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Glutamate receptor ionotropic, NMDA 2A (GluN2A) (Glutamate [NMDA] receptor subunit epsilon-1) (N-methyl D-aspartate receptor subtype 2A) (NMDAR2A) (NR2A)

 NMDE1_MOUSE             Reviewed;        1464 AA.
P35436;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
30-AUG-2017, entry version 176.
RecName: Full=Glutamate receptor ionotropic, NMDA 2A;
Short=GluN2A;
AltName: Full=Glutamate [NMDA] receptor subunit epsilon-1;
AltName: Full=N-methyl D-aspartate receptor subtype 2A;
Short=NMDAR2A;
Short=NR2A;
Flags: Precursor;
Name=Grin2a;
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].
PubMed=1374164; DOI=10.1038/357070a0;
Meguro H., Mori H., Araki K., Kushiya E., Kutsuwada T., Yamazaki M.,
Kumanishi T., Arakawa M., Sakimura K., Mishina M.;
"Functional characterization of a heteromeric NMDA receptor channel
expressed from cloned cDNAs.";
Nature 357:70-74(1992).
[2]
SEQUENCE REVISION TO 384.
Meguro H., Mori H., Araki K., Kushiya E., Kutsuwada T., Yamazaki M.,
Kumanishi T., Arakawa M., Sakimura K., Mishina M.;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
SUBCELLULAR LOCATION, AND 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).
[5]
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).
[6]
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).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929
AND SER-1059, 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).
[9]
INTERACTION WITH SNX27.
PubMed=23524343; DOI=10.1038/nm.3117;
Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y., Loo L.S.,
Cai L., Thompson R.C., Yang B., Chen Y., Johnson P.F., Wu C., Bu G.,
Mobley W.C., Zhang D., Gage F.H., Ranscht B., Zhang Y.W., Lipton S.A.,
Hong W., Xu H.;
"Loss of sorting nexin 27 contributes to excitatory synaptic
dysfunction by modulating glutamate receptor recycling in Down's
syndrome.";
Nat. Med. 19:473-480(2013).
-!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
possesses high calcium permeability and voltage-dependent
sensitivity to magnesium. Activation requires binding of agonist
to both types of subunits.
-!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a
epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
subunit (GRIN3A or GRIN3B). Found in a complex with GRIN1 and
GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB.
Interacts with PDZ domains of AIP1, PATJ and DLG4 (By similarity).
Interacts with HIP1 and NETO1. Interacts with LRFN2 (By
similarity). Interacts with SNX27 (via PDZ domain); the
interaction is required for recycling to the plasma membrane when
endocytosed and prevent degradation in lysosomes. {ECO:0000250,
ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:14602821,
ECO:0000269|PubMed:17329427, ECO:0000269|PubMed:19243221,
ECO:0000269|PubMed:23524343}.
-!- INTERACTION:
Q62108:Dlg4; NbExp=7; IntAct=EBI-400115, EBI-300895;
Q63ZW7:Patj; NbExp=4; IntAct=EBI-400115, EBI-8366894;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14602821};
Multi-pass membrane protein {ECO:0000269|PubMed:14602821}. Cell
junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:14602821}; Multi-pass membrane protein
{ECO:0000269|PubMed:14602821}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR2A/GRIN2A subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D10217; BAA01069.2; -; mRNA.
CCDS; CCDS27943.1; -.
PIR; S29159; S29159.
RefSeq; NP_032196.2; NM_008170.2.
RefSeq; XP_006521857.1; XM_006521794.3.
UniGene; Mm.2953; -.
ProteinModelPortal; P35436; -.
BioGrid; 200068; 18.
DIP; DIP-31567N; -.
IntAct; P35436; 6.
MINT; MINT-103939; -.
STRING; 10090.ENSMUSP00000032331; -.
ChEMBL; CHEMBL3832634; -.
iPTMnet; P35436; -.
PhosphoSitePlus; P35436; -.
PaxDb; P35436; -.
PeptideAtlas; P35436; -.
PRIDE; P35436; -.
DNASU; 14811; -.
Ensembl; ENSMUST00000032331; ENSMUSP00000032331; ENSMUSG00000059003.
Ensembl; ENSMUST00000115835; ENSMUSP00000111501; ENSMUSG00000059003.
Ensembl; ENSMUST00000199708; ENSMUSP00000142900; ENSMUSG00000059003.
GeneID; 14811; -.
KEGG; mmu:14811; -.
UCSC; uc007ydc.1; mouse.
CTD; 2903; -.
MGI; MGI:95820; Grin2a.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00760000119186; -.
HOGENOM; HOG000113802; -.
HOVERGEN; HBG052635; -.
InParanoid; P35436; -.
KO; K05209; -.
OMA; RDFISFI; -.
OrthoDB; EOG091G09KH; -.
PhylomeDB; P35436; -.
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; SALM protein interactions at the synapses.
PRO; PR:P35436; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000059003; -.
Genevisible; P35436; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0043197; C:dendritic spine; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
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: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; IMP:MGI.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0004972; F:NMDA glutamate receptor activity; IMP:MGI.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0033058; P:directional locomotion; IGI:MGI.
GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
GO; GO:0007612; P:learning; IMP:MGI.
GO; GO:0007611; P:learning or memory; IMP:MGI.
GO; GO:0040011; P:locomotion; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; TAS:UniProtKB.
GO; GO:0060291; P:long-term synaptic potentiation; IGI:MGI.
GO; GO:0007613; P:memory; IMP:MGI.
GO; GO:0050804; P:modulation of synaptic transmission; IMP:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; IGI:MGI.
GO; GO:0022008; P:neurogenesis; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:MGI.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:MGI.
GO; GO:0051930; P:regulation of sensory perception of pain; IMP:MGI.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
GO; GO:0001975; P:response to amphetamine; IMP:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0045471; P:response to ethanol; IMP:MGI.
GO; GO:0009611; P:response to wounding; IMP:MGI.
GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
GO; GO:0030431; P:sleep; IMP:MGI.
GO; GO:0001964; P:startle response; IMP:MGI.
GO; GO:0008542; P:visual learning; 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 22 {ECO:0000255}.
CHAIN 23 1464 Glutamate receptor ionotropic, NMDA 2A.
/FTId=PRO_0000011574.
TOPO_DOM 23 555 Extracellular. {ECO:0000255}.
TRANSMEM 556 576 Helical. {ECO:0000255}.
TOPO_DOM 577 633 Cytoplasmic. {ECO:0000255}.
TRANSMEM 634 654 Helical. {ECO:0000255}.
TOPO_DOM 655 816 Extracellular. {ECO:0000255}.
TRANSMEM 817 837 Helical. {ECO:0000255}.
TOPO_DOM 838 1464 Cytoplasmic. {ECO:0000255}.
REGION 511 513 Glutamate binding. {ECO:0000250}.
REGION 689 690 Glutamate binding. {ECO:0000250}.
MOTIF 1462 1464 PDZ-binding.
METAL 128 128 Zinc. {ECO:0000250}.
METAL 283 283 Zinc. {ECO:0000250}.
BINDING 518 518 Glutamate. {ECO:0000250}.
BINDING 731 731 Glutamate; via amide nitrogen.
{ECO:0000250}.
SITE 614 614 Functional determinant of NMDA receptors.
{ECO:0000250}.
MOD_RES 882 882 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 929 929 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1025 1025 Phosphoserine.
{ECO:0000250|UniProtKB:Q00959}.
MOD_RES 1059 1059 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1062 1062 Phosphoserine.
{ECO:0000250|UniProtKB:Q00959}.
MOD_RES 1198 1198 Phosphoserine.
{ECO:0000250|UniProtKB:Q00959}.
MOD_RES 1291 1291 Phosphoserine.
{ECO:0000250|UniProtKB:Q00959}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 380 380 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 443 443 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 87 320 {ECO:0000250}.
SEQUENCE 1464 AA; 165421 MW; 438986DD5666C152 CRC64;
MGRLGYWTLL VLPALLVWHG PAQNAAAEKG TPALNIAVLL GHSHDVTERE LRNLWGPEQA
TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSQT
FIPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY
RDFISFIKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL
SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
TAASSMLEKF SYIPEAKASC YGQTEKPETP LHTLHQFMVN VTWDGKDLSF TEEGYQVHPR
LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE PDDNHLSIVT LEEAPFVIVE
DIDPLTETCV RNTVPCRKFV KINNSTNEGM NVKKCCKGFC IDILKKLSRT VKFTYDLYLV
TNGKHGKKVN NVWNGMIGEV VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS
NGTVSPSAFL EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA AFMIQEEFVD
QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY MHQYMTKFNQ RGVEDALVSL
KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFATTG YGIALQKGSP WKRQIDLALL
QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL
FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
AKNISNMSNM NSSRMDSPKR AADFIQRGSL IVDMVSDKGN LIYSDNRSFQ GKDSIFGENM
NELQTFVANR HKDSLSNYVF QGQHPLTLNE SNPNTVEVAV STESKGNSRP RQLWKKSMES
LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR YLPEEVAHSD ISETSSRATC HREPDNNKNH
KTKDNFKRSM ASKYPKDCSE VERTYVKTKA SSPRDKIYTI DGEKEPSFHL DPPQFIENIV
LPENVDFPDT YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGNP
ATREEAYQQD WSQNNALQFQ KNKLKINRQH SYDNILDKPR EIDLSRPSRS ISLKDRERLL
EGNLYGSLFS VPSSKLLGNK SSLFPQGLED SKRSKSLLPD HTSDNPFLHT YGDDQRLVIG
RCPSDPYKHS LPSQAVNDSY LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNNMYS
TPRVLNSCSN RRVYKKMPSI ESDV


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