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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_RAT               Reviewed;        1323 AA.
Q62645; Q63381; Q63382; Q63729; Q63730;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
29-AUG-2001, sequence version 2.
30-AUG-2017, entry version 157.
RecName: Full=Glutamate receptor ionotropic, NMDA 2D;
Short=GluN2D;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-4;
AltName: Full=N-methyl D-aspartate receptor subtype 2D;
Short=NMDAR2D;
Short=NR2D;
Flags: Precursor;
Name=Grin2d; Synonyms=GluN2D;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE OF
1265-1356 (ISOFORM 2).
STRAIN=Sprague-Dawley; TISSUE=Forebrain;
PubMed=8428958;
Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H.,
Yokoi M., Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.;
"Molecular characterization of the family of the N-methyl-D-aspartate
receptor subunits.";
J. Biol. Chem. 268:2836-2843(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=7512349; DOI=10.1016/0896-6273(94)90210-0;
Monyer H., Burnashev N., Laurie D.J., Sakmann B., Seeburg P.H.;
"Developmental and regional expression in the rat brain and functional
properties of four NMDA receptors.";
Neuron 12:529-540(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Sprague-Dawley; TISSUE=Brain;
Boulter J., Pecht G.;
Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
[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]
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).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 424-827, AND DISULFIDE BONDS.
PubMed=21522138; DOI=10.1038/ncomms1295;
Vance K.M., Simorowski N., Traynelis S.F., Furukawa H.;
"Ligand-specific deactivation time course of GluN1/GluN2D NMDA
receptors.";
Nat. Commun. 2:294-294(2011).
-!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
with high calcium permeability and voltage-dependent sensitivity
to magnesium. Mediated by glycine.
-!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a
epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
subunit (GRIN3A or GRIN3B). Interacts with PDZ domains of PATJ and
DLG4. {ECO:0000269|PubMed:7569905, ECO:0000269|PubMed:9647694}.
-!- INTERACTION:
Q63ZW7:Patj (xeno); NbExp=3; IntAct=EBI-631067, EBI-8366894;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cell junction, synapse, postsynaptic cell membrane; Multi-pass
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=Q62645-1; Sequence=Displayed;
Name=1;
IsoId=Q62645-2; Sequence=VSP_000136;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in brain, mainly in the subcortical
region.
-!- DEVELOPMENTAL STAGE: Already detected in embryonic stages, peaks
at postnatal day 7, and decreases thereafter to adult levels.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2D/GRIN2D subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D13213; BAA02500.1; -; mRNA.
EMBL; D13214; BAA02501.1; -; mRNA.
EMBL; L31611; AAC37646.1; -; mRNA.
EMBL; L31612; AAC37647.1; -; mRNA.
EMBL; U08260; AAA17833.1; -; mRNA.
PIR; I78557; I78557.
RefSeq; NP_073634.1; NM_022797.1.
RefSeq; XP_008757539.1; XM_008759317.2. [Q62645-2]
UniGene; Rn.91209; -.
PDB; 3OEK; X-ray; 1.90 A; A=424-564, A=686-827.
PDB; 3OEL; X-ray; 1.90 A; A=424-564, A=686-827.
PDB; 3OEM; X-ray; 1.90 A; A=424-564, A=686-827.
PDB; 3OEN; X-ray; 1.80 A; A=424-564, A=686-827.
PDB; 4JWY; X-ray; 2.00 A; A=424-564, A=686-827.
PDBsum; 3OEK; -.
PDBsum; 3OEL; -.
PDBsum; 3OEM; -.
PDBsum; 3OEN; -.
PDBsum; 4JWY; -.
ProteinModelPortal; Q62645; -.
SMR; Q62645; -.
BioGrid; 246577; 3.
IntAct; Q62645; 4.
MINT; MINT-103662; -.
STRING; 10116.ENSRNOP00000028615; -.
BindingDB; Q62645; -.
ChEMBL; CHEMBL303; -.
GuidetoPHARMACOLOGY; 459; -.
iPTMnet; Q62645; -.
PhosphoSitePlus; Q62645; -.
PaxDb; Q62645; -.
PRIDE; Q62645; -.
Ensembl; ENSRNOT00000028615; ENSRNOP00000028615; ENSRNOG00000021063. [Q62645-1]
GeneID; 24412; -.
KEGG; rno:24412; -.
UCSC; RGD:2740; rat. [Q62645-1]
CTD; 2906; -.
RGD; 2740; Grin2d.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00760000119186; -.
HOGENOM; HOG000113803; -.
HOVERGEN; HBG052637; -.
InParanoid; Q62645; -.
KO; K05212; -.
PhylomeDB; Q62645; -.
Reactome; R-RNO-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-RNO-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-RNO-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-8849932; SALM protein interactions at the synapses.
EvolutionaryTrace; Q62645; -.
PRO; PR:Q62645; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000021063; -.
ExpressionAtlas; Q62645; baseline and differential.
Genevisible; Q62645; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0008328; C:ionotropic glutamate receptor complex; TAS:RGD.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0005261; F:cation channel activity; IDA:RGD.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0016595; F:glutamate binding; IMP:RGD.
GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
GO; GO:0042165; F:neurotransmitter binding; IMP:RGD.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:RGD.
GO; GO:0022843; F:voltage-gated cation channel activity; IMP:RGD.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:RGD.
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;
3D-structure; Alternative splicing; 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_0000011585.
TOPO_DOM 28 580 Extracellular. {ECO:0000255}.
TRANSMEM 581 601 Helical. {ECO:0000255}.
TOPO_DOM 602 653 Cytoplasmic. {ECO:0000255}.
TRANSMEM 654 674 Helical. {ECO:0000255}.
TOPO_DOM 675 841 Extracellular. {ECO:0000255}.
TRANSMEM 842 862 Helical. {ECO:0000255}.
TOPO_DOM 863 1323 Cytoplasmic. {ECO:0000255}.
MOTIF 1321 1323 PDZ-binding.
COMPBIAS 278 283 Poly-Gly.
COMPBIAS 905 913 Poly-Pro.
COMPBIAS 1030 1035 Poly-Ala.
COMPBIAS 1197 1201 Poly-Pro.
SITE 639 639 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 1303 1303 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q03391}.
MOD_RES 1313 1313 Phosphoserine.
{ECO:0000250|UniProtKB:Q03391}.
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 452 480 {ECO:0000269|PubMed:21522138}.
DISULFID 459 481 {ECO:0000269|PubMed:21522138}.
DISULFID 770 825 {ECO:0000269|PubMed:21522138}.
VAR_SEQ 1265 1323 CPRAAPTRRLTGPSRHARRCPHAAHWGPPLPTASHRRHRGG
DLGTRRGSAHFSSLESEV -> RPCPPHRTGDTGAGTWAHA
GALRISPAWSPRYDAAPAPTPTPAAPSVSAGHGPRGRAKWT
GPSWVGKDRNGPGRTPPGAASCAPTPFALGEL (in
isoform 1). {ECO:0000303|PubMed:8428958}.
/FTId=VSP_000136.
CONFLICT 25 25 A -> V (in Ref. 3; AAA17833).
{ECO:0000305}.
CONFLICT 47 47 P -> Q (in Ref. 3; AAA17833).
{ECO:0000305}.
CONFLICT 67 67 G -> V (in Ref. 2; AAC37646).
{ECO:0000305}.
CONFLICT 94 94 R -> P (in Ref. 2; AAC37646/AAC37647).
{ECO:0000305}.
CONFLICT 305 305 R -> A (in Ref. 2; AAC37646/AAC37647).
{ECO:0000305}.
CONFLICT 635 635 A -> G (in Ref. 3; AAA17833).
{ECO:0000305}.
CONFLICT 974 974 E -> D (in Ref. 3; AAA17833).
{ECO:0000305}.
CONFLICT 1253 1253 A -> G (in Ref. 3; AAA17833).
{ECO:0000305}.
CONFLICT 1266 1267 PR -> TT (in Ref. 3; AAA17833).
{ECO:0000305}.
STRAND 428 433 {ECO:0000244|PDB:3OEN}.
TURN 437 439 {ECO:0000244|PDB:3OEN}.
STRAND 440 444 {ECO:0000244|PDB:3OEN}.
TURN 447 449 {ECO:0000244|PDB:3OEN}.
STRAND 457 463 {ECO:0000244|PDB:3OEK}.
STRAND 478 483 {ECO:0000244|PDB:3OEN}.
HELIX 484 496 {ECO:0000244|PDB:3OEN}.
STRAND 499 504 {ECO:0000244|PDB:3OEN}.
STRAND 507 510 {ECO:0000244|PDB:3OEN}.
HELIX 520 526 {ECO:0000244|PDB:3OEN}.
STRAND 529 533 {ECO:0000244|PDB:3OEN}.
HELIX 541 544 {ECO:0000244|PDB:3OEN}.
STRAND 547 549 {ECO:0000244|PDB:3OEN}.
STRAND 554 563 {ECO:0000244|PDB:3OEN}.
HELIX 691 694 {ECO:0000244|PDB:3OEK}.
HELIX 696 698 {ECO:0000244|PDB:3OEK}.
STRAND 699 701 {ECO:0000244|PDB:3OEK}.
HELIX 712 720 {ECO:0000244|PDB:3OEN}.
HELIX 722 728 {ECO:0000244|PDB:3OEN}.
HELIX 729 731 {ECO:0000244|PDB:3OEN}.
HELIX 736 744 {ECO:0000244|PDB:3OEN}.
STRAND 749 754 {ECO:0000244|PDB:3OEN}.
HELIX 755 764 {ECO:0000244|PDB:3OEN}.
HELIX 766 768 {ECO:0000244|PDB:3OEN}.
STRAND 770 772 {ECO:0000244|PDB:3OEN}.
HELIX 773 776 {ECO:0000244|PDB:3OEN}.
STRAND 779 784 {ECO:0000244|PDB:3OEN}.
STRAND 787 789 {ECO:0000244|PDB:3OEN}.
HELIX 795 807 {ECO:0000244|PDB:3OEN}.
HELIX 810 819 {ECO:0000244|PDB:3OEN}.
SEQUENCE 1323 AA; 143101 MW; 40F7D60192579564 CRC64;
MRGAGGPRGP RGPAKMLLLL ALACASPFPE EVPGPGAVGG 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 LPGGSPLPAG
LFAVRSAGWR DDLARRVAAG VAVVARGAQA LLRDYGFLPE LGHDCRTQNR 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 GAAIADGFHR
YYGPIEPQGL GLGEARAAPR GAAGRPLSPP TTQPPQKPPP SYFAIVREQE PTEPPAGAFP
GFPSPPAPPA AAAAAVGPPL CRLAFEDESP PAPSRWPRSD PESQPLLGGG AGGPSAGAPT
APPPRRAAPP PCAYLDLEPS PSDSEDSESL GGASLGGLEP WWFADFPYPY AERLGPPPGR
YWSVDKLGGW RAGSWDYLPP RGGPAWHCRH CASLELLPPP RHLSCSHDGL DGGWWAPPPP
PWAAGPPPRR RARCGCPRPH PHRPRASHRA PAAAPHHHRH RRAAGGWDFP PPAPTSRSLE
DLSSCPRAAP TRRLTGPSRH ARRCPHAAHW GPPLPTASHR RHRGGDLGTR RGSAHFSSLE
SEV


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