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Glutamate receptor ionotropic, NMDA 2D (GluN2D) (Glutamate [NMDA] receptor subunit epsilon-4) (N-methyl D-aspartate receptor subtype 2D) (NMDAR2D) (NR2D)

 NMDE4_MOUSE             Reviewed;        1323 AA.
Q03391; C9K0Z5;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 163.
RecName: Full=Glutamate receptor ionotropic, NMDA 2D;
Short=GluN2D;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-4 {ECO:0000303|PubMed:1385220, ECO:0000303|PubMed:8774946};
AltName: Full=N-methyl D-aspartate receptor subtype 2D;
Short=NMDAR2D;
Short=NR2D;
Flags: Precursor;
Name=Grin2d; Synonyms=GluN2D;
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].
STRAIN=ddY; TISSUE=Spinal cord;
Nishizwa M., Ito S.;
"Expression of mRNA in mouse spinal cord.";
Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
SUBUNIT.
TISSUE=Brain;
PubMed=1385220; DOI=10.1016/0014-5793(92)81178-O;
Ikeda K., Nagasawa M., Mori H., Araki K., Sakimura K., Watanabe M.,
Inoue Y., Mishina M.;
"Cloning and expression of the epsilon 4 subunit of the NMDA receptor
channel.";
FEBS Lett. 313:34-38(1992).
[3]
SEQUENCE REVISION.
Ikeda K., Nagasawa M., Mori H., Araki K., Sakimura K., Watanabe M.,
Inoue Y., Mishina M.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4]
DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8774946;
Ikeda K., Araki K., Takayama C., Inoue Y., Yagi T., Aizawa S.,
Mishina M.;
"Reduced spontaneous activity of mice defective in the epsilon 4
subunit of the NMDA receptor channel.";
Brain Res. Mol. Brain Res. 33:61-71(1995).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1313, 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).
[6]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1303, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- 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:1385220). Sensitivity to glutamate
and channel kinetics depend on the subunit composition (Probable).
{ECO:0000269|PubMed:1385220, ECO:0000305}.
-!- SUBUNIT: Heterotetramer. Forms heterotetrameric channels composed
of two zeta subunits (GRIN1), and two epsilon subunits (GRIN2A,
GRIN2B, GRIN2C or GRIN2D) (in vitro) (PubMed:1385220). In vivo,
the subunit composition may depend on the expression levels of the
different subunits (Probable). Interacts with PDZ domains of PATJ
and DLG4 (By similarity). {ECO:0000250|UniProtKB:Q62645,
ECO:0000269|PubMed:1385220, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1385220};
Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000305|PubMed:8774946}; Multi-
pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in neonate brain synaptosomes (at
protein level). {ECO:0000269|PubMed:8774946}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
rate, are viable and fertile. Their brains appear grossly normal.
Mutant mice show reduced spontaneous locomotion activity, but have
no visible impairment of motor skills. They have normal
exploratory behavior, but their behavior in a new situation
suggests increased novelty preference.
{ECO:0000269|PubMed:8774946}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2D/GRIN2D subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB154245; BAI44630.1; -; mRNA.
EMBL; D12822; BAA02254.1; -; mRNA.
CCDS; CCDS21267.1; -.
PIR; S27224; S27224.
RefSeq; NP_032198.2; NM_008172.2.
RefSeq; XP_011249107.1; XM_011250805.2.
UniGene; Mm.322594; -.
ProteinModelPortal; Q03391; -.
BioGrid; 200071; 4.
IntAct; Q03391; 2.
MINT; MINT-4103932; -.
STRING; 10090.ENSMUSP00000002848; -.
ChEMBL; CHEMBL3832634; -.
iPTMnet; Q03391; -.
PhosphoSitePlus; Q03391; -.
PaxDb; Q03391; -.
PeptideAtlas; Q03391; -.
PRIDE; Q03391; -.
Ensembl; ENSMUST00000002848; ENSMUSP00000002848; ENSMUSG00000002771.
Ensembl; ENSMUST00000211713; ENSMUSP00000147663; ENSMUSG00000002771.
GeneID; 14814; -.
KEGG; mmu:14814; -.
UCSC; uc009gxm.1; mouse.
CTD; 2906; -.
MGI; MGI:95823; Grin2d.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00760000119186; -.
HOGENOM; HOG000113803; -.
HOVERGEN; HBG052637; -.
InParanoid; Q03391; -.
KO; K05212; -.
OMA; WDYLPPR; -.
OrthoDB; EOG091G09KH; -.
TreeFam; TF314731; -.
Reactome; R-MMU-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-MMU-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-MMU-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
PRO; PR:Q03391; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000002771; -.
ExpressionAtlas; Q03391; baseline and differential.
Genevisible; Q03391; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0022849; F:glutamate-gated calcium ion channel activity; ISS:UniProtKB.
GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:MGI.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:MGI.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0097553; P:calcium ion transmembrane import into cytosol; ISS:UniProtKB.
GO; GO:0051930; P:regulation of sensory perception of pain; IMP:MGI.
GO; GO:0001964; P:startle response; IMP:MGI.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 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; Methylation;
Phosphoprotein; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 1323 Glutamate receptor ionotropic, NMDA 2D.
/FTId=PRO_0000011584.
TOPO_DOM 28 581 Extracellular. {ECO:0000305}.
TRANSMEM 582 600 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 601 627 Cytoplasmic. {ECO:0000305}.
INTRAMEM 628 647 Discontinuously helical.
{ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 648 654 Cytoplasmic. {ECO:0000305}.
TRANSMEM 655 670 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 671 841 Extracellular. {ECO:0000305}.
TRANSMEM 842 861 Helical. {ECO:0000250|UniProtKB:Q00960}.
TOPO_DOM 862 1323 Cytoplasmic. {ECO:0000305}.
REGION 536 538 Glutamate binding.
{ECO:0000250|UniProtKB:Q00959}.
REGION 628 647 Pore-forming.
{ECO:0000250|UniProtKB:Q00960}.
REGION 714 715 Glutamate binding.
{ECO:0000250|UniProtKB:Q00959}.
MOTIF 1321 1323 PDZ-binding. {ECO:0000250}.
COMPBIAS 278 283 Poly-Gly.
COMPBIAS 905 913 Poly-Pro.
COMPBIAS 1030 1035 Poly-Ala.
COMPBIAS 1197 1201 Poly-Pro.
BINDING 538 538 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
BINDING 543 543 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
BINDING 756 756 Glutamate.
{ECO:0000250|UniProtKB:Q00960}.
SITE 639 639 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 1303 1303 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1313 1313 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 349 349 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 566 566 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 101 345 {ECO:0000250|UniProtKB:Q00959}.
DISULFID 452 480 {ECO:0000250|UniProtKB:Q00959}.
DISULFID 459 481 {ECO:0000250|UniProtKB:Q00959}.
DISULFID 770 825 {ECO:0000250|UniProtKB:Q00959}.
CONFLICT 1087 1087 A -> T (in Ref. 2; BAA02254).
{ECO:0000305}.
CONFLICT 1208 1209 PR -> AP (in Ref. 2; BAA02254).
{ECO:0000305}.
SEQUENCE 1323 AA; 142963 MW; 3DF8860D19677586 CRC64;
MRGAGGPRGP RGPAKMLLLL ALACASPFPE EVPGPGAAGG GTGGARPLNV ALVFSGPAYA
AEAARLGPAV AAAVRSPGLD VRPVALVLNG SDPRSLVLQL CDLLSGLRVH GVVFEDDSRA
PAVAPILDFL SAQTSLPIVA VHGGAALVLT PKEKGSTFLQ LGSSTEQQLQ VIFEVLEEYD
WTSFVAVTTR APGHRAFLSY IEVLTDGSLV GWEHRGALTL DPGAGEAVLG AQLRSVSAQI
RLLFCAREEA EPVFRAAEEA GLTGPGYVWF MVGPQLAGGG GSGVPGEPLL LPGGAPLPAG
LFAVRSAGWR DDLARRVAAG VAVVARGAQA LLRDYGFLPE LGHDCRAQNR THRGESLHRY
FMNITWDNRD YSFNEDGFLV NPSLVVISLT RDRTWEVVGS WEQQTLRLKY PLWSRYGRFL
QPVDDTQHLT VATLEERPFV IVEPADPISG TCIRDSVPCR SQLNRTHSPP PDAPRPEKRC
CKGFCIDILK RLAHTIGFSY DLYLVTNGKH GKKIDGVWNG MIGEVFYQRA DMAIGSLTIN
EERSEIVDFS VPFVETGISV MVARSNGTVS PSAFLEPYSP AVWVMMFVMC LTVVAVTVFI
FEYLSPVGYN RSLATGKRPG GSTFTIGKSI WLLWALVFNN SVPVENPRGT TSKIMVLVWA
FFAVIFLASY TANLAAFMIQ EEYVDTVSGL SDRKFQRPQE QYPPLKFGTV PNGSTEKNIR
SNYPDMHSYM VRYNQPRVEE ALTQLKAGKL DAFIYDAAVL NYMARKDEGC KLVTIGSGKV
FATTGYGIAL HKGSRWKRPI DLALLQFLGD DEIEMLERLW LSGICHNDKI EVMSSKLDID
NMAGVFYMLL VAMGLSLLVF AWEHLVYWRL RHCLGPTHRM DFLLAFSRGM YSCCSAEAAP
PPAKPPPPPQ PLPSPAYPAA RPPPGPAPFV PRERAAADRW RRAKGTGPPG GAALADGFHR
YYGPIEPQGL GLGEARAAPR GAAGRPLSPP TTQPPQKPPP SYFAIVREQE PAEPPAGAFP
GFPSPPAPPA AAAAAVGPPL CRLAFEDESP PAPSRWPRSD PESQPLLGGG AGGPSAGAPT
APPPRRAAPP PCAYLDLEPS PSDSEDSESL GGASLGGLEP WWFADFPYPY AERLGPPPGR
YWSVDKLGGW RAGSWDYLPP RGGPAWHCRH CASLELLPPP RHLSCSHDGL DGGWWAPPPP
PWAAGPPPRR RARCGCPRPH PHRPRASHRA PAAAPHHHRH RRAAGGWDLP PPAPTSRSLE
DLSSCPRAAP TRRLTGPSRH ARRCPHAAHW GPPLPTASHR RHRGGDLGTR RGSAHFSSLE
SEV


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