ID   NMDE3_HUMAN             Reviewed;        1233 AA.
AC   Q14957; B2RTT1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 3.
DT   24-JAN-2024, entry version 203.
DE   RecName: Full=Glutamate receptor ionotropic, NMDA 2C;
DE            Short=GluN2C;
DE   AltName: Full=Glutamate [NMDA] receptor subunit epsilon-3;
DE   AltName: Full=N-methyl D-aspartate receptor subtype 2C;
DE            Short=NMDAR2C;
DE            Short=NR2C;
DE   Flags: Precursor;
GN   Name=GRIN2C; Synonyms=NMDAR2C;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9037519; DOI=10.1016/s0169-328x(96)00146-5;
RA   Lin Y.J., Bovetto S., Carver J.M., Giordano T.;
RT   "Cloning of the cDNA for the human NMDA receptor NR2C subunit and its
RT   expression in the central nervous system and periphery.";
RL   Brain Res. Mol. Brain Res. 43:57-64(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   INTERACTION WITH SNX27.
RX   PubMed=21300787; DOI=10.1128/mcb.01044-10;
RA   Cai L., Loo L.S., Atlashkin V., Hanson B.J., Hong W.;
RT   "Deficiency of sorting nexin 27 (SNX27) leads to growth retardation and
RT   elevated levels of N-methyl-D-aspartate receptor 2C (NR2C).";
RL   Mol. Cell. Biol. 31:1734-1747(2011).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=26875626; DOI=10.1016/j.neuron.2016.01.016;
RA   Hackos D.H., Lupardus P.J., Grand T., Chen Y., Wang T.M., Reynen P.,
RA   Gustafson A., Wallweber H.J., Volgraf M., Sellers B.D., Schwarz J.B.,
RA   Paoletti P., Sheng M., Zhou Q., Hanson J.E.;
RT   "Positive Allosteric Modulators of GluN2A-Containing NMDARs with Distinct
RT   Modes of Action and Impacts on Circuit Function.";
RL   Neuron 89:983-999(2016).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF PRO-550.
RX   PubMed=28095420; DOI=10.1371/journal.pgen.1006536;
RA   Ogden K.K., Chen W., Swanger S.A., McDaniel M.J., Fan L.Z., Hu C.,
RA   Tankovic A., Kusumoto H., Kosobucki G.J., Schulien A.J., Su Z., Pecha J.,
RA   Bhattacharya S., Petrovski S., Cohen A.E., Aizenman E., Traynelis S.F.,
RA   Yuan H.;
RT   "Molecular mechanism of disease-associated mutations in the pre-M1 helix of
RT   NMDA receptors and potential rescue pharmacology.";
RL   PLoS Genet. 13:E1006536-E1006536(2017).
RN   [7]
RP   VARIANTS 18-TRP--VAL-1233 DEL; ILE-90; VAL-166; THR-573; THR-641; CYS-679;
RP   THR-863; ARG-871; SER-877; ILE-911; ALA-982; PRO-989; LEU-995; TYR-1079;
RP   ALA-1141; ARG-1180 AND ILE-1196.
RX   PubMed=22833210; DOI=10.1038/tp.2011.52;
RG   S2D team;
RA   Tarabeux J., Kebir O., Gauthier J., Hamdan F.F., Xiong L., Piton A.,
RA   Spiegelman D., Henrion E., Millet B., Fathalli F., Joober R.,
RA   Rapoport J.L., DeLisi L.E., Fombonne E., Mottron L., Forget-Dubois N.,
RA   Boivin M., Michaud J.L., Drapeau P., Lafreniere R.G., Rouleau G.A.,
RA   Krebs M.O.;
RT   "Rare mutations in N-methyl-D-aspartate glutamate receptors in autism
RT   spectrum disorders and schizophrenia.";
RL   Transl. Psychiatry 1:E55-E55(2011).
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:26875626). Sensitivity to glutamate and channel kinetics depend
CC       on the subunit composition (Probable). Plays a role in regulating the
CC       balance between excitatory and inhibitory activity of pyramidal neurons
CC       in the prefrontal cortex. Contributes to the slow phase of excitatory
CC       postsynaptic current, long-term synaptic potentiation, and learning (By
CC       similarity). {ECO:0000250|UniProtKB:Q01098,
CC       ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:28095420, ECO:0000305}.
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:26875626). In vivo, the subunit
CC       composition may depend on the expression levels of the different
CC       subunits (Probable). Interacts with PDZ domains of PATJ and DLG4 (By
CC       similarity). Interacts (via PDZ-binding motif) with SNX27 (via PDZ
CC       domain); the interaction is required for recycling to the plasma
CC       membrane when endocytosed and prevent degradation in lysosomes
CC       (PubMed:21300787). {ECO:0000250|UniProtKB:Q00961,
CC       ECO:0000269|PubMed:21300787, ECO:0000269|PubMed:26875626, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q14957; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-8285963, EBI-10173507;
CC       Q14957; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-8285963, EBI-5280499;
CC       Q14957; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-8285963, EBI-9089489;
CC       Q14957; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-8285963, EBI-2548012;
CC       Q14957; Q5PSV4: BRMS1L; NbExp=3; IntAct=EBI-8285963, EBI-5666615;
CC       Q14957; Q9ULD4-2: BRPF3; NbExp=3; IntAct=EBI-8285963, EBI-23662416;
CC       Q14957; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-8285963, EBI-10693038;
CC       Q14957; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-8285963, EBI-18036948;
CC       Q14957; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-8285963, EBI-751596;
CC       Q14957; Q5M9N0-2: CCDC158; NbExp=3; IntAct=EBI-8285963, EBI-21796846;
CC       Q14957; P24941: CDK2; NbExp=3; IntAct=EBI-8285963, EBI-375096;
CC       Q14957; O95674: CDS2; NbExp=3; IntAct=EBI-8285963, EBI-3913685;
CC       Q14957; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-8285963, EBI-749253;
CC       Q14957; Q9Y3D0: CIAO2B; NbExp=3; IntAct=EBI-8285963, EBI-744045;
CC       Q14957; P02458-1: COL2A1; NbExp=3; IntAct=EBI-8285963, EBI-12375799;
CC       Q14957; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-8285963, EBI-751783;
CC       Q14957; Q6ZN54-2: DEF8; NbExp=3; IntAct=EBI-8285963, EBI-12346463;
CC       Q14957; Q8NDP9: DKFZp547K2416; NbExp=3; IntAct=EBI-8285963, EBI-25842538;
CC       Q14957; Q12959: DLG1; NbExp=2; IntAct=EBI-8285963, EBI-357481;
CC       Q14957; P78352: DLG4; NbExp=4; IntAct=EBI-8285963, EBI-80389;
CC       Q14957; Q7Z7J5: DPPA2; NbExp=3; IntAct=EBI-8285963, EBI-741400;
CC       Q14957; Q14117: DPYS; NbExp=3; IntAct=EBI-8285963, EBI-12275416;
CC       Q14957; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-8285963, EBI-724653;
CC       Q14957; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-8285963, EBI-3443946;
CC       Q14957; A0AVK6: E2F8; NbExp=3; IntAct=EBI-8285963, EBI-7779316;
CC       Q14957; Q658K8: EEF1DP3; NbExp=3; IntAct=EBI-8285963, EBI-10248874;
CC       Q14957; O00472: ELL2; NbExp=3; IntAct=EBI-8285963, EBI-395274;
CC       Q14957; Q96GL9: FAM163A; NbExp=3; IntAct=EBI-8285963, EBI-11793142;
CC       Q14957; P15407: FOSL1; NbExp=3; IntAct=EBI-8285963, EBI-744510;
CC       Q14957; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-8285963, EBI-618189;
CC       Q14957; Q49A26-4: GLYR1; NbExp=3; IntAct=EBI-8285963, EBI-12143817;
CC       Q14957; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-8285963, EBI-2514791;
CC       Q14957; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-8285963, EBI-2558143;
CC       Q14957; Q5T447-2: HECTD3; NbExp=3; IntAct=EBI-8285963, EBI-25854793;
CC       Q14957; P10809: HSPD1; NbExp=3; IntAct=EBI-8285963, EBI-352528;
CC       Q14957; Q8NDH6-2: ICA1L; NbExp=3; IntAct=EBI-8285963, EBI-12141931;
CC       Q14957; Q9NZH6: IL37; NbExp=3; IntAct=EBI-8285963, EBI-3862125;
CC       Q14957; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-8285963, EBI-9089060;
CC       Q14957; O43504: LAMTOR5; NbExp=3; IntAct=EBI-8285963, EBI-713382;
CC       Q14957; Q14847-2: LASP1; NbExp=3; IntAct=EBI-8285963, EBI-9088686;
CC       Q14957; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-8285963, EBI-25835523;
CC       Q14957; Q68G74: LHX8; NbExp=3; IntAct=EBI-8285963, EBI-8474075;
CC       Q14957; Q8N0U6: LINC00518; NbExp=3; IntAct=EBI-8285963, EBI-10264791;
CC       Q14957; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-8285963, EBI-2510853;
CC       Q14957; Q96JB6: LOXL4; NbExp=3; IntAct=EBI-8285963, EBI-749562;
CC       Q14957; Q96LR2: LURAP1; NbExp=3; IntAct=EBI-8285963, EBI-741355;
CC       Q14957; D3DX41: MGC16703; NbExp=3; IntAct=EBI-8285963, EBI-25850974;
CC       Q14957; A0A0A0MR05: MLST8; NbExp=3; IntAct=EBI-8285963, EBI-25835557;
CC       Q14957; Q6IN84-2: MRM1; NbExp=3; IntAct=EBI-8285963, EBI-25835707;
CC       Q14957; Q96H12: MSANTD3; NbExp=3; IntAct=EBI-8285963, EBI-8466227;
CC       Q14957; Q9NPC6: MYOZ2; NbExp=3; IntAct=EBI-8285963, EBI-746712;
CC       Q14957; P41271-2: NBL1; NbExp=3; IntAct=EBI-8285963, EBI-12135485;
CC       Q14957; Q99743: NPAS2; NbExp=3; IntAct=EBI-8285963, EBI-3932727;
CC       Q14957; Q6PHZ7: NR2C2; NbExp=3; IntAct=EBI-8285963, EBI-2802743;
CC       Q14957; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-8285963, EBI-9090919;
CC       Q14957; O43482: OIP5; NbExp=3; IntAct=EBI-8285963, EBI-536879;
CC       Q14957; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-8285963, EBI-25830200;
CC       Q14957; Q495U3: PANX2; NbExp=3; IntAct=EBI-8285963, EBI-17242559;
CC       Q14957; Q9NR21-5: PARP11; NbExp=3; IntAct=EBI-8285963, EBI-17159452;
CC       Q14957; O15534: PER1; NbExp=3; IntAct=EBI-8285963, EBI-2557276;
CC       Q14957; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-8285963, EBI-12891828;
CC       Q14957; Q5SXH7-1: PLEKHS1; NbExp=3; IntAct=EBI-8285963, EBI-26412802;
CC       Q14957; P19388: POLR2E; NbExp=3; IntAct=EBI-8285963, EBI-395189;
CC       Q14957; Q07869: PPARA; NbExp=3; IntAct=EBI-8285963, EBI-78615;
CC       Q14957; O60237-2: PPP1R12B; NbExp=3; IntAct=EBI-8285963, EBI-10700351;
CC       Q14957; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-8285963, EBI-25835994;
CC       Q14957; O43741: PRKAB2; NbExp=3; IntAct=EBI-8285963, EBI-1053424;
CC       Q14957; P62333: PSMC6; NbExp=3; IntAct=EBI-8285963, EBI-357669;
CC       Q14957; Q06323: PSME1; NbExp=3; IntAct=EBI-8285963, EBI-712149;
CC       Q14957; P06454-2: PTMA; NbExp=3; IntAct=EBI-8285963, EBI-10194874;
CC       Q14957; Q8WUD1-2: RAB2B; NbExp=3; IntAct=EBI-8285963, EBI-25835884;
CC       Q14957; P47804-3: RGR; NbExp=3; IntAct=EBI-8285963, EBI-25834767;
CC       Q14957; Q15382: RHEB; NbExp=3; IntAct=EBI-8285963, EBI-1055287;
CC       Q14957; Q8WVD3: RNF138; NbExp=3; IntAct=EBI-8285963, EBI-749039;
CC       Q14957; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-8285963, EBI-751555;
CC       Q14957; P62701: RPS4X; NbExp=3; IntAct=EBI-8285963, EBI-354303;
CC       Q14957; Q9NTN9-3: SEMA4G; NbExp=3; IntAct=EBI-8285963, EBI-9089805;
CC       Q14957; O60902-3: SHOX2; NbExp=3; IntAct=EBI-8285963, EBI-9092164;
CC       Q14957; Q13573: SNW1; NbExp=3; IntAct=EBI-8285963, EBI-632715;
CC       Q14957; Q496A3: SPATS1; NbExp=3; IntAct=EBI-8285963, EBI-3923692;
CC       Q14957; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-8285963, EBI-12408727;
CC       Q14957; Q13586: STIM1; NbExp=3; IntAct=EBI-8285963, EBI-448878;
CC       Q14957; O15273: TCAP; NbExp=3; IntAct=EBI-8285963, EBI-954089;
CC       Q14957; Q86WV5: TEN1; NbExp=3; IntAct=EBI-8285963, EBI-2562799;
CC       Q14957; P54274-2: TERF1; NbExp=3; IntAct=EBI-8285963, EBI-711018;
CC       Q14957; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-8285963, EBI-12090309;
CC       Q14957; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-8285963, EBI-12833746;
CC       Q14957; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-8285963, EBI-17438286;
CC       Q14957; O60830: TIMM17B; NbExp=3; IntAct=EBI-8285963, EBI-2372529;
CC       Q14957; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-8285963, EBI-25830583;
CC       Q14957; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-8285963, EBI-9089156;
CC       Q14957; P36406: TRIM23; NbExp=3; IntAct=EBI-8285963, EBI-740098;
CC       Q14957; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-8285963, EBI-17716262;
CC       Q14957; Q6PF05: TTC23L; NbExp=3; IntAct=EBI-8285963, EBI-8656864;
CC       Q14957; P49459: UBE2A; NbExp=3; IntAct=EBI-8285963, EBI-2339348;
CC       Q14957; Q13404: UBE2V1; NbExp=3; IntAct=EBI-8285963, EBI-1050671;
CC       Q14957; Q9P1Q0-4: VPS54; NbExp=3; IntAct=EBI-8285963, EBI-25835297;
CC       Q14957; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-8285963, EBI-10316321;
CC       Q14957; O43829: ZBTB14; NbExp=3; IntAct=EBI-8285963, EBI-10176632;
CC       Q14957; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-8285963, EBI-14104088;
CC       Q14957; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-8285963, EBI-746345;
CC       Q14957; Q96JL9-2: ZNF333; NbExp=3; IntAct=EBI-8285963, EBI-25835852;
CC       Q14957; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-8285963, EBI-18036029;
CC       Q14957; B7Z3E8; NbExp=3; IntAct=EBI-8285963, EBI-25831617;
CC       Q14957; Q62936: Dlg3; Xeno; NbExp=6; IntAct=EBI-8285963, EBI-349596;
CC       Q14957; P31016: Dlg4; Xeno; NbExp=2; IntAct=EBI-8285963, EBI-375655;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26875626};
CC       Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane;
CC       Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain with predominant
CC       expression is in the cerebellum, also present in the hippocampus,
CC       amygdala, caudate nucleus, corpus callosum, subthalamic nuclei and
CC       thalamus. Detected in the heart, skeletal muscle and pancreas.
CC       {ECO:0000269|PubMed:9037519}.
CC   -!- DOMAIN: A hydrophobic region that gives rise to the prediction of a
CC       transmembrane span does not cross the membrane, but is part of a
CC       discontinuously helical region that dips into the membrane and is
CC       probably part of the pore and of the selectivity filter.
CC       {ECO:0000250|UniProtKB:Q00960}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. NR2C/GRIN2C subfamily. {ECO:0000305}.
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DR   EMBL; L76224; AAA88096.1; -; mRNA.
DR   EMBL; AC068874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC140801; AAI40802.1; -; mRNA.
DR   CCDS; CCDS32724.1; -.
DR   RefSeq; NP_000826.2; NM_000835.4.
DR   PDB; 8E92; EM; 3.96 A; B/D=26-849.
DR   PDB; 8E93; EM; 3.71 A; B/D=26-849.
DR   PDB; 8E94; EM; 3.72 A; B/D=26-849.
DR   PDB; 8E97; EM; 4.19 A; B/D=26-849.
DR   PDB; 8E98; EM; 3.75 A; B/D=26-849.
DR   PDB; 8E99; EM; 4.24 A; D=26-849.
DR   PDBsum; 8E92; -.
DR   PDBsum; 8E93; -.
DR   PDBsum; 8E94; -.
DR   PDBsum; 8E97; -.
DR   PDBsum; 8E98; -.
DR   PDBsum; 8E99; -.
DR   AlphaFoldDB; Q14957; -.
DR   EMDB; EMD-27953; -.
DR   EMDB; EMD-27954; -.
DR   EMDB; EMD-27955; -.
DR   EMDB; EMD-27958; -.
DR   EMDB; EMD-27959; -.
DR   EMDB; EMD-27960; -.
DR   EMDB; EMD-27961; -.
DR   SMR; Q14957; -.
DR   BioGRID; 109162; 14.
DR   ComplexPortal; CPX-286; NMDA receptor complex, GluN1-GluN2C.
DR   IntAct; Q14957; 108.
DR   MINT; Q14957; -.
DR   STRING; 9606.ENSP00000293190; -.
DR   BindingDB; Q14957; -.
DR   ChEMBL; CHEMBL4109; -.
DR   DrugBank; DB00659; Acamprosate.
DR   DrugBank; DB01238; Aripiprazole.
DR   DrugBank; DB00289; Atomoxetine.
DR   DrugBank; DB00647; Dextropropoxyphene.
DR   DrugBank; DB00843; Donepezil.
DR   DrugBank; DB00228; Enflurane.
DR   DrugBank; DB11823; Esketamine.
DR   DrugBank; DB13146; Fluciclovine (18F).
DR   DrugBank; DB06741; Gavestinel.
DR   DrugBank; DB00142; Glutamic acid.
DR   DrugBank; DB00145; Glycine.
DR   DrugBank; DB00874; Guaifenesin.
DR   DrugBank; DB06738; Ketobemidone.
DR   DrugBank; DB09409; Magnesium acetate tetrahydrate.
DR   DrugBank; DB09481; Magnesium carbonate.
DR   DrugBank; DB01043; Memantine.
DR   DrugBank; DB00454; Meperidine.
DR   DrugBank; DB00333; Methadone.
DR   DrugBank; DB04896; Milnacipran.
DR   DrugBank; DB00312; Pentobarbital.
DR   DrugBank; DB01174; Phenobarbital.
DR   DrugBank; DB01708; Prasterone.
DR   DrugBank; DB00418; Secobarbital.
DR   DrugBank; DB01520; Tenocyclidine.
DR   DrugBank; DB00193; Tramadol.
DR   DrugCentral; Q14957; -.
DR   GuidetoPHARMACOLOGY; 458; -.
DR   TCDB; 1.A.10.1.3; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR   GlyCosmos; Q14957; 6 sites, No reported glycans.
DR   GlyGen; Q14957; 6 sites.
DR   iPTMnet; Q14957; -.
DR   PhosphoSitePlus; Q14957; -.
DR   BioMuta; GRIN2C; -.
DR   DMDM; 313104210; -.
DR   jPOST; Q14957; -.
DR   MassIVE; Q14957; -.
DR   PaxDb; 9606-ENSP00000293190; -.
DR   PeptideAtlas; Q14957; -.
DR   ProteomicsDB; 60260; -.
DR   ABCD; Q14957; 3 sequenced antibodies.
DR   Antibodypedia; 19474; 344 antibodies from 35 providers.
DR   DNASU; 2905; -.
DR   Ensembl; ENST00000293190.10; ENSP00000293190.5; ENSG00000161509.14.
DR   GeneID; 2905; -.
DR   KEGG; hsa:2905; -.
DR   MANE-Select; ENST00000293190.10; ENSP00000293190.5; NM_000835.6; NP_000826.2.
DR   UCSC; uc002jlt.3; human.
DR   AGR; HGNC:4587; -.
DR   CTD; 2905; -.
DR   DisGeNET; 2905; -.
DR   GeneCards; GRIN2C; -.
DR   HGNC; HGNC:4587; GRIN2C.
DR   HPA; ENSG00000161509; Tissue enriched (brain).
DR   MIM; 138254; gene.
DR   neXtProt; NX_Q14957; -.
DR   OpenTargets; ENSG00000161509; -.
DR   PharmGKB; PA28981; -.
DR   VEuPathDB; HostDB:ENSG00000161509; -.
DR   eggNOG; KOG1053; Eukaryota.
DR   GeneTree; ENSGT00940000156964; -.
DR   HOGENOM; CLU_002039_1_0_1; -.
DR   InParanoid; Q14957; -.
DR   OMA; FPIHYGD; -.
DR   OrthoDB; 1034721at2759; -.
DR   PhylomeDB; Q14957; -.
DR   TreeFam; TF314731; -.
DR   PathwayCommons; Q14957; -.
DR   Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR   Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
DR   Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR   Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission.
DR   Reactome; R-HSA-9620244; Long-term potentiation.
DR   SignaLink; Q14957; -.
DR   SIGNOR; Q14957; -.
DR   BioGRID-ORCS; 2905; 10 hits in 1157 CRISPR screens.
DR   GeneWiki; GRIN2C; -.
DR   GenomeRNAi; 2905; -.
DR   Pharos; Q14957; Tclin.
DR   PRO; PR:Q14957; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q14957; Protein.
DR   Bgee; ENSG00000161509; Expressed in right hemisphere of cerebellum and 104 other cell types or tissues.
DR   ExpressionAtlas; Q14957; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; NAS:ComplexPortal.
DR   GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IDA:UniProtKB.
DR   GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007420; P:brain development; NAS:ARUK-UCL.
DR   GO; GO:0097553; P:calcium ion transmembrane import into cytosol; IDA:UniProtKB.
DR   GO; GO:0033058; P:directional locomotion; IEA:Ensembl.
DR   GO; GO:0098976; P:excitatory chemical synaptic transmission; NAS:ARUK-UCL.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IBA:GO_Central.
DR   GO; GO:0007215; P:glutamate receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:ComplexPortal.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IBA:GO_Central.
DR   GO; GO:0098655; P:monoatomic cation transmembrane transport; ISS:ComplexPortal.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:ComplexPortal.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:ComplexPortal.
DR   GO; GO:1903539; P:protein localization to postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:1904062; P:regulation of monoatomic cation transmembrane transport; ISO:ComplexPortal.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; NAS:ComplexPortal.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; NAS:ARUK-UCL.
DR   GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   CDD; cd06378; PBP1_iGluR_NMDA_NR2; 1.
DR   CDD; cd13718; PBP2_iGluR_NMDA_Nr2; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR018884; NMDAR2_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF361; GLUTAMATE RECEPTOR IONOTROPIC, NMDA 2C; 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; PF10565; NMDAR2_C; 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   Genevisible; Q14957; HS.
PE   1: Evidence at protein level;
KW   3D-structure; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1233
FT                   /note="Glutamate receptor ionotropic, NMDA 2C"
FT                   /id="PRO_0000011580"
FT   TOPO_DOM        20..554
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   TRANSMEM        555..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   TOPO_DOM        574..600
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   INTRAMEM        601..620
FT                   /note="Discontinuously helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   TOPO_DOM        621..627
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   TRANSMEM        628..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   TOPO_DOM        644..814
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   TRANSMEM        815..834
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   TOPO_DOM        835..1233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   REGION          601..620
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   REGION          920..995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1231..1233
FT                   /note="PDZ-binding"
FT   COMPBIAS        929..960
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         509..511
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:Q00959"
FT   BINDING         511
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   BINDING         516
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:Q00959"
FT   BINDING         687..688
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:Q00959"
FT   BINDING         729
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:Q00960"
FT   SITE            612
FT                   /note="Functional determinant of NMDA receptors"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         875
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01098"
FT   MOD_RES         881
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01098"
FT   MOD_RES         912
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00961"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        539
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        685
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..317
FT                   /evidence="ECO:0000250|UniProtKB:Q00959"
FT   DISULFID        426..453
FT                   /evidence="ECO:0000250|UniProtKB:Q00959"
FT   DISULFID        433..454
FT                   /evidence="ECO:0000250|UniProtKB:Q00959"
FT   DISULFID        743..798
FT                   /evidence="ECO:0000250|UniProtKB:Q00959"
FT   VARIANT         18..1233
FT                   /note="Missing (found in a patient with autism spectrum
FT                   disorder; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079958"
FT   VARIANT         90
FT                   /note="V -> I (in dbSNP:rs192960268)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079959"
FT   VARIANT         166
FT                   /note="A -> V (in dbSNP:rs201199917)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079960"
FT   VARIANT         573
FT                   /note="M -> T"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079961"
FT   VARIANT         641
FT                   /note="A -> T (in dbSNP:rs746610735)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079962"
FT   VARIANT         679
FT                   /note="R -> C (found in a patient with schizophrenia;
FT                   uncertain significance; dbSNP:rs1381530257)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079963"
FT   VARIANT         863
FT                   /note="I -> T (found in a patient with autism spectrum
FT                   disorder; uncertain significance; dbSNP:rs1308468356)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079964"
FT   VARIANT         871
FT                   /note="Q -> R (in dbSNP:rs765016248)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079965"
FT   VARIANT         877
FT                   /note="P -> S (in dbSNP:rs139011774)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079966"
FT   VARIANT         911
FT                   /note="S -> I (in dbSNP:rs370546831)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079967"
FT   VARIANT         982
FT                   /note="P -> A (in dbSNP:rs960726960)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079968"
FT   VARIANT         989
FT                   /note="S -> P (found in a patient with schizophrenia;
FT                   uncertain significance; dbSNP:rs552196496)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079969"
FT   VARIANT         995
FT                   /note="S -> L (found in a patient with schizophrenia;
FT                   uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079970"
FT   VARIANT         1079
FT                   /note="H -> Y (in dbSNP:rs889196426)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079971"
FT   VARIANT         1141
FT                   /note="P -> A (in dbSNP:rs751640851)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079972"
FT   VARIANT         1180
FT                   /note="G -> R (in dbSNP:rs115230539)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079973"
FT   VARIANT         1196
FT                   /note="T -> I (in dbSNP:rs143282101)"
FT                   /evidence="ECO:0000269|PubMed:22833210"
FT                   /id="VAR_079974"
FT   VARIANT         1209
FT                   /note="R -> S (in dbSNP:rs3744215)"
FT                   /id="VAR_037634"
FT   MUTAGEN         550
FT                   /note="P->R: Changed glutamate-gated calcium ion channel
FT                   activity characterized by increased glutamate and glycine
FT                   potency."
FT                   /evidence="ECO:0000269|PubMed:28095420"
FT   CONFLICT        1048
FT                   /note="E -> EPPE (in Ref. 3; AAI40802)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1057
FT                   /note="P -> K (in Ref. 1; AAA88096)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1233 AA;  134209 MW;  7B1F2F7995C0D689 CRC64;
     MGGALGPALL LTSLFGAWAG LGPGQGEQGM TVAVVFSSSG PPQAQFRARL TPQSFLDLPL
     EIQPLTVGVN TTNPSSLLTQ ICGLLGAAHV HGIVFEDNVD TEAVAQILDF ISSQTHVPIL
     SISGGSAVVL TPKEPGSAFL QLGVSLEQQL QVLFKVLEEY DWSAFAVITS LHPGHALFLE
     GVRAVADASH VSWRLLDVVT LELGPGGPRA RTQRLLRQLD APVFVAYCSR EEAEVLFAEA
     AQAGLVGPGH VWLVPNLALG STDAPPATFP VGLISVVTES WRLSLRQKVR DGVAILALGA
     HSYWRQHGTL PAPAGDCRVH PGPVSPAREA FYRHLLNVTW EGRDFSFSPG GYLVQPTMVV
     IALNRHRLWE MVGRWEHGVL YMKYPVWPRY SASLQPVVDS RHLTVATLEE RPFVIVESPD
     PGTGGCVPNT VPCRRQSNHT FSSGDVAPYT KLCCKGFCID ILKKLARVVK FSYDLYLVTN
     GKHGKRVRGV WNGMIGEVYY KRADMAIGSL TINEERSEIV DFSVPFVETG ISVMVARSNG
     TVSPSAFLEP YSPAVWVMMF VMCLTVVAIT VFMFEYFSPV SYNQNLTRGK KSGGPAFTIG
     KSVWLLWALV FNNSVPIENP RGTTSKIMVL VWAFFAVIFL ASYTANLAAF MIQEQYIDTV
     SGLSDKKFQR PQDQYPPFRF GTVPNGSTER NIRSNYRDMH THMVKFNQRS VEDALTSLKM
     GKLDAFIYDA AVLNYMAGKD EGCKLVTIGS GKVFATTGYG IAMQKDSHWK RAIDLALLQF
     LGDGETQKLE TVWLSGICQN EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAWEHLVY
     WKLRHSVPNS SQLDFLLAFS RGIYSCFSGV QSLASPPRQA SPDLTASSAQ ASVLKMLQAA
     RDMVTTAGVS SSLDRATRTI ENWGGGRRAP PPSPCPTPRS GPSPCLPTPD PPPEPSPTGW
     GPPDGGRAAL VRRAPQPPGR PPTPGPPLSD VSRVSRRPAW EARWPVRTGH CGRHLSASER
     PLSPARCHYS SFPRADRSGR PFLPLFPELE DLPLLGPEQL ARREALLHAA WARGSRPRHA
     SLPSSVAEAF ARPSSLPAGC TGPACARPDG HSACRRLAQA QSMCLPIYRE ACQEGEQAGA
     PAWQHRQHVC LHAHAHLPFC WGAVCPHLPP CASHGSWLSG AWGPLGHRGR TLGLGTGYRD
     SGGLDEISRV ARGTQGFPGP CTWRRISSLE SEV
//