28469074, ECO:0000269|PubMed:7816096,
CC ECO:0000269|PubMed:8987814}.
CC -!- DOMAIN: Contains an N-terminal domain, a ligand-binding domain and a
CC transmembrane domain. Agonist binding to the extracellular ligand-
CC binding domains triggers channel gating.
CC {ECO:0000250|UniProtKB:Q00959}.
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:B7ZSK1}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice appear grossly normal and are fertile
CC (PubMed:7816096, PubMed:8987814). NMDA channel currents are decreased
CC in mutant brain slices. Contrary to wild-type, where tetanic
CC stimulation leads to a strong long-term increase in synaptic strength,
CC only modest long-term synaptic potentiation is seen in mutant mice
CC (PubMed:7816096). Mossy fiber granule cells from mutant mice present a
CC decrease of the slow component of the excitatory postsynaptic current
CC (PubMed:8987814). The slow component of the excitatory postsynaptic
CC current is nearly abolished in mossy fiber cells from mice lacking both
CC Grin2a and Grin2c (PubMed:8987814). Mutant mice present subtle deficits
CC in spatial learning (PubMed:7816096). Mice lacking both Grin2a and
CC Grin2c display subtle motor deficits; they have no visible phenotype
CC when performing simple tasks, but have decreased ability to walk across
CC a narrow wooden bar, and are unable to stay on a rapidly rotating rod
CC (PubMed:8987814). {ECO:0000269|PubMed:7816096,
CC ECO:0000269|PubMed:8987814}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR2A/GRIN2A 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; D10217; BAA01069.2; -; mRNA.
DR CCDS; CCDS27943.1; -.
DR PIR; S29159; S29159.
DR RefSeq; NP_032196.2; NM_008170.2.
DR RefSeq; XP_006521857.1; XM_006521794.3.
DR AlphaFoldDB; P35436; -.
DR SMR; P35436; -.
DR BioGRID; 200068; 29.
DR ComplexPortal; CPX-290; NMDA receptor complex, GluN1-GluN2A.
DR ComplexPortal; CPX-296; NMDA receptor complex, GluN1-GluN2A-GluN2B.
DR CORUM; P35436; -.
DR DIP; DIP-31567N; -.
DR IntAct; P35436; 17.
DR MINT; P35436; -.
DR STRING; 10090.ENSMUSP00000111501; -.
DR ChEMBL; CHEMBL3832634; -.
DR GlyConnect; 2350; 1 N-Linked glycan (3 sites).
DR GlyGen; P35436; 7 sites, 1 N-linked glycan (3 sites).
DR iPTMnet; P35436; -.
DR PhosphoSitePlus; P35436; -.
DR SwissPalm; P35436; -.
DR CPTAC; non-CPTAC-3341; -.
DR CPTAC; non-CPTAC-3342; -.
DR PaxDb; P35436; -.
DR PeptideAtlas; P35436; -.
DR PRIDE; P35436; -.
DR ProteomicsDB; 293690; -.
DR ABCD; P35436; 2 sequenced antibodies.
DR Antibodypedia; 1402; 778 antibodies from 41 providers.
DR DNASU; 14811; -.
DR Ensembl; ENSMUST00000032331; ENSMUSP00000032331; ENSMUSG00000059003.
DR Ensembl; ENSMUST00000115835; ENSMUSP00000111501; ENSMUSG00000059003.
DR Ensembl; ENSMUST00000199708; ENSMUSP00000142900; ENSMUSG00000059003.
DR GeneID; 14811; -.
DR KEGG; mmu:14811; -.
DR UCSC; uc007ydc.1; mouse.
DR CTD; 2903; -.
DR MGI; MGI:95820; Grin2a.
DR VEuPathDB; HostDB:ENSMUSG00000059003; -.
DR eggNOG; KOG1053; Eukaryota.
DR GeneTree; ENSGT00940000156222; -.
DR InParanoid; P35436; -.
DR OMA; FPDAYQD; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P35436; -.
DR TreeFam; TF314731; -.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
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; 14811; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Grin2a; mouse.
DR PRO; PR:P35436; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P35436; protein.
DR Bgee; ENSMUSG00000059003; Expressed in CA1 field of hippocampus and 120 other tissues.
DR Genevisible; P35436; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
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:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
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:MGI.
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: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:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IMP:MGI.
DR GO; GO:0005261; F:cation channel activity; IMP:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISO:MGI.
DR GO; GO:0016595; F:glutamate binding; ISO:MGI.
DR GO; GO:0035254; F:glutamate receptor binding; ISO:MGI.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI.
DR GO; GO:0042165; F:neurotransmitter binding; ISO:MGI.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IMP: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; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor 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:0022843; F:voltage-gated cation channel activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0001508; P:action potential; ISO: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; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:MGI.
DR GO; GO:0071294; P:cellular response to zinc ion; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0097061; P:dendritic spine organization; ISO:MGI.
DR GO; GO:0033058; P:directional locomotion; IGI:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0040011; P:locomotion; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; TAS:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IGI:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; IGI:MGI.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; IMP:MGI.
DR GO; GO:1904062; P:regulation of cation transmembrane transport; ISO:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IC:ComplexPortal.
DR GO; GO:2000310; P:regulation of NMDA receptor activity; ISO:MGI.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0048511; P:rhythmic process; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
DR GO; GO:0030431; P:sleep; IMP:MGI.
DR GO; GO:0001964; P:startle response; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP: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; 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; Cell projection; Cytoplasmic vesicle;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1464
FT /note="Glutamate receptor ionotropic, NMDA 2A"
FT /id="PRO_0000011574"
FT TOPO_DOM 23..555
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT TOPO_DOM 577..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 601..620
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT TOPO_DOM 621..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 626..645
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT TOPO_DOM 646..816
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT TOPO_DOM 838..1464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 599..620
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:B7ZSK1"
FT REGION 1021..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1462..1464
FT /note="PDZ-binding"
FT /evidence="ECO:0000305"
FT COMPBIAS 1035..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 511..513
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 518
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 689..690
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT BINDING 730..731
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT SITE 614
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 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
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 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..320
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT DISULFID 429..455
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT DISULFID 436..456
FT /evidence="ECO:0000250|UniProtKB:Q00959"
FT DISULFID 745..800
FT /evidence="ECO:0000250|UniProtKB:Q00959"
SQ SEQUENCE 1464 AA; 165421 MW; 438986DD5666C152 CRC64;
MGRLGYWTLL VLPALLVWHG PAQNAAAEKG TPALNIAVLL GHSHDVTERE LRNLWGPEQA
TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSQT
FIPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY
RDFISFIKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL
SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
TAASSMLEKF SYIPEAKASC YGQTEKPETP LHTLHQFMVN VTWDGKDLSF TEEGYQVHPR
LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE PDDNHLSIVT LEEAPFVIVE
DIDPLTETCV RNTVPCRKFV KINNSTNEGM NVKKCCKGFC IDILKKLSRT VKFTYDLYLV
TNGKHGKKVN NVWNGMIGEV VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS
NGTVSPSAFL EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA AFMIQEEFVD
QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY MHQYMTKFNQ RGVEDALVSL
KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFATTG YGIALQKGSP WKRQIDLALL
QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL
FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
AKNISNMSNM NSSRMDSPKR AADFIQRGSL IVDMVSDKGN LIYSDNRSFQ GKDSIFGENM
NELQTFVANR HKDSLSNYVF QGQHPLTLNE SNPNTVEVAV STESKGNSRP RQLWKKSMES
LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR YLPEEVAHSD ISETSSRATC HREPDNNKNH
KTKDNFKRSM ASKYPKDCSE VERTYVKTKA SSPRDKIYTI DGEKEPSFHL DPPQFIENIV
LPENVDFPDT YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGNP
ATREEAYQQD WSQNNALQFQ KNKLKINRQH SYDNILDKPR EIDLSRPSRS ISLKDRERLL
EGNLYGSLFS VPSSKLLGNK SSLFPQGLED SKRSKSLLPD HTSDNPFLHT YGDDQRLVIG
RCPSDPYKHS LPSQAVNDSY LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNNMYS
TPRVLNSCSN RRVYKKMPSI ESDV
