NMDZ1_RAT
ID NMDZ1_RAT Reviewed; 938 AA.
AC P35439; Q62646;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Glutamate receptor ionotropic, NMDA 1;
DE Short=GluN1;
DE AltName: Full=Glutamate [NMDA] receptor subunit zeta-1;
DE AltName: Full=N-methyl-D-aspartate receptor subunit NR1 {ECO:0000303|PubMed:1350383};
DE Short=NMD-R1;
DE Flags: Precursor;
GN Name=Grin1; Synonyms=Nmdar1 {ECO:0000303|PubMed:1834949};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=1834949; DOI=10.1038/354031a0;
RA Moriyoshi K., Masu M., Ishii T., Shigemoto R., Mizuno N., Nakanishi S.;
RT "Molecular cloning and characterization of the rat NMDA receptor.";
RL Nature 354:31-37(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=1386026; DOI=10.1016/0014-5793(92)80648-z;
RA Anantharam V., Panchal R., Wilson A., Koltchin V.V., Treistman S.N.,
RA Bayley H.;
RT "Combinatorial RNA splicing alters the surface charge on the NMDA
RT receptor.";
RL FEBS Lett. 305:27-30(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), ALTERNATIVE SPLICING,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1388270; DOI=10.1073/pnas.89.18.8552;
RA Nakanishi N., Axel R., Shneider N.A.;
RT "Alternative splicing generates functionally distinct N-methyl-D-aspartate
RT receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8552-8556(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Forebrain;
RX PubMed=7684237; DOI=10.1016/0896-6273(93)90209-a;
RA Hollmann M., Boulter J., Maron C., Beasley L., Sullivan J., Pecht G.,
RA Heinemann S.F.;
RT "Zinc potentiates agonist-induced currents at certain splice variants of
RT the NMDA receptor.";
RL Neuron 10:943-954(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-86.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8399301; DOI=10.1016/0005-2736(93)90249-y;
RA Bai G., Kusiak J.W.;
RT "Cloning and analysis of the 5' flanking sequence of the rat N-methyl-D-
RT aspartate receptor 1 (NMDAR1) gene.";
RL Biochim. Biophys. Acta 1152:197-200(1993).
RN [6]
RP ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=1352681; DOI=10.1016/0006-291x(92)91701-q;
RA Sugihara H., Moriyoshi K., Ishii T., Masu M., Nakanishi S.;
RT "Structures and properties of seven isoforms of the NMDA receptor generated
RT by alternative splicing.";
RL Biochem. Biophys. Res. Commun. 185:826-832(1992).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=1350383; DOI=10.1126/science.256.5060.1217;
RA Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
RA Burnashev N., Sakmann B., Seeburg P.H.;
RT "Heteromeric NMDA receptors: molecular and functional distinction of
RT subtypes.";
RL Science 256:1217-1221(1992).
RN [8]
RP SUBUNIT, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8428958; DOI=10.1016/s0021-9258(18)53849-7;
RA Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H., Yokoi M.,
RA Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.;
RT "Molecular characterization of the family of the N-methyl-D-aspartate
RT receptor subunits.";
RL J. Biol. Chem. 268:2836-2843(1993).
RN [9]
RP PHOSPHORYLATION AT SER-897, DEPHOSPHORYLATION BY PPP2CB, AND IDENTIFICATION
RP IN A COMPLEX WITH GRIN2A OR GRIN2B; GRIN3A AND PPP2CB.
RX PubMed=11588171; DOI=10.1523/jneurosci.21-20-07985.2001;
RA Chan S.F., Sucher N.J.;
RT "An NMDA receptor signaling complex with protein phosphatase 2A.";
RL J. Neurosci. 21:7985-7992(2001).
RN [10]
RP CHARACTERIZATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND
RP GRIN3A.
RX PubMed=11160393; DOI=10.1523/jneurosci.21-04-01228.2001;
RA Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S.,
RA Sucher N.J., Heinemann S.F.;
RT "Assembly with the NR1 subunit is required for surface expression of NR3A-
RT containing NMDA receptors.";
RL J. Neurosci. 21:1228-1237(2001).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
RX PubMed=12391275; DOI=10.1124/mol.62.5.1119;
RA Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.;
RT "Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2
RT subunits.";
RL Mol. Pharmacol. 62:1119-1127(2002).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3A.
RX PubMed=11929923; DOI=10.1152/jn.00531.2001;
RA Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V.,
RA Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J.,
RA Lipton S.A.;
RT "Characterization and comparison of the NR3A subunit of the NMDA receptor
RT in recombinant systems and primary cortical neurons.";
RL J. Neurophysiol. 87:2052-2063(2002).
RN [13]
RP INTERACTION WITH MPDZ AND DLG4.
RX PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
RA Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
RT "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity
RT and NMDA receptor-dependent synaptic AMPA receptor potentiation.";
RL Neuron 43:563-574(2004).
RN [14]
RP PHOSPHORYLATION AT SER-890.
RX PubMed=15936117; DOI=10.1016/j.neuint.2005.04.011;
RA Sanchez-Perez A.M., Felipo V.;
RT "Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially
RT phosphorylated by protein kinase C isoforms.";
RL Neurochem. Int. 47:84-91(2005).
RN [15]
RP INTERACTION WITH LRFN2.
RX PubMed=16495444; DOI=10.1523/jneurosci.3799-05.2006;
RA Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.;
RT "A novel family of adhesion-like molecules that interacts with the NMDA
RT receptor.";
RL J. Neurosci. 26:2174-2183(2006).
RN [16]
RP INTERACTION WITH LRFN1.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18177891; DOI=10.1016/j.jmb.2007.11.105;
RA Schmidt C., Hollmann M.;
RT "Apparent homomeric NR1 currents observed in Xenopus oocytes are caused by
RT an endogenous NR2 subunit.";
RL J. Mol. Biol. 376:658-670(2008).
RN [18]
RP INTERACTION WITH MYZAP.
RX PubMed=18849881; DOI=10.1097/wnr.0b013e328317f05f;
RA Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R.,
RA Yang J.;
RT "GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit and
RT reduces N-methyl D-aspartate toxicity.";
RL NeuroReport 19:1721-1726(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877 (ISOFORM E),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898 (ISOFORM G), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [20]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-203; ASN-350; ASN-368; ASN-440
RP AND ASN-771, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [21]
RP IDENTIFICATION IN COMPLEX WITH DLG4 AND PRR7, IDENTIFICATION IN A COMPLEX
RP WITH GRIN2B AND PRR7, AND INTERACTION WITH PRR7.
RX PubMed=27458189; DOI=10.15252/embj.201593070;
RA Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
RA Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
RT "Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and regulates
RT NMDA-mediated excitotoxicity.";
RL EMBO J. 35:1923-1934(2016).
RN [22]
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 [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=28384476; DOI=10.1016/j.neuron.2017.03.018;
RA Sun W., Hansen K.B., Jahr C.E.;
RT "Allosteric Interactions between NMDA Receptor Subunits Shape the
RT Developmental Shift in Channel Properties.";
RL Neuron 94:58-64(2017).
RN [24] {ECO:0007744|PDB:1PB7, ECO:0007744|PDB:1PB8, ECO:0007744|PDB:1PB9, ECO:0007744|PDB:1PBQ}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 394-800 IN COMPLEXES WITH AGONIST
RP SERINE AND ANTAGONIST, AND DISULFIDE BOND.
RX PubMed=12805203; DOI=10.1093/emboj/cdg303;
RA Furukawa H., Gouaux E.;
RT "Mechanisms of activation, inhibition and specificity: crystal structures
RT of the NMDA receptor NR1 ligand-binding core.";
RL EMBO J. 22:2873-2885(2003).
RN [25] {ECO:0007744|PDB:2A5T}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 394-800 IN COMPLEX WITH GRIN2A;
RP GLYCINE AND GLUTAMATE, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=16281028; DOI=10.1038/nature04089;
RA Furukawa H., Singh S.K., Mancusso R., Gouaux E.;
RT "Subunit arrangement and function in NMDA receptors.";
RL Nature 438:185-192(2005).
RN [26] {ECO:0007744|PDB:1Y1M, ECO:0007744|PDB:1Y1Z, ECO:0007744|PDB:1Y20}
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 394-800 IN COMPLEXES WITH
RP AGONISTS, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=15996549; DOI=10.1016/j.neuron.2005.05.022;
RA Inanobe A., Furukawa H., Gouaux E.;
RT "Mechanism of partial agonist action at the NR1 subunit of NMDA
RT receptors.";
RL Neuron 47:71-84(2005).
RN [27] {ECO:0007744|PDB:3Q41}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 21-393, SUBUNIT, SUBCELLULAR
RP LOCATION, GLYCOSYLATION AT ASN-61; ASN-203; ASN-239; ASN-276 AND ASN-368,
RP AND DISULFIDE BONDS.
RX PubMed=21389213; DOI=10.1523/jneurosci.6041-10.2011;
RA Farina A.N., Blain K.Y., Maruo T., Kwiatkowski W., Choe S., Nakagawa T.;
RT "Separation of domain contacts is required for heterotetrameric assembly of
RT functional NMDA receptors.";
RL J. Neurosci. 31:3565-3579(2011).
RN [28] {ECO:0007744|PDB:4PE5}
RP X-RAY CRYSTALLOGRAPHY (3.96 ANGSTROMS) OF 23-847 IN COMPLEX WITH GRIN2B;
RP GLYCINE AND ALLOSTERIC INHIBITOR, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP TOPOLOGY, GLYCOSYLATION AT ASN-203; ASN-276; ASN-300; ASN-368 AND ASN-440,
RP AND DISULFIDE BONDS.
RX PubMed=24876489; DOI=10.1126/science.1251915;
RA Karakas E., Furukawa H.;
RT "Crystal structure of a heterotetrameric NMDA receptor ion channel.";
RL Science 344:992-997(2014).
RN [29] {ECO:0007744|PDB:5FXG, ECO:0007744|PDB:5FXH, ECO:0007744|PDB:5FXI, ECO:0007744|PDB:5FXJ, ECO:0007744|PDB:5FXK}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.10 ANGSTROMS) OF 23-847 IN COMPLEX WITH
RP GRIN2A, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TOPOLOGY.
RX PubMed=27135925; DOI=10.1038/nature17679;
RA Tajima N., Karakas E., Grant T., Simorowski N., Diaz-Avalos R.,
RA Grigorieff N., Furukawa H.;
RT "Activation of NMDA receptors and the mechanism of inhibition by
RT ifenprodil.";
RL Nature 534:63-68(2016).
RN [30] {ECO:0007744|PDB:5I56, ECO:0007744|PDB:5I57, ECO:0007744|PDB:5I58, ECO:0007744|PDB:5I59, ECO:0007744|PDB:5JTY}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 394-544 AND 663-800 IN COMPLEXES
RP WITH GLYCINE AND GRIN2A, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP DISULFIDE BONDS.
RX PubMed=27618671; DOI=10.1016/j.neuron.2016.08.014;
RA Yi F., Mou T.C., Dorsett K.N., Volkmann R.A., Menniti F.S., Sprang S.R.,
RA Hansen K.B.;
RT "Structural Basis for Negative Allosteric Modulation of GluN2A-Containing
RT NMDA Receptors.";
RL Neuron 91:1316-1329(2016).
RN [31] {ECO:0007744|PDB:5U8C}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 394-544 AND 663-800 IN COMPLEX
RP WITH GRIN2A AND SYNTHETIC ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=28468946; DOI=10.1124/mol.116.107912;
RA Romero-Hernandez A., Furukawa H.;
RT "Novel Mode of Antagonist Binding in NMDA Receptors Revealed by the Crystal
RT Structure of the GluN1-GluN2A Ligand-Binding Domain Complexed to NVP-
RT AAM077.";
RL Mol. Pharmacol. 92:22-29(2017).
RN [32] {ECO:0007744|PDB:5DEX, ECO:0007744|PDB:5VIH, ECO:0007744|PDB:5VII, ECO:0007744|PDB:5VIJ}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 394-544 AND 663-800 IN COMPLEX
RP WITH GRIN2A AND GLYCINE, AND DISULFIDE BONDS.
RA Mou T.C., Sprang S.R., Hansen K.B.;
RT "Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains
RT with glycine and antagonist, phenyl-ACEPC.";
RL Submitted (APR-2017) to the PDB data bank.
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:1350383, PubMed:1834949, PubMed:1388270, PubMed:8428958,
CC PubMed:18177891, PubMed:28384476, PubMed:15996549, PubMed:24876489,
CC PubMed:27135925, PubMed:27618671, PubMed:28468946). Sensitivity to
CC glutamate and channel kinetics depend on the subunit composition
CC (PubMed:28384476). {ECO:0000269|PubMed:1350383,
CC ECO:0000269|PubMed:1388270, ECO:0000269|PubMed:15996549,
CC ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:1834949,
CC ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
CC ECO:0000269|PubMed:27618671, ECO:0000269|PubMed:28384476,
CC ECO:0000269|PubMed:28468946, ECO:0000269|PubMed:8428958}.
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:18177891, PubMed:28384476,
CC PubMed:16281028, PubMed:15996549, PubMed:21389213, PubMed:24876489,
CC PubMed:27135925, PubMed:28468946, Ref.32). Can also form
CC heterotetrameric channels that contain at least one zeta subunit
CC (GRIN1), an epsilon subunit, plus GRIN3A or GRIN3B (in vitro)
CC (PubMed:11160393, PubMed:11929923, PubMed:12391275). In vivo, the
CC subunit composition may vary in function of the expression levels of
CC the different subunits (Probable). Found in a complex with GRIN2A or
CC GRIN2B, GRIN3A and PPP2CB (PubMed:11588171). Found in a complex with
CC GRIN2A or GRIN2B and GRIN3B (By similarity). Interacts with SNX27 (via
CC PDZ domain); the interaction is required for recycling to the plasma
CC membrane when endocytosed and prevent degradation in lysosomes (By
CC similarity). Interacts with DLG4 and MPDZ (PubMed:15312654). Interacts
CC with LRFN1 and LRFN2 (PubMed:16495444, PubMed:16630835). Interacts with
CC MYZAP (PubMed:18849881). Found in a complex with DLG4 and PRR7
CC (PubMed:27458189). Found in a complex with GRIN2B and PRR7
CC (PubMed:27458189). Interacts with PRR7; the interaction is reduced
CC following NMDA receptor activity (PubMed:27458189).
CC {ECO:0000250|UniProtKB:P35438, ECO:0000269|PubMed:11160393,
CC ECO:0000269|PubMed:11588171, ECO:0000269|PubMed:11929923,
CC ECO:0000269|PubMed:12391275, ECO:0000269|PubMed:1350383,
CC ECO:0000269|PubMed:15312654, ECO:0000269|PubMed:15996549,
CC ECO:0000269|PubMed:16281028, ECO:0000269|PubMed:16495444,
CC ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:18177891,
CC ECO:0000269|PubMed:18849881, ECO:0000269|PubMed:21389213,
CC ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
CC ECO:0000269|PubMed:27458189, ECO:0000269|PubMed:27618671,
CC ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946,
CC ECO:0000269|PubMed:8428958, ECO:0000269|Ref.32, ECO:0000305}.
CC -!- INTERACTION:
CC P35439; P31016: Dlg4; NbExp=4; IntAct=EBI-877897, EBI-375655;
CC P35439; Q00960: Grin2b; NbExp=12; IntAct=EBI-877897, EBI-396905;
CC P35439; Q460M5: Lrfn2; NbExp=2; IntAct=EBI-877897, EBI-877185;
CC P35439; Q9JJ40: Pdzk1; NbExp=3; IntAct=EBI-877897, EBI-7713572;
CC P35439; Q80TG9: Lrfn2; Xeno; NbExp=2; IntAct=EBI-877897, EBI-877092;
CC P35439-1; Q80TG9: Lrfn2; Xeno; NbExp=2; IntAct=EBI-877923, EBI-877092;
CC P35439-4; Q80TG9: Lrfn2; Xeno; NbExp=2; IntAct=EBI-877935, EBI-877092;
CC P35439-7; Q00960: Grin2b; NbExp=2; IntAct=EBI-15932497, EBI-396905;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1350383,
CC ECO:0000269|PubMed:1388270, ECO:0000269|PubMed:15996549,
CC ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:1834949,
CC ECO:0000269|PubMed:21389213, ECO:0000269|PubMed:24876489,
CC ECO:0000269|PubMed:27135925, ECO:0000269|PubMed:27618671,
CC ECO:0000269|PubMed:28384476, ECO:0000269|PubMed:28468946,
CC ECO:0000269|PubMed:8428958}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925}.
CC Postsynaptic cell membrane {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Note=Enriched in postsynaptic plasma membrane and
CC postsynaptic densities. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=A;
CC IsoId=P35439-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P35439-2; Sequence=VSP_000140;
CC Name=C; Synonyms=NMDAR1-2a subunit;
CC IsoId=P35439-3; Sequence=VSP_000141;
CC Name=D;
CC IsoId=P35439-4; Sequence=VSP_000144;
CC Name=E;
CC IsoId=P35439-5; Sequence=VSP_000142, VSP_000143;
CC Name=F; Synonyms=NMDAR1-2b subunit;
CC IsoId=P35439-6; Sequence=VSP_000140, VSP_000141;
CC Name=G; Synonyms=NMDAR1-4b subunit;
CC IsoId=P35439-7; Sequence=VSP_000140, VSP_000142, VSP_000143;
CC -!- TISSUE SPECIFICITY: Detected throughout the brain, in brain cortex,
CC cerebellum, thalamus and olfactory bulb. {ECO:0000269|PubMed:1350383}.
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:A0A1L8F5J9}.
CC -!- PTM: NMDA is probably regulated by C-terminal phosphorylation of an
CC isoform of NR1 by PKC. Dephosphorylated on Ser-897 probably by protein
CC phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the
CC formation of the NMDAR-PPP2CB complex and the NMDAR channel activity.
CC {ECO:0000269|PubMed:11588171, ECO:0000269|PubMed:15936117}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. NR1/GRIN1 subfamily. {ECO:0000305}.
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DR EMBL; X63255; CAA44914.1; -; mRNA.
DR EMBL; AY157515; AAA16366.1; -; Genomic_DNA.
DR EMBL; X65227; CAA46335.1; -; mRNA.
DR EMBL; U08261; AAB50926.1; -; mRNA.
DR EMBL; U08262; AAB50927.1; -; mRNA.
DR EMBL; U08263; AAB50928.1; -; mRNA.
DR EMBL; U08264; AAB50929.1; -; mRNA.
DR EMBL; U08265; AAB50930.1; -; mRNA.
DR EMBL; U08267; AAB50932.1; -; mRNA.
DR EMBL; U08268; AAB50933.1; -; mRNA.
DR EMBL; S39217; AAB22431.1; -; mRNA.
DR EMBL; S39218; AAB22432.1; -; mRNA.
DR EMBL; S39219; AAB22433.1; -; mRNA.
DR EMBL; S39220; AAB22434.1; -; mRNA.
DR EMBL; S39221; AAB22435.1; -; mRNA.
DR PIR; JN0336; JN0336.
DR PIR; JN0337; JN0337.
DR PIR; JN0338; JN0338.
DR PIR; JN0339; JN0339.
DR PIR; JN0340; JN0340.
DR PIR; JN0341; JN0341.
DR PIR; JN0342; JN0342.
DR PIR; S19710; S19710.
DR RefSeq; NP_001257531.1; NM_001270602.1. [P35439-2]
DR RefSeq; NP_001257532.1; NM_001270603.1. [P35439-6]
DR RefSeq; NP_001257534.1; NM_001270605.1. [P35439-3]
DR RefSeq; NP_001257537.1; NM_001270608.1. [P35439-7]
DR RefSeq; NP_001257539.1; NM_001270610.1. [P35439-5]
DR RefSeq; NP_001274352.1; NM_001287423.1. [P35439-4]
DR RefSeq; NP_058706.1; NM_017010.2. [P35439-1]
DR PDB; 1PB7; X-ray; 1.35 A; A=394-544, A=663-800.
DR PDB; 1PB8; X-ray; 1.45 A; A=394-544, A=663-800.
DR PDB; 1PB9; X-ray; 1.60 A; A=394-544, A=663-800.
DR PDB; 1PBQ; X-ray; 1.90 A; A/B=394-544, A/B=663-800.
DR PDB; 1Y1M; X-ray; 1.80 A; A/B=394-544, A/B=663-800.
DR PDB; 1Y1Z; X-ray; 1.50 A; A=394-544, A=663-800.
DR PDB; 1Y20; X-ray; 1.40 A; A=394-544, A=663-800.
DR PDB; 2A5T; X-ray; 2.00 A; A=394-544.
DR PDB; 3Q41; X-ray; 3.40 A; A/B/C=21-393.
DR PDB; 4KCC; X-ray; 1.89 A; A=394-544, A=663-800.
DR PDB; 4KFQ; X-ray; 2.20 A; A/B=394-544, A/B=663-800.
DR PDB; 4NF4; X-ray; 2.00 A; A=394-544, A=663-800.
DR PDB; 4NF5; X-ray; 1.90 A; A=394-544, A=663-800.
DR PDB; 4NF6; X-ray; 2.10 A; A=394-544, A=663-800.
DR PDB; 4NF8; X-ray; 1.86 A; A=394-544, A=663-800.
DR PDB; 4PE5; X-ray; 3.96 A; A/C=23-847.
DR PDB; 5DEX; X-ray; 2.40 A; A=394-544, A=663-800.
DR PDB; 5FXG; EM; 6.80 A; A/C=23-863.
DR PDB; 5FXH; EM; 6.10 A; A/C=23-863.
DR PDB; 5FXI; EM; 6.40 A; A/C=23-863.
DR PDB; 5FXJ; EM; 6.50 A; A/C=23-863.
DR PDB; 5FXK; EM; 6.40 A; A/C=23-863.
DR PDB; 5I56; X-ray; 2.28 A; A=394-544, A=663-800.
DR PDB; 5I57; X-ray; 1.70 A; A=394-544, A=684-821.
DR PDB; 5I58; X-ray; 2.52 A; A=394-544, A=663-800.
DR PDB; 5I59; X-ray; 2.25 A; A=394-544, A=663-800.
DR PDB; 5JTY; X-ray; 2.72 A; A=394-544, A=684-821.
DR PDB; 5U8C; X-ray; 1.60 A; A=394-544, A=663-800.
DR PDB; 5VIH; X-ray; 2.40 A; A=394-544, A=663-800.
DR PDB; 5VII; X-ray; 1.95 A; A=394-544, A=663-800.
DR PDB; 5VIJ; X-ray; 2.10 A; A=394-544, A=663-800.
DR PDB; 6CNA; EM; 4.60 A; A/C=25-838.
DR PDB; 6MM9; EM; 5.97 A; A/C=1-838.
DR PDB; 6MMA; EM; 6.31 A; A/C=1-838.
DR PDB; 6MMB; EM; 12.70 A; A/C=1-838.
DR PDB; 6MMG; EM; 6.23 A; A/C=1-838.
DR PDB; 6MMH; EM; 8.21 A; A/C=1-838.
DR PDB; 6MMI; EM; 8.93 A; A/C=1-838.
DR PDB; 6MMJ; EM; 16.50 A; A/C=1-838.
DR PDB; 6MMK; EM; 6.08 A; A/C=1-838.
DR PDB; 6MML; EM; 7.14 A; A/C=1-838.
DR PDB; 6MMM; EM; 6.84 A; A/C=1-838.
DR PDB; 6MMN; EM; 7.51 A; A/C=1-838.
DR PDB; 6MMP; EM; 6.88 A; A/C=1-838.
DR PDB; 6MMR; EM; 5.13 A; A/C=1-838.
DR PDB; 6MMS; EM; 5.38 A; A/C=1-838.
DR PDB; 6MMT; EM; 7.46 A; A/C=1-838.
DR PDB; 6MMU; EM; 5.30 A; A/C=1-838.
DR PDB; 6MMV; EM; 4.71 A; A/C=1-797.
DR PDB; 6MMW; EM; 6.20 A; A/C=1-838.
DR PDB; 6MMX; EM; 6.99 A; A/C=1-838.
DR PDB; 6OVD; X-ray; 2.10 A; A=394-544, A=663-800.
DR PDB; 6OVE; X-ray; 2.00 A; A=394-544, A=663-800.
DR PDB; 6USU; X-ray; 2.09 A; A=394-544, A=663-800.
DR PDB; 6USV; X-ray; 2.30 A; A=394-544, A=663-800.
DR PDB; 6UZ6; X-ray; 1.66 A; A=394-544, A=663-800.
DR PDB; 6UZG; X-ray; 1.94 A; A=394-544, A=663-800.
DR PDB; 6UZR; X-ray; 1.87 A; A=394-544, A=663-800.
DR PDB; 6UZW; X-ray; 2.13 A; A=394-544, A=663-800.
DR PDB; 6UZX; X-ray; 2.41 A; A=394-544, A=663-800.
DR PDB; 6WHR; EM; 3.99 A; A/C=1-938.
DR PDB; 6WHS; EM; 4.00 A; A/C=1-938.
DR PDB; 6WHT; EM; 4.39 A; A/C=1-938.
DR PDB; 6WHU; EM; 3.93 A; A/C=1-938.
DR PDB; 6WHV; EM; 4.05 A; A/C=1-938.
DR PDB; 6WHW; EM; 4.09 A; A/C=1-938.
DR PDB; 6WHX; EM; 4.09 A; A/C=1-938.
DR PDB; 6WHY; EM; 4.03 A; A/C=1-938.
DR PDB; 6WI0; EM; 4.27 A; A/C=1-938.
DR PDB; 6WI1; EM; 3.62 A; A/C=1-847.
DR PDB; 7TE9; EM; 3.92 A; A/C=1-838.
DR PDB; 7TEB; EM; 4.23 A; A/C=1-838.
DR PDB; 7TEE; EM; 6.59 A; A/C=1-838.
DR PDB; 7TEQ; EM; 7.51 A; A/C=1-838.
DR PDB; 7TER; EM; 5.23 A; A/C=1-838.
DR PDB; 7TES; EM; 4.70 A; A/C=1-838.
DR PDB; 7TET; EM; 4.45 A; A/C=1-838.
DR PDBsum; 1PB7; -.
DR PDBsum; 1PB8; -.
DR PDBsum; 1PB9; -.
DR PDBsum; 1PBQ; -.
DR PDBsum; 1Y1M; -.
DR PDBsum; 1Y1Z; -.
DR PDBsum; 1Y20; -.
DR PDBsum; 2A5T; -.
DR PDBsum; 3Q41; -.
DR PDBsum; 4KCC; -.
DR PDBsum; 4KFQ; -.
DR PDBsum; 4NF4; -.
DR PDBsum; 4NF5; -.
DR PDBsum; 4NF6; -.
DR PDBsum; 4NF8; -.
DR PDBsum; 4PE5; -.
DR PDBsum; 5DEX; -.
DR PDBsum; 5FXG; -.
DR PDBsum; 5FXH; -.
DR PDBsum; 5FXI; -.
DR PDBsum; 5FXJ; -.
DR PDBsum; 5FXK; -.
DR PDBsum; 5I56; -.
DR PDBsum; 5I57; -.
DR PDBsum; 5I58; -.
DR PDBsum; 5I59; -.
DR PDBsum; 5JTY; -.
DR PDBsum; 5U8C; -.
DR PDBsum; 5VIH; -.
DR PDBsum; 5VII; -.
DR PDBsum; 5VIJ; -.
DR PDBsum; 6CNA; -.
DR PDBsum; 6MM9; -.
DR PDBsum; 6MMA; -.
DR PDBsum; 6MMB; -.
DR PDBsum; 6MMG; -.
DR PDBsum; 6MMH; -.
DR PDBsum; 6MMI; -.
DR PDBsum; 6MMJ; -.
DR PDBsum; 6MMK; -.
DR PDBsum; 6MML; -.
DR PDBsum; 6MMM; -.
DR PDBsum; 6MMN; -.
DR PDBsum; 6MMP; -.
DR PDBsum; 6MMR; -.
DR PDBsum; 6MMS; -.
DR PDBsum; 6MMT; -.
DR PDBsum; 6MMU; -.
DR PDBsum; 6MMV; -.
DR PDBsum; 6MMW; -.
DR PDBsum; 6MMX; -.
DR PDBsum; 6OVD; -.
DR PDBsum; 6OVE; -.
DR PDBsum; 6USU; -.
DR PDBsum; 6USV; -.
DR PDBsum; 6UZ6; -.
DR PDBsum; 6UZG; -.
DR PDBsum; 6UZR; -.
DR PDBsum; 6UZW; -.
DR PDBsum; 6UZX; -.
DR PDBsum; 6WHR; -.
DR PDBsum; 6WHS; -.
DR PDBsum; 6WHT; -.
DR PDBsum; 6WHU; -.
DR PDBsum; 6WHV; -.
DR PDBsum; 6WHW; -.
DR PDBsum; 6WHX; -.
DR PDBsum; 6WHY; -.
DR PDBsum; 6WI0; -.
DR PDBsum; 6WI1; -.
DR PDBsum; 7TE9; -.
DR PDBsum; 7TEB; -.
DR PDBsum; 7TEE; -.
DR PDBsum; 7TEQ; -.
DR PDBsum; 7TER; -.
DR PDBsum; 7TES; -.
DR PDBsum; 7TET; -.
DR AlphaFoldDB; P35439; -.
DR SMR; P35439; -.
DR BioGRID; 246573; 24.
DR ComplexPortal; CPX-283; NMDA receptor complex, GluN1-GluN2A.
DR ComplexPortal; CPX-284; NMDA receptor complex, GluN1-GluN2B.
DR ComplexPortal; CPX-287; NMDA receptor complex, GluN1-GluN2C.
DR ComplexPortal; CPX-288; NMDA receptor complex, GluN1-GluN2D.
DR ComplexPortal; CPX-295; NMDA receptor complex, GluN1-GluN2A-GluN2B.
DR CORUM; P35439; -.
DR DIP; DIP-674N; -.
DR IntAct; P35439; 18.
DR MINT; P35439; -.
DR STRING; 10116.ENSRNOP00000029227; -.
DR BindingDB; P35439; -.
DR ChEMBL; CHEMBL330; -.
DR DrugCentral; P35439; -.
DR GuidetoPHARMACOLOGY; 455; -.
DR TCDB; 1.A.10.1.6; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; P35439; 12 sites, 12 N-linked glycans (5 sites).
DR iPTMnet; P35439; -.
DR PhosphoSitePlus; P35439; -.
DR PaxDb; P35439; -.
DR PRIDE; P35439; -.
DR ABCD; P35439; 9 sequenced antibodies.
DR Ensembl; ENSRNOT00000037725; ENSRNOP00000029227; ENSRNOG00000011726. [P35439-2]
DR Ensembl; ENSRNOT00000044246; ENSRNOP00000043301; ENSRNOG00000011726. [P35439-6]
DR Ensembl; ENSRNOT00000049297; ENSRNOP00000049198; ENSRNOG00000011726. [P35439-1]
DR GeneID; 24408; -.
DR KEGG; rno:24408; -.
DR UCSC; RGD:2736; rat. [P35439-1]
DR CTD; 2902; -.
DR RGD; 2736; Grin1.
DR eggNOG; KOG4440; Eukaryota.
DR GeneTree; ENSGT00940000158016; -.
DR HOGENOM; CLU_007257_2_0_1; -.
DR InParanoid; P35439; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P35439; -.
DR TreeFam; TF351405; -.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-RNO-9609736; Assembly and cell surface presentation of NMDA receptors.
DR EvolutionaryTrace; P35439; -.
DR PRO; PR:P35439; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000011726; Expressed in frontal cortex and 9 other tissues.
DR ExpressionAtlas; P35439; baseline and differential.
DR Genevisible; P35439; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:BHF-UCL.
DR GO; GO:0044307; C:dendritic branch; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; IDA:RGD.
DR GO; GO:0097060; C:synaptic membrane; IPI:ARUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
DR GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0005261; F:cation channel activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0016595; F:glutamate binding; IDA:UniProtKB.
DR GO; GO:0035254; F:glutamate receptor binding; IPI:RGD.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISO:RGD.
DR GO; GO:0016594; F:glycine binding; IDA:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
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; IDA:SynGO.
DR GO; GO:0042165; F:neurotransmitter binding; IDA:RGD.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0022843; F:voltage-gated cation channel activity; IMP:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0006812; P:cation transport; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0071287; P:cellular response to manganese ion; IEP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0001661; P:conditioned taste aversion; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0007616; P:long-term memory; ISO:RGD.
DR GO; GO:0060179; P:male mating behavior; ISO:RGD.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0008355; P:olfactory learning; ISO:RGD.
DR GO; GO:0021586; P:pons maturation; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IGI:ARUK-UCL.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; IGI:ARUK-UCL.
DR GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IGI:ARUK-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IGI:ARUK-UCL.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; IMP:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0060134; P:prepulse inhibition; ISO:RGD.
DR GO; GO:0018964; P:propylene metabolic process; ISO:RGD.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0050770; P:regulation of axonogenesis; ISO:RGD.
DR GO; GO:1904062; P:regulation of cation transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0010646; P:regulation of cell communication; ISO:RGD.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0043576; P:regulation of respiratory gaseous exchange; ISO:RGD.
DR GO; GO:0051963; P:regulation of synapse assembly; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0014075; P:response to amine; IEP:RGD.
DR GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; ISO:RGD.
DR GO; GO:0060992; P:response to fungicide; IEP:RGD.
DR GO; GO:1905429; P:response to glycine; ISO:RGD.
DR GO; GO:0043278; P:response to morphine; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0048511; P:rhythmic process; IDA:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0001964; P:startle response; ISO:RGD.
DR GO; GO:0001967; P:suckling behavior; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF10562; CaM_bdg_C0; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Magnesium; Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..938
FT /note="Glutamate receptor ionotropic, NMDA 1"
FT /id="PRO_0000011589"
FT TOPO_DOM 19..559
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TOPO_DOM 581..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24876489"
FT INTRAMEM 603..624
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:A0A1L8F5J9"
FT TOPO_DOM 625..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TRANSMEM 631..647
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TOPO_DOM 648..812
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24876489"
FT TOPO_DOM 834..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24876489"
FT REGION 603..624
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:A0A1L8F5J9"
FT REGION 889..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 516..518
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:1PB7, ECO:0007744|PDB:2A5T,
FT ECO:0007744|PDB:4NF5, ECO:0007744|PDB:4NF6,
FT ECO:0007744|PDB:4NF8, ECO:0007744|PDB:4PE5,
FT ECO:0007744|PDB:5DEX, ECO:0007744|PDB:5I56,
FT ECO:0007744|PDB:5I57, ECO:0007744|PDB:5I58,
FT ECO:0007744|PDB:5I59, ECO:0007744|PDB:5U8C,
FT ECO:0007744|PDB:5VIH, ECO:0007744|PDB:5VII,
FT ECO:0007744|PDB:5VIJ"
FT BINDING 523
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:24876489, ECO:0007744|PDB:1PB7,
FT ECO:0007744|PDB:2A5T, ECO:0007744|PDB:4NF5,
FT ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:4PE5, ECO:0007744|PDB:5DEX,
FT ECO:0007744|PDB:5I56, ECO:0007744|PDB:5I57,
FT ECO:0007744|PDB:5I58, ECO:0007744|PDB:5I59,
FT ECO:0007744|PDB:5U8C, ECO:0007744|PDB:5VIH,
FT ECO:0007744|PDB:5VII, ECO:0007744|PDB:5VIJ"
FT BINDING 688
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:24876489, ECO:0007744|PDB:1PB7,
FT ECO:0007744|PDB:2A5T, ECO:0007744|PDB:4NF5,
FT ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:4PE5, ECO:0007744|PDB:5DEX,
FT ECO:0007744|PDB:5I56, ECO:0007744|PDB:5I57,
FT ECO:0007744|PDB:5I58, ECO:0007744|PDB:5I59,
FT ECO:0007744|PDB:5U8C, ECO:0007744|PDB:5VIH,
FT ECO:0007744|PDB:5VII, ECO:0007744|PDB:5VIJ"
FT BINDING 732
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000269|PubMed:16281028,
FT ECO:0000269|PubMed:24876489, ECO:0007744|PDB:1PB7,
FT ECO:0007744|PDB:2A5T, ECO:0007744|PDB:4NF5,
FT ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:4PE5, ECO:0007744|PDB:5DEX,
FT ECO:0007744|PDB:5I56, ECO:0007744|PDB:5I57,
FT ECO:0007744|PDB:5I58, ECO:0007744|PDB:5I59,
FT ECO:0007744|PDB:5U8C, ECO:0007744|PDB:5VIH,
FT ECO:0007744|PDB:5VII, ECO:0007744|PDB:5VIJ"
FT MOD_RES 889
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
FT MOD_RES 890
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:15936117"
FT MOD_RES 896
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
FT MOD_RES 897
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:11588171"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:3Q41"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:3Q41, ECO:0007744|PDB:4PE5,
FT ECO:0007744|PubMed:24090084"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:3Q41"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:3Q41, ECO:0007744|PDB:4PE5"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:3Q41, ECO:0007744|PDB:4PE5,
FT ECO:0007744|PubMed:24090084"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24876489,
FT ECO:0007744|PDB:4PE5, ECO:0007744|PubMed:24090084"
FT CARBOHYD 471
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 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 79..308
FT /evidence="ECO:0007744|PDB:3Q41, ECO:0007744|PDB:4PE5"
FT DISULFID 420..454
FT /evidence="ECO:0007744|PDB:1PB7, ECO:0007744|PDB:1PB8,
FT ECO:0007744|PDB:1PB9, ECO:0007744|PDB:1PBQ,
FT ECO:0007744|PDB:1Y1M, ECO:0007744|PDB:1Y1Z,
FT ECO:0007744|PDB:1Y20, ECO:0007744|PDB:2A5T,
FT ECO:0007744|PDB:4KCC, ECO:0007744|PDB:4KFQ,
FT ECO:0007744|PDB:4NF4, ECO:0007744|PDB:4NF5,
FT ECO:0007744|PDB:4NF8, ECO:0007744|PDB:4PE5,
FT ECO:0007744|PDB:5DEX, ECO:0007744|PDB:5I56,
FT ECO:0007744|PDB:5I57, ECO:0007744|PDB:5I58,
FT ECO:0007744|PDB:5I59, ECO:0007744|PDB:5JTY,
FT ECO:0007744|PDB:5U8C, ECO:0007744|PDB:5VIH,
FT ECO:0007744|PDB:5VII, ECO:0007744|PDB:5VIJ"
FT DISULFID 436..455
FT /evidence="ECO:0007744|PDB:1PB7, ECO:0007744|PDB:1PB8,
FT ECO:0007744|PDB:1PB9, ECO:0007744|PDB:1PBQ,
FT ECO:0007744|PDB:1Y1M, ECO:0007744|PDB:1Y1Z,
FT ECO:0007744|PDB:1Y20, ECO:0007744|PDB:2A5T,
FT ECO:0007744|PDB:4KCC, ECO:0007744|PDB:4KFQ,
FT ECO:0007744|PDB:4NF4, ECO:0007744|PDB:4NF5,
FT ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4NF8,
FT ECO:0007744|PDB:4PE5, ECO:0007744|PDB:5DEX,
FT ECO:0007744|PDB:5I56, ECO:0007744|PDB:5I57,
FT ECO:0007744|PDB:5I58, ECO:0007744|PDB:5I59,
FT ECO:0007744|PDB:5JTY, ECO:0007744|PDB:5U8C,
FT ECO:0007744|PDB:5VIH, ECO:0007744|PDB:5VII,
FT ECO:0007744|PDB:5VIJ"
FT DISULFID 744..798
FT /evidence="ECO:0007744|PDB:1PB7, ECO:0007744|PDB:1PB8,
FT ECO:0007744|PDB:1PB9, ECO:0007744|PDB:1PBQ,
FT ECO:0007744|PDB:1Y1Z, ECO:0007744|PDB:1Y20,
FT ECO:0007744|PDB:4KCC, ECO:0007744|PDB:4KFQ,
FT ECO:0007744|PDB:4NF6, ECO:0007744|PDB:4PE5,
FT ECO:0007744|PDB:5I56, ECO:0007744|PDB:5U8C"
FT VAR_SEQ 190
FT /note="K -> KSKKRNYENLDQLSYDNKRGPK (in isoform B, isoform F
FT and isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_000140"
FT VAR_SEQ 864..900
FT /note="Missing (in isoform F and isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_000141"
FT VAR_SEQ 864..885
FT /note="DRKSGRAEPDPKKKATFRAITS -> QYHPTDITGPLNLSDPSVSTVV (in
FT isoform E and isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_000142"
FT VAR_SEQ 886..938
FT /note="Missing (in isoform E and isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_000143"
FT VAR_SEQ 901..938
FT /note="STGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES -> QYHPTDITGP
FT LNLSDPSVSTVV (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_000144"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:3Q41"
FT TURN 98..103
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:3Q41"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3Q41"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:3Q41"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 205..212
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3Q41"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:3Q41"
FT TURN 256..260
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 277..296
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3Q41"
FT HELIX 317..326
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:3Q41"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:1PB7"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:1PB7"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:5I59"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4NF4"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 458..470
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:5VIH"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:1Y1M"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 500..506
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 533..543
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 666..669
FT /evidence="ECO:0007829|PDB:5VII"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:5VIJ"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:1Y1Z"
FT HELIX 688..694
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 700..706
FT /evidence="ECO:0007829|PDB:1PB7"
FT TURN 707..709
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 714..722
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 727..732
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 733..742
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 753..758
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 769..781
FT /evidence="ECO:0007829|PDB:1PB7"
FT HELIX 784..792
FT /evidence="ECO:0007829|PDB:1PB7"
FT STRAND 794..796
FT /evidence="ECO:0007829|PDB:1PB7"
FT MOD_RES P35439-5:877
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES P35439-7:898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 938 AA; 105509 MW; 613D36E38F05BC73 CRC64;
MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL
NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG
LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL
ETLLEERESK AEKVLQFDPG TKNVTALLME ARELEARVII LSASEDDAAT VYRAAAMLNM
TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK
LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC
KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCI DLLIKLARTM NFTYEVHLVA
DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI
LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP
EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA
VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH
ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH
KDARRKQMQL AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES
