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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_RAT               Reviewed;        1482 AA.
Q00960; Q62684;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 168.
RecName: Full=Glutamate receptor ionotropic, NMDA 2B;
Short=GluN2B;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-2;
AltName: Full=N-methyl D-aspartate receptor subtype 2B;
Short=NMDAR2B;
Short=NR2B {ECO:0000303|PubMed:1350383};
Flags: Precursor;
Name=Grin2b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
SUBUNIT.
TISSUE=Brain;
PubMed=1350383; DOI=10.1126/science.256.5060.1217;
Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H.,
Burnashev N., Sakmann B., Seeburg P.H.;
"Heteromeric NMDA receptors: molecular and functional distinction of
subtypes.";
Science 256:1217-1221(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7524561; DOI=10.1016/0896-6273(94)90258-5;
Sullivan J.M., Traynelis S.F., Chen H.S., Escobar W., Heinemann S.F.,
Lipton S.A.;
"Identification of two cysteine residues that are required for redox
modulation of the NMDA subtype of glutamate receptor.";
Neuron 13:929-936(1994).
[3]
PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=7513428;
Moon I.S., Apperson M.L., Kennedy M.B.;
"The major tyrosine-phosphorylated protein in the postsynaptic density
fraction is N-methyl-D-aspartate receptor subunit 2B.";
Proc. Natl. Acad. Sci. U.S.A. 91:3954-3958(1994).
[4]
INTERACTION WITH DLG4.
PubMed=7569905; DOI=10.1126/science.7569905;
Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.;
"Domain interaction between NMDA receptor subunits and the
postsynaptic density protein PSD-95.";
Science 269:1737-1740(1995).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9509416;
Jin D.H., Jung Y.W., Ko B.H., Moon I.S.;
"Immunoblot analyses on the differential distribution of NR2A and NR2B
subunits in the adult rat brain.";
Mol. Cells 7:749-754(1997).
[6]
INTERACTION WITH PATJ.
PubMed=9647694; DOI=10.1006/mcne.1998.0679;
Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
"CIPP, a novel multivalent PDZ domain protein, selectively interacts
with Kir4.0 family members, NMDA receptor subunits, neurexins, and
neuroligins.";
Mol. Cell. Neurosci. 11:161-172(1998).
[7]
IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN3A AND PPP2CB.
PubMed=11588171;
Chan S.F., Sucher N.J.;
"An NMDA receptor signaling complex with protein phosphatase 2A.";
J. Neurosci. 21:7985-7992(2001).
[8]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
PubMed=11160393;
Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A.,
Trimmer J.S., Sucher N.J., Heinemann S.F.;
"Assembly with the NR1 subunit is required for surface expression of
NR3A-containing NMDA receptors.";
J. Neurosci. 21:1228-1237(2001).
[9]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
PubMed=12391275; DOI=10.1124/mol.62.5.1119;
Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B.,
Yasuda R.P.;
"Association of NR3A with the N-methyl-D-aspartate receptor NR1 and
NR2 subunits.";
Mol. Pharmacol. 62:1119-1127(2002).
[10]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
PubMed=11929923; DOI=10.1152/jn.00531.2001;
Sasaki Y.F., Rothe T., Premkumar L.S., Das S., Cui J., Talantova M.V.,
Wong H.-K., Gong X., Chan S.F., Zhang D., Nakanishi N., Sucher N.J.,
Lipton S.A.;
"Characterization and comparison of the NR3A subunit of the NMDA
receptor in recombinant systems and primary cortical neurons.";
J. Neurophysiol. 87:2052-2063(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-886; SER-917;
SER-920; TYR-1039; SER-1255; SER-1259 AND SER-1303, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[12]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND PRR7, AND INTERACTION WITH
PRR7.
PubMed=27458189; DOI=10.15252/embj.201593070;
Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
"Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and
regulates NMDA-mediated excitotoxicity.";
EMBO J. 35:1923-1934(2016).
[13] {ECO:0000244|PDB:3JPW, ECO:0000244|PDB:3JPY}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 32-394, FUNCTION,
SUBCELLULAR LOCATION, SUBUNIT, ENZYME REGULATION, GLYCOSYLATION AT
ASN-74 AND ASN-341, MUTAGENESIS OF HIS-60; HIS-127; ASP-283; GLU-284;
HIS-311 AND HIS-359, AND DISULFIDE BOND.
PubMed=19910922; DOI=10.1038/emboj.2009.338;
Karakas E., Simorowski N., Furukawa H.;
"Structure of the zinc-bound amino-terminal domain of the NMDA
receptor NR2B subunit.";
EMBO J. 28:3910-3920(2009).
[14] {ECO:0000244|PDB:3QEL, ECO:0000244|PDB:3QEM}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 31-394, FUNCTION,
SUBCELLULAR LOCATION, SUBUNIT, ENZYME REGULATION, GLYCOSYLATION AT
ASN-74 AND ASN-341, AND DISULFIDE BONDS.
PubMed=21677647; DOI=10.1038/nature10180;
Karakas E., Simorowski N., Furukawa H.;
"Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B
NMDA receptors.";
Nature 475:249-253(2011).
[15] {ECO:0000244|PDB:4PE5}
X-RAY CRYSTALLOGRAPHY (3.96 ANGSTROMS) OF 27-852 IN COMPLEX WITH GRIN1
AND GLUTAMATE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT,
GLYCOSYLATION AT ASN-74; ASN-341 AND ASN-688, AND DISULFIDE BONDS.
PubMed=24876489; DOI=10.1126/science.1251915;
Karakas E., Furukawa H.;
"Crystal structure of a heterotetrameric NMDA receptor ion channel.";
Science 344:992-997(2014).
[16] {ECO:0000244|PDB:5B3J, ECO:0000244|PDB:5FXG, ECO:0000244|PDB:5FXH, ECO:0000244|PDB:5FXI, ECO:0000244|PDB:5FXJ, ECO:0000244|PDB:5FXK}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 31-394, STRUCTURE BY
ELECTRON MICROSCOPY (6.1 ANGSTROMS) OF 27-852 IN COMPLEX WITH GRIN1,
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, AND DISULFIDE
BONDS.
PubMed=27135925; DOI=10.1038/nature17679;
Tajima N., Karakas E., Grant T., Simorowski N., Diaz-Avalos R.,
Grigorieff N., Furukawa H.;
"Activation of NMDA receptors and the mechanism of inhibition by
ifenprodil.";
Nature 534:63-68(2016).
[17] {ECO:0000244|PDB:5TPZ}
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 32-393 IN COMPLEX WITH
GRIN1, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT
ASN-341, AND DISULFIDE BONDS.
PubMed=27916457; DOI=10.1016/j.neuron.2016.11.006;
Romero-Hernandez A., Simorowski N., Karakas E., Furukawa H.;
"Molecular Basis for Subtype Specificity and High-Affinity Zinc
Inhibition in the GluN1-GluN2A NMDA Receptor Amino-Terminal Domain.";
Neuron 92:1324-1336(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:1350383, PubMed:19910922,
PubMed:21677647, PubMed:24876489, PubMed:27135925,
PubMed:27916457). Sensitivity to glutamate and channel kinetics
depend on the subunit composition (Probable). 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.
Contributes to neural pattern formation in the developing brain.
Plays a role in long-term depression (LTD) of hippocampus membrane
currents and in synaptic plasticity (By similarity).
{ECO:0000250|UniProtKB:Q01097, ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647,
ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
ECO:0000269|PubMed:27916457, ECO:0000305}.
-!- ENZYME REGULATION: Channel activity is inhibited by micromolar
levels of zinc ions (PubMed:19910922). Channel activity is
inhibited by ifenprodil (PubMed:19910922, PubMed:21677647).
{ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1350383,
PubMed:19910922, PubMed:21677647, PubMed:24876489,
PubMed:27135925, PubMed:27916457). Can also form heterotetrameric
channels that contain at least one zeta subunit (GRIN1), at least
one epsilon subunit, plus GRIN3A or GRIN3B. In vivo, the subunit
composition may depend on the expression levels of the different
subunits. Found in a complex with GRIN1, GRIN3A and PPP2CB. Found
in a complex with GRIN1 and GRIN3B. Interacts with MAGI3.
Interacts with HIP1 and NETO1. Interacts with PDZ domains of PATJ
and DLG4. Interacts with DAPK1 (By similarity). Found in a complex
with GRIN1 and PRR7 (PubMed:27458189). Interacts with PRR7
(PubMed:27458189). {ECO:0000250|UniProtKB:Q01097,
ECO:0000250|UniProtKB:Q13224, ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647,
ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
ECO:0000269|PubMed:27458189, ECO:0000269|PubMed:27916457}.
-!- INTERACTION:
P11275:Camk2a; NbExp=2; IntAct=EBI-396905, EBI-2640645;
P11798:Camk2a (xeno); NbExp=3; IntAct=EBI-396905, EBI-400384;
Q62936:Dlg3; NbExp=6; IntAct=EBI-396905, EBI-349596;
P31016:Dlg4; NbExp=8; IntAct=EBI-396905, EBI-375655;
P35439:Grin1; NbExp=12; IntAct=EBI-396905, EBI-877897;
P35439-7:Grin1; NbExp=2; IntAct=EBI-396905, EBI-15932497;
Q91977:grin1 (xeno); NbExp=6; IntAct=EBI-396905, EBI-15932423;
Q460M5:Lrfn2; NbExp=2; IntAct=EBI-396905, EBI-877185;
Q8R4I7:Neto1 (xeno); NbExp=2; IntAct=EBI-396905, EBI-2314926;
Q63ZW7:Patj (xeno); NbExp=4; IntAct=EBI-396905, EBI-8366894;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1350383,
ECO:0000269|PubMed:19910922, ECO:0000269|PubMed:21677647,
ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925,
ECO:0000269|PubMed:27916457}; Multi-pass membrane protein
{ECO:0000269|PubMed:24876489, ECO:0000269|PubMed:27135925}. Cell
junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:7513428, ECO:0000269|PubMed:9509416}; Multi-
pass membrane protein {ECO:0000269|PubMed:24876489,
ECO:0000269|PubMed:27135925}.
-!- TISSUE SPECIFICITY: Detected in adult olfactory bulb, brain
cortex, hippocampus, striatum, thalamus, superior colliculus, with
much lower levels in inferior colliculus, midbrain and cerebellum.
{ECO:0000269|PubMed:9509416}.
-!- 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:0000305|PubMed:24876489}.
-!- PTM: Phosphorylated on tyrosine residues (PubMed:7513428).
Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA
receptor channel activity (By similarity).
{ECO:0000250|UniProtKB:Q01097, ECO:0000269|PubMed:7513428}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2B/GRIN2B subfamily. {ECO:0000305}.
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EMBL; M91562; AAA41714.1; -; mRNA.
EMBL; U11419; AAA50554.1; -; mRNA.
PIR; B43274; B43274.
RefSeq; NP_036706.1; NM_012574.1.
UniGene; Rn.9711; -.
PDB; 3JPW; X-ray; 2.80 A; A=32-394.
PDB; 3JPY; X-ray; 3.21 A; A=32-394.
PDB; 3QEL; X-ray; 2.60 A; B/D=31-394.
PDB; 3QEM; X-ray; 3.00 A; B/D=31-394.
PDB; 4PE5; X-ray; 3.96 A; B/D=27-852.
PDB; 5B3J; X-ray; 2.90 A; C/D=31-394.
PDB; 5FXG; EM; 6.80 A; B/D=27-852.
PDB; 5FXH; EM; 6.10 A; B/D=27-852.
PDB; 5FXI; EM; 6.40 A; B/D=27-852.
PDB; 5FXJ; EM; 6.50 A; B/D=27-852.
PDB; 5FXK; EM; 6.40 A; B/D=27-852.
PDB; 5TPZ; X-ray; 3.10 A; D=32-393.
PDBsum; 3JPW; -.
PDBsum; 3JPY; -.
PDBsum; 3QEL; -.
PDBsum; 3QEM; -.
PDBsum; 4PE5; -.
PDBsum; 5B3J; -.
PDBsum; 5FXG; -.
PDBsum; 5FXH; -.
PDBsum; 5FXI; -.
PDBsum; 5FXJ; -.
PDBsum; 5FXK; -.
PDBsum; 5TPZ; -.
ProteinModelPortal; Q00960; -.
SMR; Q00960; -.
BioGrid; 246575; 12.
CORUM; Q00960; -.
DIP; DIP-33702N; -.
IntAct; Q00960; 18.
MINT; MINT-104014; -.
STRING; 10116.ENSRNOP00000011697; -.
BindingDB; Q00960; -.
ChEMBL; CHEMBL311; -.
GuidetoPHARMACOLOGY; 457; -.
TCDB; 1.A.10.1.6; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
iPTMnet; Q00960; -.
PhosphoSitePlus; Q00960; -.
SwissPalm; Q00960; -.
UniCarbKB; Q00960; -.
PaxDb; Q00960; -.
PRIDE; Q00960; -.
GeneID; 24410; -.
KEGG; rno:24410; -.
UCSC; RGD:2738; rat.
CTD; 2904; -.
RGD; 2738; Grin2b.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
HOGENOM; HOG000113802; -.
HOVERGEN; HBG052635; -.
InParanoid; Q00960; -.
KO; K05210; -.
PhylomeDB; Q00960; -.
EvolutionaryTrace; Q00960; -.
PRO; PR:Q00960; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0097440; C:apical dendrite; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098794; C:postsynapse; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0043083; C:synaptic cleft; IDA:RGD.
GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0030018; C:Z disc; IDA:RGD.
GO; GO:0008013; F:beta-catenin binding; IPI:RGD.
GO; GO:0005262; F:calcium channel activity; ISO:RGD.
GO; GO:0005261; F:cation channel activity; ISO:RGD.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
GO; GO:0031749; F:D2 dopamine receptor binding; IPI:RGD.
GO; GO:0008144; F:drug binding; IPI:RGD.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IDA:RGD.
GO; GO:0016595; F:glutamate binding; IDA:UniProtKB.
GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
GO; GO:0016594; F:glycine binding; ISO:RGD.
GO; GO:0005149; F:interleukin-1 receptor binding; IPI:RGD.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0042165; F:neurotransmitter binding; IDA:RGD.
GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
GO; GO:0099529; F:neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0001508; P:action potential; IMP:RGD.
GO; GO:0008306; P:associative learning; IMP:RGD.
GO; GO:0001662; P:behavioral fear response; IMP:RGD.
GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
GO; GO:0006816; P:calcium ion transport; ISO:RGD.
GO; GO:0006812; P:cation transport; ISO:RGD.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD.
GO; GO:0071386; P:cellular response to corticosterone stimulus; IEP:RGD.
GO; GO:1904644; P:cellular response to curcumin; IEP:RGD.
GO; GO:0071359; P:cellular response to dsRNA; IEP:RGD.
GO; GO:1904322; P:cellular response to forskolin; IEP:RGD.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0071396; P:cellular response to lipid; IEP:RGD.
GO; GO:0010350; P:cellular response to magnesium starvation; IEP:RGD.
GO; GO:0071287; P:cellular response to manganese ion; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:RGD.
GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
GO; GO:0042596; P:fear response; ISO:RGD.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
GO; GO:0007612; P:learning; ISO:RGD.
GO; GO:0007611; P:learning or memory; TAS:RGD.
GO; GO:0007616; P:long-term memory; IEP:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
GO; GO:0007613; P:memory; IDA:UniProtKB.
GO; GO:0033555; P:multicellular organismal response to stress; IEP:RGD.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; ISO:RGD.
GO; GO:0098989; P:NMDA selective glutamate receptor signaling pathway; IMP:SynGO.
GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
GO; GO:0014049; P:positive regulation of glutamate secretion; IDA:UniProtKB.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:RGD.
GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
GO; GO:0043113; P:receptor clustering; IDA:RGD.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD.
GO; GO:0043408; P:regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:RGD.
GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
GO; GO:0014075; P:response to amine; IEP:RGD.
GO; GO:0001975; P:response to amphetamine; IEP:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0060992; P:response to fungicide; IEP:RGD.
GO; GO:0060416; P:response to growth hormone; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
GO; GO:0010042; P:response to manganese ion; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0051597; P:response to methylmercury; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IMP:RGD.
GO; GO:0051707; P:response to other organism; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0048511; P:rhythmic process; IDA:RGD.
GO; GO:0046960; P:sensitization; IMP:RGD.
GO; GO:0007423; P:sensory organ development; ISO:RGD.
GO; GO:0001964; P:startle response; ISO:RGD.
GO; GO:0001967; P:suckling behavior; ISO:RGD.
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;
3D-structure; Calcium; Cell junction; Cell membrane;
Complete proteome; Direct protein sequencing; 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.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 1482 Glutamate receptor ionotropic, NMDA 2B.
/FTId=PRO_0000011579.
TOPO_DOM 27 557 Extracellular.
{ECO:0000269|PubMed:24876489}.
TRANSMEM 558 576 Helical. {ECO:0000269|PubMed:24876489}.
TOPO_DOM 577 603 Cytoplasmic.
{ECO:0000269|PubMed:24876489}.
INTRAMEM 604 623 Discontinuously helical.
{ECO:0000305|PubMed:24876489}.
TOPO_DOM 624 630 Cytoplasmic.
{ECO:0000269|PubMed:24876489}.
TRANSMEM 631 646 Helical. {ECO:0000269|PubMed:24876489}.
TOPO_DOM 647 817 Extracellular.
{ECO:0000269|PubMed:24876489}.
TRANSMEM 818 837 Helical. {ECO:0000269|PubMed:24876489}.
TOPO_DOM 838 1482 Cytoplasmic.
{ECO:0000269|PubMed:24876489}.
REGION 604 623 Pore-forming.
{ECO:0000269|PubMed:24876489,
ECO:0000305|PubMed:24876489}.
REGION 690 691 Glutamate binding.
{ECO:0000244|PDB:4PE5}.
REGION 1292 1304 Interaction with DAPK1.
{ECO:0000250|UniProtKB:Q01097}.
MOTIF 1480 1482 PDZ-binding.
COMPBIAS 984 989 Poly-His.
METAL 127 127 Zinc. {ECO:0000244|PDB:3JPY,
ECO:0000305|PubMed:19910922}.
METAL 284 284 Zinc. {ECO:0000244|PDB:3JPY,
ECO:0000305|PubMed:19910922}.
BINDING 514 514 Glutamate. {ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
BINDING 519 519 Glutamate. {ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
BINDING 732 732 Glutamate. {ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
SITE 615 615 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 917 917 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 962 962 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1039 1039 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1058 1058 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1061 1061 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1109 1109 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1133 1133 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1143 1143 Phosphoserine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1155 1155 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1255 1255 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1259 1259 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1303 1303 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1303 1303 Phosphoserine; by DAPK1.
{ECO:0000250|UniProtKB:Q01097}.
MOD_RES 1472 1472 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01097}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JPW,
ECO:0000244|PDB:3JPY,
ECO:0000244|PDB:3QEL,
ECO:0000244|PDB:3QEM,
ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:19910922,
ECO:0000269|PubMed:24876489}.
CARBOHYD 341 341 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JPW,
ECO:0000244|PDB:3JPY,
ECO:0000244|PDB:3QEL,
ECO:0000244|PDB:3QEM,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5TPZ,
ECO:0000269|PubMed:19910922,
ECO:0000269|PubMed:24876489}.
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:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
DISULFID 86 321 {ECO:0000244|PDB:3JPW,
ECO:0000244|PDB:3JPY,
ECO:0000244|PDB:3QEL,
ECO:0000244|PDB:3QEM,
ECO:0000244|PDB:4PE5,
ECO:0000244|PDB:5B3J,
ECO:0000244|PDB:5TPZ,
ECO:0000269|PubMed:19910922}.
DISULFID 429 456 {ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
DISULFID 436 457 {ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
DISULFID 746 801 {ECO:0000244|PDB:4PE5,
ECO:0000269|PubMed:24876489}.
MUTAGEN 60 60 H->A: Normal zinc binding.
{ECO:0000269|PubMed:19910922}.
MUTAGEN 127 127 H->A: Reduced zinc binding.
{ECO:0000269|PubMed:19910922}.
MUTAGEN 283 283 D->A: Slightly reduced zinc binding.
{ECO:0000269|PubMed:19910922}.
MUTAGEN 284 284 E->A: Reduced zinc binding.
{ECO:0000269|PubMed:19910922}.
MUTAGEN 311 311 H->A: Normal zinc binding.
{ECO:0000269|PubMed:19910922}.
MUTAGEN 359 359 H->A: Normal zinc binding.
{ECO:0000269|PubMed:19910922}.
CONFLICT 1256 1256 E -> K (in Ref. 2; AAA50554).
{ECO:0000305}.
CONFLICT 1430 1431 VT -> SA (in Ref. 2; AAA50554).
{ECO:0000305}.
STRAND 34 44 {ECO:0000244|PDB:3QEL}.
HELIX 47 50 {ECO:0000244|PDB:3QEL}.
HELIX 53 55 {ECO:0000244|PDB:3JPW}.
STRAND 64 73 {ECO:0000244|PDB:3QEL}.
HELIX 78 91 {ECO:0000244|PDB:3QEL}.
STRAND 94 103 {ECO:0000244|PDB:3QEL}.
HELIX 107 119 {ECO:0000244|PDB:3QEL}.
STRAND 123 127 {ECO:0000244|PDB:3QEL}.
HELIX 128 131 {ECO:0000244|PDB:3QEL}.
STRAND 143 147 {ECO:0000244|PDB:3QEL}.
HELIX 150 163 {ECO:0000244|PDB:3QEL}.
STRAND 168 175 {ECO:0000244|PDB:3QEL}.
HELIX 179 191 {ECO:0000244|PDB:3QEL}.
STRAND 198 205 {ECO:0000244|PDB:3QEL}.
STRAND 211 213 {ECO:0000244|PDB:3QEL}.
HELIX 215 220 {ECO:0000244|PDB:3QEL}.
STRAND 226 232 {ECO:0000244|PDB:3QEL}.
HELIX 234 245 {ECO:0000244|PDB:3QEL}.
TURN 246 248 {ECO:0000244|PDB:3QEL}.
STRAND 251 253 {ECO:0000244|PDB:5B3J}.
STRAND 255 258 {ECO:0000244|PDB:3QEL}.
HELIX 260 263 {ECO:0000244|PDB:3QEL}.
STRAND 265 267 {ECO:0000244|PDB:5TPZ}.
STRAND 271 273 {ECO:0000244|PDB:5TPZ}.
STRAND 275 281 {ECO:0000244|PDB:3JPW}.
TURN 284 286 {ECO:0000244|PDB:3QEL}.
HELIX 289 308 {ECO:0000244|PDB:3QEL}.
TURN 309 311 {ECO:0000244|PDB:3QEL}.
TURN 322 326 {ECO:0000244|PDB:3QEL}.
HELIX 327 330 {ECO:0000244|PDB:3QEL}.
HELIX 336 339 {ECO:0000244|PDB:3QEL}.
STRAND 345 348 {ECO:0000244|PDB:5TPZ}.
STRAND 355 359 {ECO:0000244|PDB:3QEL}.
STRAND 362 367 {ECO:0000244|PDB:3QEL}.
STRAND 369 371 {ECO:0000244|PDB:3JPY}.
STRAND 373 379 {ECO:0000244|PDB:3QEL}.
STRAND 384 387 {ECO:0000244|PDB:3QEL}.
SEQUENCE 1482 AA; 166071 MW; AEF8B9DF3C1B0D5D CRC64;
MKPSAECCSP KFWLVLAVLA VSGSKARSQK SPPSIGIAVI LVGTSDEVAI KDAHEKDDFH
HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVFA 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 HGTGEKHGVV GGVPAPWEKN
LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN LYDISEDNSL
QELDQPAAPV AVTSNASSTK YPQSPTNSKA QKKNRNKLRR QHSYDTFVDL QKEEAALAPR
SVSLKDKGRF MDGSPYAHMF EMPAGESSFA NKSSVPTAGH HHNNPGSGYM LSKSLYPDRV
TQNPFIPTFG DDQCLLHGSK SYFFRQPTVA GASKTRPDFR ALVTNKPVVV TLHGAVPGRF
QKDICIGNQS NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV


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