NMDZ1_MOUSE
ID NMDZ1_MOUSE Reviewed; 938 AA.
AC P35438; A2AI15; A2AI18; Q8CFS4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 218.
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;
DE Short=NMD-R1;
DE Flags: Precursor;
GN Name=Grin1; Synonyms=Glurz1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1532151; DOI=10.1016/0014-5793(92)80160-i;
RA Yamazaki M., Mori H., Araki K., Mori K.J., Mishina M.;
RT "Cloning, expression and modulation of a mouse NMDA receptor subunit.";
RL FEBS Lett. 300:39-45(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8060614; DOI=10.1016/0896-6273(94)90350-6;
RA Forrest D., Yuzaki M., Soares H.D., Ng L., Luk D.C., Sheng M.,
RA Stewart C.L., Morgan J.I., Connor J.A., Curran T.;
RT "Targeted disruption of NMDA receptor 1 gene abolishes NMDA response and
RT results in neonatal death.";
RL Neuron 13:325-338(1994).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3B, FUNCTION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=12008020; DOI=10.1016/s0169-328x(02)00173-0;
RA Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.;
RT "Cloning and characterization of a novel NMDA receptor subunit NR3B: a
RT dominant subunit that reduces calcium permeability.";
RL Brain Res. Mol. Brain Res. 100:43-52(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B
RP AND GRIN3B.
RX PubMed=14602821; DOI=10.1523/jneurosci.23-31-10064.2003;
RA Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
RT "Specific assembly with the NMDA receptor 3B subunit controls surface
RT expression and calcium permeability of NMDA receptors.";
RL J. Neurosci. 23:10064-10073(2003).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH SNX27.
RX PubMed=23524343; DOI=10.1038/nm.3117;
RA Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y., Loo L.S., Cai L.,
RA Thompson R.C., Yang B., Chen Y., Johnson P.F., Wu C., Bu G., Mobley W.C.,
RA Zhang D., Gage F.H., Ranscht B., Zhang Y.W., Lipton S.A., Hong W., Xu H.;
RT "Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by
RT modulating glutamate receptor recycling in Down's syndrome.";
RL Nat. Med. 19:473-480(2013).
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:1532151, PubMed:8060614, PubMed:12008020). Sensitivity to
CC glutamate and channel kinetics depend on the subunit composition
CC (PubMed:12008020). {ECO:0000269|PubMed:12008020,
CC ECO:0000269|PubMed:1532151, ECO:0000269|PubMed:8060614}.
CC -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a epsilon
CC subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third subunit (GRIN3A
CC or GRIN3B) (PubMed:12008020, PubMed:14602821). Found in a complex with
CC GRIN2A or GRIN2B and GRIN3B (PubMed:12008020, PubMed:14602821). Found
CC in a complex with GRIN2A or GRIN2B, GRIN3A and PPP2CB (By similarity).
CC Interacts with DLG4 and MPDZ (By similarity). Interacts with LRFN1 and
CC LRFN2 (By similarity). Interacts with MYZAP (PubMed:18849881).
CC Interacts with SNX27 (via PDZ domain); the interaction is required for
CC recycling to the plasma membrane when endocytosed and prevent
CC degradation in lysosomes (PubMed:23524343). Found in a complex with
CC DLG4 and PRR7 (By similarity). Found in a complex with GRIN2B and PRR7
CC (By similarity). Interacts with PRR7; the interaction is reduced
CC following NMDA receptor activity (By similarity).
CC {ECO:0000250|UniProtKB:P35439, ECO:0000269|PubMed:12008020,
CC ECO:0000269|PubMed:14602821, ECO:0000269|PubMed:18849881,
CC ECO:0000269|PubMed:23524343}.
CC -!- INTERACTION:
CC P35438; Q62108: Dlg4; NbExp=13; IntAct=EBI-400084, EBI-300895;
CC P35438; Q01097: Grin2b; NbExp=11; IntAct=EBI-400084, EBI-400125;
CC P35438; Q924X6: Lrp8; NbExp=4; IntAct=EBI-400084, EBI-432319;
CC P35438; P49769: Psen1; NbExp=3; IntAct=EBI-400084, EBI-990067;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12008020,
CC ECO:0000269|PubMed:1532151, ECO:0000269|PubMed:8060614}; Multi-pass
CC membrane protein {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Enriched in
CC postsynaptic plasma membrane and postsynaptic densities. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35438-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35438-2; Sequence=VSP_014222, VSP_014223;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Detected in
CC brain. {ECO:0000269|PubMed:8060614}.
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 (By similarity). {ECO:0000250|UniProtKB:P35439}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian
CC rate, appear grossly normal and have apparently normal brain structure,
CC but the pups do not feed and all die during the first day after birth.
CC Cerebellum granule cells and hippocampus pyramidal neurons from mutants
CC lack NMDA-induced Ca(2+)influx and membrane currents, contrary to wild-
CC type. {ECO:0000269|PubMed:8060614}.
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; D10028; BAA00920.1; -; mRNA.
DR EMBL; AL732309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039157; AAH39157.1; -; mRNA.
DR CCDS; CCDS15764.1; -. [P35438-1]
DR CCDS; CCDS50528.1; -. [P35438-2]
DR PIR; S21104; S21104.
DR RefSeq; NP_001171127.1; NM_001177656.2.
DR RefSeq; NP_001171128.1; NM_001177657.2. [P35438-2]
DR RefSeq; NP_032195.1; NM_008169.3. [P35438-1]
DR AlphaFoldDB; P35438; -.
DR SMR; P35438; -.
DR BioGRID; 200067; 88.
DR ComplexPortal; CPX-290; NMDA receptor complex, GluN1-GluN2A.
DR ComplexPortal; CPX-291; NMDA receptor complex, GluN1-GluN2B.
DR ComplexPortal; CPX-292; NMDA receptor complex, GluN1-GluN2C.
DR ComplexPortal; CPX-293; NMDA receptor complex, GluN1-GluN2D.
DR ComplexPortal; CPX-296; NMDA receptor complex, GluN1-GluN2A-GluN2B.
DR CORUM; P35438; -.
DR DIP; DIP-31577N; -.
DR IntAct; P35438; 72.
DR MINT; P35438; -.
DR STRING; 10090.ENSMUSP00000028335; -.
DR ChEMBL; CHEMBL3885583; -.
DR GlyConnect; 2349; 14 N-Linked glycans (9 sites).
DR GlyGen; P35438; 12 sites, 13 N-linked glycans (9 sites).
DR iPTMnet; P35438; -.
DR PhosphoSitePlus; P35438; -.
DR SwissPalm; P35438; -.
DR MaxQB; P35438; -.
DR PaxDb; P35438; -.
DR PeptideAtlas; P35438; -.
DR PRIDE; P35438; -.
DR ProteomicsDB; 293691; -. [P35438-1]
DR ProteomicsDB; 293692; -. [P35438-2]
DR ABCD; P35438; 8 sequenced antibodies.
DR Antibodypedia; 3475; 1291 antibodies from 49 providers.
DR DNASU; 14810; -.
DR Ensembl; ENSMUST00000028335; ENSMUSP00000028335; ENSMUSG00000026959. [P35438-1]
DR Ensembl; ENSMUST00000114312; ENSMUSP00000109951; ENSMUSG00000026959. [P35438-2]
DR GeneID; 14810; -.
DR KEGG; mmu:14810; -.
DR UCSC; uc008iri.3; mouse. [P35438-2]
DR UCSC; uc008irk.3; mouse. [P35438-1]
DR CTD; 2902; -.
DR MGI; MGI:95819; Grin1.
DR VEuPathDB; HostDB:ENSMUSG00000026959; -.
DR eggNOG; KOG4440; Eukaryota.
DR GeneTree; ENSGT00940000158016; -.
DR HOGENOM; CLU_007257_2_0_1; -.
DR InParanoid; P35438; -.
DR TreeFam; TF351405; -.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-MMU-9609736; Assembly and cell surface presentation of NMDA receptors.
DR BioGRID-ORCS; 14810; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Grin1; mouse.
DR PRO; PR:P35438; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P35438; protein.
DR Bgee; ENSMUSG00000026959; Expressed in perirhinal cortex and 117 other tissues.
DR ExpressionAtlas; P35438; baseline and differential.
DR Genevisible; P35438; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0044307; C:dendritic branch; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; NAS:UniProtKB.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IPI:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR GO; GO:0005261; F:cation channel activity; IGI:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0016595; F:glutamate binding; ISO:MGI.
DR GO; GO:0035254; F:glutamate receptor binding; ISO:MGI.
DR GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISO:MGI.
DR GO; GO:0016594; F:glycine binding; IMP:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI.
DR GO; GO:0042165; F:neurotransmitter binding; ISO:MGI.
DR GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
DR GO; GO:0022843; F:voltage-gated cation channel activity; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IDA:MGI.
DR GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0098655; P:cation transmembrane transport; ISO:MGI.
DR GO; GO:0006812; P:cation transport; IGI:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0007616; P:long-term memory; IMP:MGI.
DR GO; GO:0060179; P:male mating behavior; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:0008355; P:olfactory learning; IMP:MGI.
DR GO; GO:0021586; P:pons maturation; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:1902952; P:positive regulation of dendritic spine maintenance; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; ISO:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR GO; GO:0018964; P:propylene metabolic process; IDA:BHF-UCL.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; IMP:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR GO; GO:1904062; P:regulation of cation transmembrane transport; ISO:MGI.
DR GO; GO:0010646; P:regulation of cell communication; IMP:MGI.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:MGI.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR GO; GO:1905429; P:response to glycine; ISO:MGI.
DR GO; GO:0043278; P:response to morphine; IMP:MGI.
DR GO; GO:0048511; P:rhythmic process; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0001964; P:startle response; IMP:MGI.
DR GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
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 Alternative splicing; Calcium; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..938
FT /note="Glutamate receptor ionotropic, NMDA 1"
FT /id="PRO_0000011588"
FT TOPO_DOM 19..559
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TOPO_DOM 581..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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:0000305"
FT TRANSMEM 631..647
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TOPO_DOM 648..812
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT TOPO_DOM 834..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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:0000250|UniProtKB:P35439"
FT BINDING 523
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 688
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT BINDING 732
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT MOD_RES 889
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05586"
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:0000250|UniProtKB:Q05586"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
FT DISULFID 79..308
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT DISULFID 420..454
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT DISULFID 436..455
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT DISULFID 744..798
FT /evidence="ECO:0000250|UniProtKB:P35439"
FT VAR_SEQ 864..885
FT /note="DRKSGRAEPDPKKKATFRAITS -> QYHPTDITGPLNLSDPSVSTVV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014222"
FT VAR_SEQ 886..938
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014223"
FT VARIANT 936
FT /note="R -> T"
SQ SEQUENCE 938 AA; 105481 MW; C610632DD3E06171 CRC64;
MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL
NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG
LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL
ETLLEERESK AEKVLQFDPG TKNVTALLME ARDLEARVII LSASEDDAAT VYRAAAMLNM
TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK
LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC
KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCV 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
