ID   NMDE4_HUMAN             Reviewed;        1336 AA.
AC   O15399;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   13-FEB-2019, entry version 170.
DE   RecName: Full=Glutamate receptor ionotropic, NMDA 2D;
DE            Short=GluN2D;
DE   AltName: Full=EB11;
DE   AltName: Full=Glutamate [NMDA] receptor subunit epsilon-4;
DE   AltName: Full=N-methyl D-aspartate receptor subtype 2D;
DE            Short=NMDAR2D;
DE            Short=NR2D;
DE   Flags: Precursor;
GN   Name=GRIN2D; Synonyms=GluN2D, NMDAR2D;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   SUBUNIT.
RC   TISSUE=Fetal brain;
RX   PubMed=9489750;
RA   Hess S.D., Daggett L.P., Deal C., Lu C.-C., Johnson E.C.,
RA   Velicelebi G.;
RT   "Functional characterization of human N-methyl-D-aspartate subtype
RT   1A/2D receptors.";
RL   J. Neurochem. 70:1269-1279(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   FUNCTION, INVOLVEMENT IN EIEE46, VARIANT EIEE46 ILE-667, AND
RP   CHARACTERIZATION OF VARIANT EIEE46 ILE-667.
RX   PubMed=27616483; DOI=10.1016/j.ajhg.2016.07.013;
RA   Li D., Yuan H., Ortiz-Gonzalez X.R., Marsh E.D., Tian L.,
RA   McCormick E.M., Kosobucki G.J., Chen W., Schulien A.J., Chiavacci R.,
RA   Tankovic A., Naase C., Brueckner F., von Stuelpnagel-Steinbeis C.,
RA   Hu C., Kusumoto H., Hedrich U.B., Elsen G., Hoertnagel K.,
RA   Aizenman E., Lemke J.R., Hakonarson H., Traynelis S.F., Falk M.J.;
RT   "GRIN2D recurrent de novo dominant mutation causes a severe epileptic
RT   encephalopathy treatable with NMDA receptor channel blockers.";
RL   Am. J. Hum. Genet. 99:802-816(2016).
RN   [4]
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
RT   Distinct Modes of Action and Impacts on Circuit Function.";
RL   Neuron 89:983-999(2016).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF MET-845.
RX   PubMed=28126851; DOI=10.1124/mol.116.106781;
RA   Chen W., Tankovic A., Burger P.B., Kusumoto H., Traynelis S.F.,
RA   Yuan H.;
RT   "Functional evaluation of a de novo GRIN2A mutation identified in a
RT   patient with profound global developmental delay and refractory
RT   epilepsy.";
RL   Mol. Pharmacol. 91:317-330(2017).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF PRO-580.
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.,
RA   Pecha J., Bhattacharya S., Petrovski S., Cohen A.E., Aizenman E.,
RA   Traynelis S.F., Yuan H.;
RT   "Molecular mechanism of disease-associated mutations in the pre-M1
RT   helix of NMDA receptors and potential rescue pharmacology.";
RL   PLoS Genet. 13:E1006536-E1006536(2017).
RN   [7]
RP   VARIANTS [LARGE SCALE ANALYSIS] SER-140; ARG-286 AND GLY-527.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [8]
RP   VARIANTS VAL-466; LEU-592; VAL-733; HIS-872; ILE-883; VAL-922;
RP   THR-926; PRO-982 AND SER-1317.
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.
CC       Channel activation requires binding of the neurotransmitter
CC       glutamate to the epsilon subunit, glycine binding to the zeta
CC       subunit, plus membrane depolarization to eliminate channel
CC       inhibition by Mg(2+) (PubMed:9489750, PubMed:27616483,
CC       PubMed:26875626, PubMed:28126851). Sensitivity to glutamate and
CC       channel kinetics depend on the subunit composition
CC       (PubMed:9489750). {ECO:0000269|PubMed:26875626,
CC       ECO:0000269|PubMed:27616483, ECO:0000269|PubMed:28095420,
CC       ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:9489750}.
CC   -!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
CC       of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
CC       GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:9489750,
CC       PubMed:26875626, PubMed:28126851). 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
CC       (By similarity). {ECO:0000250, ECO:0000269|PubMed:26875626,
CC       ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:9489750,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       Q62936:Dlg3 (xeno); NbExp=2; IntAct=EBI-1754030, EBI-349596;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26875626,
CC       ECO:0000269|PubMed:28126851, ECO:0000269|PubMed:9489750}; Multi-
CC       pass membrane protein. Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: A hydrophobic region that gives rise to the prediction of
CC       a 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   -!- DISEASE: Epileptic encephalopathy, early infantile, 46 (EIEE46)
CC       [MIM:617162]: A form of epileptic encephalopathy, a heterogeneous
CC       group of severe childhood onset epilepsies characterized by
CC       refractory seizures, neurodevelopmental impairment, and poor
CC       prognosis. Development is normal prior to seizure onset, after
CC       which cognitive and motor delays become apparent.
CC       {ECO:0000269|PubMed:27616483}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
CC       1.A.10.1) family. NR2D/GRIN2D subfamily. {ECO:0000305}.
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DR   EMBL; U77783; AAC15910.1; -; mRNA.
DR   EMBL; AC008403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS12719.1; -.
DR   RefSeq; NP_000827.2; NM_000836.2.
DR   RefSeq; XP_011525174.1; XM_011526872.1.
DR   UniGene; Hs.445015; -.
DR   ProteinModelPortal; O15399; -.
DR   SMR; O15399; -.
DR   BioGrid; 109163; 3.
DR   ComplexPortal; CPX-289; NMDA receptor complex, GluN1-GluN2D.
DR   IntAct; O15399; 5.
DR   MINT; O15399; -.
DR   STRING; 9606.ENSP00000263269; -.
DR   BindingDB; O15399; -.
DR   ChEMBL; CHEMBL2591; -.
DR   DrugBank; DB00659; Acamprosate.
DR   DrugBank; DB06151; Acetylcysteine.
DR   DrugBank; DB00289; Atomoxetine.
DR   DrugBank; DB00996; Gabapentin.
DR   DrugBank; DB06741; Gavestinel.
DR   DrugBank; DB06738; Ketobemidone.
DR   DrugBank; DB00142; L-Glutamic Acid.
DR   DrugBank; DB04896; Milnacipran.
DR   DrugBank; DB01173; Orphenadrine.
DR   DrugBank; DB00312; Pentobarbital.
DR   DrugBank; DB00454; Pethidine.
DR   DrugBank; DB01174; Phenobarbital.
DR   DrugBank; DB01708; Prasterone.
DR   DrugBank; DB00418; Secobarbital.
DR   DrugBank; DB01520; Tenocyclidine.
DR   iPTMnet; O15399; -.
DR   PhosphoSitePlus; O15399; -.
DR   BioMuta; GRIN2D; -.
DR   EPD; O15399; -.
DR   jPOST; O15399; -.
DR   PaxDb; O15399; -.
DR   PeptideAtlas; O15399; -.
DR   PRIDE; O15399; -.
DR   ProteomicsDB; 48638; -.
DR   Ensembl; ENST00000263269; ENSP00000263269; ENSG00000105464.
DR   GeneID; 2906; -.
DR   KEGG; hsa:2906; -.
DR   UCSC; uc002pjc.4; human.
DR   CTD; 2906; -.
DR   DisGeNET; 2906; -.
DR   EuPathDB; HostDB:ENSG00000105464.3; -.
DR   GeneCards; GRIN2D; -.
DR   H-InvDB; HIX0040164; -.
DR   HGNC; HGNC:4588; GRIN2D.
DR   MalaCards; GRIN2D; -.
DR   MIM; 602717; gene.
DR   MIM; 617162; phenotype.
DR   neXtProt; NX_O15399; -.
DR   OpenTargets; ENSG00000105464; -.
DR   Orphanet; 442835; Undetermined early-onset epileptic encephalopathy.
DR   PharmGKB; PA28982; -.
DR   eggNOG; KOG1053; Eukaryota.
DR   eggNOG; ENOG410XNUR; LUCA.
DR   GeneTree; ENSGT00940000159109; -.
DR   HOGENOM; HOG000113803; -.
DR   HOVERGEN; HBG052637; -.
DR   InParanoid; O15399; -.
DR   KO; K05212; -.
DR   OMA; YPYAERL; -.
DR   OrthoDB; 188544at2759; -.
DR   PhylomeDB; O15399; -.
DR   TreeFam; TF314731; -.
DR   Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR   Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
DR   Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission.
DR   Reactome; R-HSA-9620244; Long-term potentiation.
DR   SignaLink; O15399; -.
DR   GeneWiki; GRIN2D; -.
DR   GenomeRNAi; 2906; -.
DR   PRO; PR:O15399; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000105464; Expressed in 83 organ(s), highest expression level in hypothalamus.
DR   Genevisible; O15399; HS.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IDA:UniProtKB.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:UniProtKB.
DR   GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
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:0098976; P:excitatory chemical synaptic transmission; NAS:ARUK-UCL.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IBA:GO_Central.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IBA:GO_Central.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; NAS:ARUK-UCL.
DR   GO; GO:0001964; P:startle response; IEA:Ensembl.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_rcpt_met.
DR   InterPro; IPR001320; Iontro_rcpt.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell junction; Cell membrane; Complete proteome;
KW   Disease mutation; Disulfide bond; Epilepsy; Glycoprotein; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
KW   Methylation; Phosphoprotein; Polymorphism; Postsynaptic cell membrane;
KW   Receptor; Reference proteome; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   1336       Glutamate receptor ionotropic, NMDA 2D.
FT                                /FTId=PRO_0000011583.
FT   TOPO_DOM     28    584       Extracellular.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   TRANSMEM    585    603       Helical. {ECO:0000250|UniProtKB:Q00960}.
FT   TOPO_DOM    604    630       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   INTRAMEM    631    650       Discontinuously helical.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   TOPO_DOM    651    657       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   TRANSMEM    658    673       Helical. {ECO:0000250|UniProtKB:Q00960}.
FT   TOPO_DOM    674    844       Extracellular.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   TRANSMEM    845    864       Helical. {ECO:0000250|UniProtKB:Q00960}.
FT   TOPO_DOM    865   1336       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   REGION      539    541       Glutamate binding.
FT                                {ECO:0000250|UniProtKB:Q00959}.
FT   REGION      631    650       Pore-forming.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   REGION      717    718       Glutamate binding.
FT                                {ECO:0000250|UniProtKB:Q00959}.
FT   MOTIF      1334   1336       PDZ-binding. {ECO:0000250}.
FT   COMPBIAS    281    286       Poly-Gly.
FT   COMPBIAS    908    916       Poly-Pro.
FT   COMPBIAS   1035   1040       Poly-Ala.
FT   COMPBIAS   1209   1213       Poly-Pro.
FT   COMPBIAS   1244   1247       Poly-Ala.
FT   BINDING     541    541       Glutamate.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   BINDING     546    546       Glutamate.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   BINDING     759    759       Glutamate.
FT                                {ECO:0000250|UniProtKB:Q00960}.
FT   SITE        642    642       Functional determinant of NMDA receptors.
FT                                {ECO:0000250}.
FT   MOD_RES    1316   1316       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:Q03391}.
FT   MOD_RES    1326   1326       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q03391}.
FT   CARBOHYD     92     92       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    352    352       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    366    366       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    467    467       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    569    569       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    104    348       {ECO:0000250|UniProtKB:Q00959}.
FT   DISULFID    455    483       {ECO:0000250|UniProtKB:Q00959}.
FT   DISULFID    462    484       {ECO:0000250|UniProtKB:Q00959}.
FT   DISULFID    773    828       {ECO:0000250|UniProtKB:Q00959}.
FT   VARIANT     140    140       P -> S (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035698.
FT   VARIANT     286    286       G -> R (in a breast cancer sample;
FT                                somatic mutation; dbSNP:rs1259830926).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035699.
FT   VARIANT     466    466       L -> V (found in a patient with
FT                                schizophrenia; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079975.
FT   VARIANT     527    527       E -> G (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035700.
FT   VARIANT     592    592       M -> L (found in a patient with autism
FT                                spectrum disorder; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079976.
FT   VARIANT     667    667       V -> I (in EIEE46; gain-of-function
FT                                mutation that potentiates ionotropic
FT                                glutamate receptor signaling; mutant
FT                                receptors are activated by lower
FT                                concentrations of glutamate and glycine
FT                                and show slower deactivation after
FT                                agonist removal as well as decreased
FT                                sensitivity to allosteric inhibitors
FT                                indicating that NMDA glutamate receptor
FT                                activity is changed; dbSNP:rs886040861).
FT                                {ECO:0000269|PubMed:27616483}.
FT                                /FTId=VAR_077103.
FT   VARIANT     733    733       M -> V (found in a patient with
FT                                schizophrenia; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079977.
FT   VARIANT     872    872       R -> H (found in a patient with
FT                                schizophrenia; unknown pathological
FT                                significance; dbSNP:rs750543659).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079978.
FT   VARIANT     883    883       M -> I (in dbSNP:rs781567305).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079979.
FT   VARIANT     922    922       A -> V (found in patients with
FT                                schizophrenia; unknown pathological
FT                                significance; dbSNP:rs571334598).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079980.
FT   VARIANT     926    926       A -> T (found in a patient with autism
FT                                spectrum disorder; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079981.
FT   VARIANT     982    982       A -> P (in dbSNP:rs1225338399).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079982.
FT   VARIANT    1317   1317       G -> S (in dbSNP:rs191119443).
FT                                {ECO:0000269|PubMed:22833210}.
FT                                /FTId=VAR_079983.
FT   MUTAGEN     580    580       P->R: Changed glutamate-gated calcium ion
FT                                channel activity characterized by
FT                                increased glutamate and glycine potency.
FT                                {ECO:0000269|PubMed:28095420}.
FT   MUTAGEN     845    845       M->V: Increased glutamate and glycine
FT                                agonist potency.
FT                                {ECO:0000269|PubMed:28126851}.
FT   CONFLICT    924    924       R -> G (in Ref. 1; AAC15910).
FT                                {ECO:0000305}.
FT   CONFLICT   1005   1005       P -> A (in Ref. 1; AAC15910).
FT                                {ECO:0000305}.
FT   CONFLICT   1097   1097       R -> C (in Ref. 1; AAC15910).
FT                                {ECO:0000305}.
FT   CONFLICT   1130   1130       E -> D (in Ref. 1; AAC15910).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1336 AA;  143752 MW;  0DB7559056AE4593 CRC64;
     MRGAGGPRGP RGPAKMLLLL ALACASPFPE EAPGPGGAGG PGGGLGGARP LNVALVFSGP
     AYAAEAARLG PAVAAAVRSP GLDVRPVALV LNGSDPRSLV LQLCDLLSGL RVHGVVFEDD
     SRAPAVAPIL DFLSAQTSLP IVAVHGGAAL VLTPKEKGST FLQLGSSTEQ QLQVIFEVLE
     EYDWTSFVAV TTRAPGHRAF LSYIEVLTDG SLVGWEHRGA LTLDPGAGEA VLSAQLRSVS
     AQIRLLFCAR EEAEPVFRAA EEAGLTGSGY VWFMVGPQLA GGGGSGAPGE PPLLPGGAPL
     PAGLFAVRSA GWRDDLARRV AAGVAVVARG AQALLRDYGF LPELGHDCRA QNRTHRGESL
     HRYFMNITWD NRDYSFNEDG FLVNPSLVVI SLTRDRTWEV VGSWEQQTLR LKYPLWSRYG
     RFLQPVDDTQ HLTVATLEER PFVIVEPADP ISGTCIRDSV PCRSQLNRTH SPPPDAPRPE
     KRCCKGFCID ILKRLAHTIG FSYDLYLVTN GKHGKKIDGV WNGMIGEVFY QRADMAIGSL
     TINEERSEIV DFSVPFVETG ISVMVARSNG TVSPSAFLEP YSPAVWVMMF VMCLTVVAVT
     VFIFEYLSPV GYNRSLATGK RPGGSTFTIG KSIWLLWALV FNNSVPVENP RGTTSKIMVL
     VWAFFAVIFL ASYTANLAAF MIQEEYVDTV SGLSDRKFQR PQEQYPPLKF GTVPNGSTEK
     NIRSNYPDMH SYMVRYNQPR VEEALTQLKA GKLDAFIYDA AVLNYMARKD EGCKLVTIGS
     GKVFATTGYG IALHKGSRWK RPIDLALLQF LGDDEIEMLE RLWLSGICHN DKIEVMSSKL
     DIDNMAGVFY MLLVAMGLSL LVFAWEHLVY WRLRHCLGPT HRMDFLLAFS RGMYSCCSAE
     AAPPPAKPPP PPQPLPSPAY PAPRPAPGPA PFVPRERASV DRWRRTKGAG PPGGAGLADG
     FHRYYGPIEP QGLGLGLGEA RAAPRGAAGR PLSPPAAQPP QKPPPSYFAI VRDKEPAEPP
     AGAFPGFPSP PAPPAAAATA VGPPLCRLAF EDESPPAPAR WPRSDPESQP LLGPGAGGAG
     GTGGAGGGAP AAPPPCRAAP PPCPYLDLEP SPSDSEDSES LGGASLGGLE PWWFADFPYP
     YAERLGPPPG RYWSVDKLGG WRAGSWDYLP PRSGPAAWHC RHCASLELLP PPRHLSCSHD
     GLDGGWWAPP PPPWAAGPLP RRRARCGCPR SHPHRPRASH RTPAAAAPHH HRHRRAAGGW
     DLPPPAPTSR SLEDLSSCPR AAPARRLTGP SRHARRCPHA AHWGPPLPTA SHRRHRGGDL
     GTRRGSAHFS SLESEV
//