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Glutamate receptor ionotropic, NMDA 2B (GluN2B) (Glutamate [NMDA] receptor subunit epsilon-2) (N-methyl D-aspartate receptor subtype 2B) (NMDAR2B) (NR2B)

 NMDE2_MOUSE             Reviewed;        1482 AA.
Q01097; Q9DCB2;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
20-JUN-2001, sequence version 3.
22-NOV-2017, entry version 176.
RecName: Full=Glutamate receptor ionotropic, NMDA 2B;
Short=GluN2B;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-2 {ECO:0000303|PubMed:1377365};
AltName: Full=N-methyl D-aspartate receptor subtype 2B;
Short=NMDAR2B;
Short=NR2B;
Flags: Precursor;
Name=Grin2b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
AND TISSUE SPECIFICITY.
PubMed=1377365; DOI=10.1038/358036a0;
Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E.,
Araki K., Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.;
"Molecular diversity of the NMDA receptor channel.";
Nature 358:36-41(1992).
[2]
SEQUENCE REVISION.
Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E.,
Araki K., Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=8789948;
Kutsuwada T., Sakimura K., Manabe T., Takayama C., Katakura N.,
Kushiya E., Natsume R., Watanabe M., Inoue Y., Yagi T., Aizawa S.,
Arakawa M., Takahashi T., Nakamura Y., Mori H., Mishina M.;
"Impairment of suckling response, trigeminal neuronal pattern
formation, and hippocampal LTD in NMDA receptor epsilon 2 subunit
mutant mice.";
Neuron 16:333-344(1996).
[5]
PHOSPHORYLATION AT TYR-1472.
PubMed=12451687;
Nakazawa T., Tezuka T., Yamamoto T.;
"Regulation of NMDA receptor function by Fyn-mediated tyrosine
phosphorylation.";
Nihon Shinkei Seishin Yakurigaku Zasshi 22:165-167(2002).
[6]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
PubMed=12008020; DOI=10.1016/S0169-328X(02)00173-0;
Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.;
"Cloning and characterization of a novel NMDA receptor subunit NR3B: a
dominant subunit that reduces calcium permeability.";
Brain Res. Mol. Brain Res. 100:43-52(2002).
[7]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
PubMed=14602821;
Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
"Specific assembly with the NMDA receptor 3B subunit controls surface
expression and calcium permeability of NMDA receptors.";
J. Neurosci. 23:10064-10073(2003).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
INTERACTION WITH HIP1.
PubMed=17329427; DOI=10.1523/JNEUROSCI.5175-06.2007;
Metzler M., Gan L., Wong T.P., Liu L., Helm J., Liu L., Georgiou J.,
Wang Y., Bissada N., Cheng K., Roder J.C., Wang Y.T., Hayden M.R.;
"NMDA receptor function and NMDA receptor-dependent phosphorylation of
huntingtin is altered by the endocytic protein HIP1.";
J. Neurosci. 27:2298-2308(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-962; TYR-1039; TYR-1109;
TYR-1133 AND TYR-1155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[12]
INTERACTION WITH NETO1.
PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M.,
Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M.,
Roder J.C., Salter M.W., McInnes R.R.;
"Neto1 is a novel CUB-domain NMDA receptor-interacting protein
required for synaptic plasticity and learning.";
PLoS Biol. 7:E41-E41(2009).
[13]
FUNCTION, PHOSPHORYLATION AT SER-1303, AND INTERACTION WITH DAPK1.
PubMed=20141836; DOI=10.1016/j.cell.2009.12.055;
Tu W., Xu X., Peng L., Zhong X., Zhang W., Soundarapandian M.M.,
Balel C., Wang M., Jia N., Zhang W., Lew F., Chan S.L., Chen Y.,
Lu Y.;
"DAPK1 interaction with NMDA receptor NR2B subunits mediates brain
damage in stroke.";
Cell 140:222-234(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-917; SER-920;
SER-1058; SER-1061; SER-1064; SER-1143; SER-1255; SER-1259 AND
SER-1303, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=26912815; DOI=10.1124/mol.115.103036;
Stroebel D., Buhl D.L., Knafels J.D., Chanda P.K., Green M.,
Sciabola S., Mony L., Paoletti P., Pandit J.;
"A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor
GluN2B-selective Antagonists.";
Mol. Pharmacol. 89:541-551(2016).
-!- FUNCTION: Component of NMDA receptor complexes that function as
heterotetrameric, ligand-gated ion channels with high calcium
permeability and voltage-dependent sensitivity to magnesium.
Channel activation requires binding of the neurotransmitter
glutamate to the epsilon subunit, glycine binding to the zeta
subunit, plus membrane depolarization to eliminate channel
inhibition by Mg(2+) (PubMed:1377365, PubMed:26912815).
Sensitivity to glutamate and channel kinetics depend on the
subunit composition (PubMed:1377365). In concert with DAPK1 at
extrasynaptic sites, acts as a central mediator for stroke damage.
Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA
receptor channel activity inducing injurious Ca2+ influx through
them, resulting in an irreversible neuronal death
(PubMed:20141836). Contributes to neural pattern formation in the
developing brain (PubMed:8789948). Plays a role in long-term
depression (LTD) of hippocampus membrane currents and in synaptic
plasticity (PubMed:8789948). {ECO:0000269|PubMed:1377365,
ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:26912815,
ECO:0000269|PubMed:8789948}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1377365,
PubMed:26912815). Can also form heterotetrameric channels that
contain at least one zeta subunit (GRIN1), at least one epsilon
subunit, plus GRIN3A or GRIN3B (PubMed:12008020, PubMed:14602821).
In vivo, the subunit composition may depend on the expression
levels of the different subunits (Probable). Found in a complex
with GRIN1, GRIN3A and PPP2CB (By similarity). Found in a complex
with GRIN1 and GRIN3B (PubMed:12008020, PubMed:14602821).
Interacts with MAGI3 (By similarity). Interacts with HIP1 and
NETO1 (PubMed:17329427, PubMed:19243221). Interacts with PDZ
domains of PATJ and DLG4. Interacts with DAPK1 (PubMed:20141836).
Found in a complex with GRIN1 and PRR7. Interacts with PRR7 (By
similarity). {ECO:0000250|UniProtKB:Q00960,
ECO:0000250|UniProtKB:Q13224, ECO:0000269|PubMed:12008020,
ECO:0000269|PubMed:1377365, ECO:0000269|PubMed:14602821,
ECO:0000269|PubMed:17329427, ECO:0000269|PubMed:19243221,
ECO:0000269|PubMed:20141836, ECO:0000269|PubMed:26912815}.
-!- INTERACTION:
Q9JI91:Actn2; NbExp=4; IntAct=EBI-400125, EBI-299169;
P17426:Ap2a1; NbExp=2; IntAct=EBI-400125, EBI-775189;
P11798:Camk2a; NbExp=7; IntAct=EBI-400125, EBI-400384;
Q80YE7:Dapk1; NbExp=8; IntAct=EBI-400125, EBI-2584874;
Q62108:Dlg4; NbExp=19; IntAct=EBI-400125, EBI-300895;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1377365,
ECO:0000269|PubMed:26912815}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q00960}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00960}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:Q00960}.
-!- TISSUE SPECIFICITY: Detected in brain (at protein level)
(PubMed:8789948). Detected throughout the brain, and in brain stem
trigeminal nucleus (PubMed:8789948). Detected in forebrain
(PubMed:1377365). {ECO:0000269|PubMed:1377365,
ECO:0000269|PubMed:8789948}.
-!- DOMAIN: A hydrophobic region that gives rise to the prediction of
a transmembrane span does not cross the membrane, but is part of a
discontinuously helical region that dips into the membrane and is
probably part of the pore and of the selectivity filter.
{ECO:0000250|UniProtKB:Q00960}.
-!- PTM: Phosphorylated on tyrosine residues (PubMed:12451687).
Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA
receptor channel activity (PubMed:20141836).
{ECO:0000269|PubMed:12451687, ECO:0000269|PubMed:20141836}.
-!- DISRUPTION PHENOTYPE: Mutant pups are born at the expected
Mendelian rate and appear grossly normal, but lack suckling
behavior. As a consequence, all die shortly after birth, except
when they are fed manually via a soft tube that delivers milk
directly into the stomach. While mutant neonate brain structures
are grossly normal, the mutant brain stem trigeminal complex lacks
the neural repeating units called barrelettes that correspond to
whisker-associated nerve fibers. Primary afferent nerve fibers
from whiskers fail to show normal clustering in the region where
barrelette structures form in wild-type. In contrast, nasolabial
motor neurons appear normal. Contrary to wild-type neonates, brain
slices from the mutant neonate hippocampus CA1 region lack NMDA
receptor-type ion channel activity. Contrary to wild-type pups,
prolonged low frequency stimulation of afferent fibers does not
induce long-term depression (LTD) in the hippocampus.
{ECO:0000269|PubMed:8789948}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2B/GRIN2B subfamily. {ECO:0000305}.
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EMBL; D10651; BAA01498.2; -; mRNA.
EMBL; AK002963; BAB22483.1; -; mRNA.
CCDS; CCDS20648.1; -.
PIR; I49704; I49704.
RefSeq; NP_032197.3; NM_008171.3.
UniGene; Mm.436649; -.
ProteinModelPortal; Q01097; -.
SMR; Q01097; -.
BioGrid; 200069; 75.
CORUM; Q01097; -.
DIP; DIP-31568N; -.
IntAct; Q01097; 190.
MINT; MINT-135847; -.
STRING; 10090.ENSMUSP00000062284; -.
ChEMBL; CHEMBL3442; -.
iPTMnet; Q01097; -.
PhosphoSitePlus; Q01097; -.
MaxQB; Q01097; -.
PaxDb; Q01097; -.
PRIDE; Q01097; -.
GeneID; 14812; -.
KEGG; mmu:14812; -.
CTD; 2904; -.
MGI; MGI:95821; Grin2b.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
HOGENOM; HOG000113802; -.
HOVERGEN; HBG052635; -.
InParanoid; Q01097; -.
KO; K05210; -.
PhylomeDB; Q01097; -.
PRO; PR:Q01097; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IPI:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098794; C:postsynapse; IDA:ParkinsonsUK-UCL.
GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0005262; F:calcium channel activity; IMP:MGI.
GO; GO:0005261; F:cation channel activity; IGI:MGI.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0016595; F:glutamate binding; ISS:UniProtKB.
GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
GO; GO:0016594; F:glycine binding; ISO:MGI.
GO; GO:0099529; F:neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
GO; GO:0004972; F:NMDA glutamate receptor activity; IMP:MGI.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0001662; P:behavioral fear response; IMP:MGI.
GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0006812; P:cation transport; IGI:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
GO; GO:0042596; P:fear response; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0007612; P:learning; IDA:MGI.
GO; GO:0007611; P:learning or memory; TAS:UniProtKB.
GO; GO:0060291; P:long-term synaptic potentiation; IGI:MGI.
GO; GO:0007613; P:memory; IDA:MGI.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IGI:ARUK-UCL.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:MGI.
GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; TAS:UniProtKB.
GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:MGI.
GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:MGI.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
GO; GO:0045471; P:response to ethanol; IMP:MGI.
GO; GO:0007423; P:sensory organ development; IMP:MGI.
GO; GO:0001964; P:startle response; IMP:MGI.
GO; GO:0001967; P:suckling behavior; IMP:MGI.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR018884; NMDAR2_C.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
Pfam; PF10565; NMDAR2_C; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
Calcium; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Magnesium; Membrane; Metal-binding;
Phosphoprotein; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport; Zinc.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 1482 Glutamate receptor ionotropic, NMDA 2B.
/FTId=PRO_0000011578.
TOPO_DOM 27 557 Extracellular.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 558 576 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 577 603 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
INTRAMEM 604 623 Discontinuously helical.
{ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 624 630 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 631 646 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 647 817 Extracellular.
{ECO:0000250|UniProtKB:Q00960}.
TRANSMEM 818 837 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 838 1482 Cytoplasmic.
{ECO:0000250|UniProtKB:Q00960}.
REGION 604 623 Pore-forming.
{ECO:0000250|UniProtKB:A7XY94}.
REGION 690 691 Glutamate binding.
{ECO:0000250|UniProtKB:Q00960}.
REGION 1292 1304 Interaction with DAPK1.
{ECO:0000269|PubMed:20141836}.
MOTIF 1480 1482 PDZ-binding. {ECO:0000250}.
COMPBIAS 984 989 Poly-His.
METAL 127 127 Zinc. {ECO:0000250|UniProtKB:Q00960}.
METAL 284 284 Zinc. {ECO:0000250|UniProtKB:Q00960}.
BINDING 514 514 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
BINDING 519 519 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
BINDING 732 732 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
SITE 615 615 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000250|UniProtKB:Q00960}.
MOD_RES 917 917 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 962 962 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1039 1039 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1058 1058 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1061 1061 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1109 1109 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1133 1133 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1143 1143 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1155 1155 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1255 1255 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1259 1259 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1303 1303 Phosphoserine; by DAPK1.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:20141836}.
MOD_RES 1472 1472 Phosphotyrosine.
{ECO:0000269|PubMed:12451687}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 688 688 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 86 321 {ECO:0000250|UniProtKB:Q00960}.
DISULFID 429 456 {ECO:0000250|UniProtKB:Q00960}.
DISULFID 436 457 {ECO:0000250|UniProtKB:Q00960}.
DISULFID 746 801 {ECO:0000250|UniProtKB:Q00960}.
CONFLICT 99 99 L -> F (in Ref. 3; BAB22483).
{ECO:0000305}.
SEQUENCE 1482 AA; 165959 MW; B8C3FA10E9A4B36D CRC64;
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SAPSIGIAVI LVGTSDEVAI KDAHEKDDFH
HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVLA DDTDQEAIAQ ILDFISAQTL
TPILGIHGGS SMIMADKDES SMFFQFGPSI EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ
DFVNKIRSTI ENSFVGWELE EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI
FEVANSVGLT GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII
TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS FSEDGYQMHP
KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE QEDDHLSIVT LEEAPFVIVE
SVDPLSGTCM RNTVPCQKRI ISENKTDEEP GYIKKCCKGF CIDILKKISK SVKFTYDLYL
VTNGKHGKKI NGTWNGMIGE VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR
SNGTVSPSAF LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL AAFMIQEEYV
DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA EMHAYMGKFN QRGVDDALLS
LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT IGSGKVFAST GYGIAIQKDS GWKRQVDLAI
LQLFGDGEME ELEALWLTGI CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH
LFYWQFRHCF MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN NPPCEENLFS
DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSTSSI DGLYDCDNPP FTTQPRSISK
KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS GHDDLIRSDV SDISTHTVTY GNIEGNAAKR
RKQQYKDSLK KRPASAKSRR EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK
ENSPHWEHVD LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGDKHGVV GGVPAPWEKN
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN LYDISEDNSL
QELDQPAAPV AVSSNASTTK YPQSPTNSKA QKKNRNKLRR QHSYDTFVDL QKEEAALAPR
SVSLKDKGRF MDGSPYAHMF EMPAGESSFA NKSSVTTAGH HHNNPGSGYM LSKSLYPDRV
TQNPFIPTFG DDQCLLHGSK SYFFRQPTVA GASKTRPDFR ALVTNKPVVS ALHGAVPGRF
QKDICIGNQS NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV


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