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 27-MAR-2024, entry version 241. 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=13; 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}. 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; 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; 7SAA; EM; 2.97 A; A/C=1-847. DR PDB; 7SAB; EM; 4.30 A; A/C=1-847. DR PDB; 7SAC; EM; 3.69 A; A/C=1-847. DR PDB; 7SAD; EM; 3.96 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 PDB; 7YFG; EM; 3.60 A; A/C=1-847. DR PDB; 7YFH; EM; 3.00 A; A/C=1-847. DR PDB; 7YFI; EM; 3.30 A; A/C=1-798. DR PDB; 8HDK; EM; 4.30 A; A/C=1-796. 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; 7SAA; -. DR PDBsum; 7SAB; -. DR PDBsum; 7SAC; -. DR PDBsum; 7SAD; -. DR PDBsum; 7TE9; -. DR PDBsum; 7TEB; -. DR PDBsum; 7TEE; -. DR PDBsum; 7TEQ; -. DR PDBsum; 7TER; -. DR PDBsum; 7TES; -. DR PDBsum; 7TET; -. DR PDBsum; 7YFG; -. DR PDBsum; 7YFH; -. DR PDBsum; 7YFI; -. DR PDBsum; 8HDK; -. DR AlphaFoldDB; P35439; -. DR EMDB; EMD-21673; -. DR EMDB; EMD-21674; -. DR EMDB; EMD-21675; -. DR EMDB; EMD-21676; -. DR EMDB; EMD-21677; -. DR EMDB; EMD-21678; -. DR EMDB; EMD-21679; -. DR EMDB; EMD-21680; -. DR EMDB; EMD-21681; -. DR EMDB; EMD-21682; -. DR EMDB; EMD-24946; -. DR EMDB; EMD-24947; -. DR EMDB; EMD-24948; -. DR EMDB; EMD-24949; -. DR EMDB; EMD-25843; -. DR EMDB; EMD-25844; -. DR EMDB; EMD-25845; -. DR EMDB; EMD-25849; -. DR EMDB; EMD-25850; -. DR EMDB; EMD-25851; -. DR EMDB; EMD-25852; -. DR EMDB; EMD-3352; -. DR EMDB; EMD-3353; -. DR EMDB; EMD-3354; -. DR EMDB; EMD-3355; -. DR EMDB; EMD-3356; -. DR EMDB; EMD-33789; -. DR EMDB; EMD-33790; -. DR EMDB; EMD-33791; -. DR EMDB; EMD-34674; -. DR EMDB; EMD-7529; -. DR EMDB; EMD-9147; -. DR EMDB; EMD-9148; -. DR EMDB; EMD-9149; -. DR EMDB; EMD-9150; -. DR EMDB; EMD-9151; -. DR EMDB; EMD-9152; -. DR EMDB; EMD-9153; -. DR EMDB; EMD-9154; -. DR EMDB; EMD-9155; -. DR EMDB; EMD-9156; -. DR EMDB; EMD-9157; -. DR EMDB; EMD-9158; -. DR EMDB; EMD-9159; -. DR EMDB; EMD-9160; -. DR EMDB; EMD-9161; -. DR EMDB; EMD-9162; -. DR EMDB; EMD-9163; -. DR EMDB; EMD-9164; -. DR EMDB; EMD-9165; -. 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; 19. 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 GlyCosmos; P35439; 12 sites, 12 glycans. DR GlyGen; P35439; 12 sites, 12 N-linked glycans (5 sites). DR iPTMnet; P35439; -. DR PhosphoSitePlus; P35439; -. DR PaxDb; 10116-ENSRNOP00000029227; -. DR ABCD; P35439; 9 sequenced antibodies. DR Ensembl; ENSRNOT00000037725.6; ENSRNOP00000029227.5; ENSRNOG00000011726.8. [P35439-2] DR Ensembl; ENSRNOT00000044246.5; ENSRNOP00000043301.3; ENSRNOG00000011726.8. [P35439-6] DR Ensembl; ENSRNOT00000049297.4; ENSRNOP00000049198.1; ENSRNOG00000011726.8. [P35439-1] DR Ensembl; ENSRNOT00055000870; ENSRNOP00055000684; ENSRNOG00055000504. [P35439-1] DR Ensembl; ENSRNOT00060054953; ENSRNOP00060045438; ENSRNOG00060031665. [P35439-1] DR Ensembl; ENSRNOT00065043348; ENSRNOP00065035543; ENSRNOG00065025127. [P35439-1] DR GeneID; 24408; -. DR KEGG; rno:24408; -. DR UCSC; RGD:2736; rat. [P35439-1] DR AGR; RGD:2736; -. 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 OMA; AYKKHQI; -. DR OrthoDB; 1034721at2759; -. 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 cell types or tissues. DR ExpressionAtlas; P35439; baseline and differential. 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: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:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; ISO:RGD. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD. DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0043083; C:synaptic cleft; IDA:RGD. DR GO; GO:0097060; C:synaptic membrane; IDA:RGD. 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: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:0004970; F:glutamate-gated receptor activity; IDA:RGD. DR GO; GO:0016594; F:glycine binding; IDA:UniProtKB. DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IBA:GO_Central. DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO. DR GO; GO:0005261; F:monoatomic cation channel activity; ISO: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 monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO. DR GO; GO:0022843; F:voltage-gated monoatomic 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: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:0006874; P:intracellular calcium ion homeostasis; 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:0098655; P:monoatomic cation transmembrane transport; IDA:ComplexPortal. DR GO; GO:0006812; P:monoatomic cation transport; 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:0070050; P:neuron cellular homeostasis; 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: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: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:1904062; P:regulation of monoatomic cation transmembrane transport; IDA:ComplexPortal. 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:0006366; P:transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0008542; P:visual learning; ISO:RGD. DR CDD; cd06379; PBP1_iGluR_NMDA_NR1; 1. DR CDD; cd13719; PBP2_iGluR_NMDA_Nr1; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 3.40.50.2300; -; 2. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3. DR InterPro; IPR001828; ANF_lig-bd_rcpt. DR InterPro; IPR019594; Glu/Gly-bd. DR InterPro; IPR001508; Iono_Glu_rcpt_met. DR InterPro; IPR015683; Ionotropic_Glu_rcpt. DR InterPro; IPR001320; Iontro_rcpt_C. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR001638; Solute-binding_3/MltF_N. DR PANTHER; PTHR18966:SF377; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 1; 1. DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00060; Lig_chan; 1. DR Pfam; PF10613; Lig_chan-Glu_bd; 1. DR Pfam; PF00497; SBP_bac_3; 1. DR PRINTS; PR00177; NMDARECEPTOR. DR SMART; SM00918; Lig_chan-Glu_bd; 1. DR SMART; SM00079; PBPe; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; P35439; RN. 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 29..32 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 36..50 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 62..65 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 71..85 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:7SAA" FT TURN 96..99 FT /evidence="ECO:0007829|PDB:7YFI" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:7YFH" FT HELIX 105..113 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:7SAA" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 149..157 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 163..170 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 171..186 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 205..211 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 218..222 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 225..237 FT /evidence="ECO:0007829|PDB:7SAA" FT TURN 238..241 FT /evidence="ECO:0007829|PDB:7YFI" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:7SAA" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 256..260 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 267..273 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 277..295 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:7SAA" FT TURN 308..310 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 319..326 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 330..333 FT /evidence="ECO:0007829|PDB:7YFH" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:3Q41" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:3Q41" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:7YFH" FT STRAND 351..357 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 360..367 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:7SAA" FT STRAND 382..384 FT /evidence="ECO:0007829|PDB:7YFI" 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 TURN 443..445 FT /evidence="ECO:0007829|PDB:7YFH" 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 TURN 553..557 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 560..583 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 603..615 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 627..656 FT /evidence="ECO:0007829|PDB:7SAA" 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 HELIX 811..825 FT /evidence="ECO:0007829|PDB:7SAA" FT HELIX 827..840 FT /evidence="ECO:0007829|PDB:7SAA" 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 //