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UniProtKB/Swiss-Prot entry Q00959


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NMDE1_RAT
Primary accession number Q00959
Secondary accession numbers O08948 Q63728
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on December 15, 1998 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 85)
Name and origin of the protein
Protein name Glutamate [NMDA] receptor subunit epsilon-1 [Precursor]
Synonyms N-methyl D-aspartate receptor subtype 2A
NMDAR2A
NR2A
Gene name
Name: Grin2a
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=1350383 [NCBI, ExPASy, EBI, Israel, Japan]
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]
SEQUENCE REVISION TO 595 AND 597-598.
Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H., Burnashev N., Sakmann B., Seeburg P.H.;
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Forebrain;
PubMed=8428958 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Boulter J.;
"Nucleotide sequence of rat NMDA receptor gene NMDAR2A.";
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH DLG4.
PubMed=7569905 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
INTERACTION WITH AIP1.
DOI=10.1074/jbc.273.33.21105; PubMed=9694864 [NCBI, ExPASy, EBI, Israel, Japan]
Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M., Toyoda A., Suedhof T.C., Takai Y.;
"A novel multiple PDZ domain-containing molecule interacting with N-methyl-d-aspartate receptors and neuronal cell adhesion proteins.";
J. Biol. Chem. 273:21105-21110(1998).
[7]
INTERACTION WITH INADL.
DOI=10.1006/mcne.1998.0679; PubMed=9647694 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
PubMed=11160393 [NCBI, ExPASy, EBI, Israel, Japan]
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; GRIN3A AND PPP2CB.
PubMed=11588171 [NCBI, ExPASy, EBI, Israel, Japan]
Chan S.F., Sucher N.J.;
"An NMDA receptor signaling complex with protein phosphatase 2A.";
J. Neurosci. 21:7985-7992(2001).
[10]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
DOI=10.1124/mol.62.5.1119; PubMed=12391275 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
DOI=10.1152/jn.00531.2001; PubMed=11929923 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 401-802 IN COMPLEXES WITH GRIN1 AND GLUTAMATE.
DOI=10.1038/nature04089; PubMed=16281028 [NCBI, ExPASy, EBI, Israel, Japan]
Furukawa H., Singh S.K., Mancusso R., Gouaux E.;
"Subunit arrangement and function in NMDA receptors.";
Nature 438:185-192(2005).
Comments
  • 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, GRIN3A and PPP2CB. Interacts with AIP1. Found in a complex with GRIN1 and GRIN3B (By similarity). Interacts with PDZ domains of INADL and DLG4.
  • INTERACTION:
    P31016:Dlg4; NbExp=2; IntAct=EBI-630970, EBI-375655;
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein.
  • SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10) family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M91561; AAC03565.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D13211; BAA02498.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF001423; AAB58801.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A43274; A43274.
RefSeq NP_036705.3; -.
UniGene Rn.9710
3D structure databases
PDB
2A5S; X-ray; 1.70 A; A=401-802.[ExPASy / RCSB / EBI]
2A5T; X-ray; 2.00 A; B=401-802.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2A5S; -.
2A5T; -.
ModBase Q00959.
Protein-protein interaction databases
IntAct Q00959; -.
PTM databases
PhosphoSite Q00959; -.
Organism-specific databases
RGD 2737; Grin2a.
Gene expression databases
ArrayExpress Q00959; -.
GermOnline ENSRNOG00000033942; Rattus norvegicus.
Ontologies
GO
GO:0017146; Cellular component: N-methyl-D-aspartate selective glutamate receptor complex (inferred from direct assay from UniProtKB).
GO:0043005; Cellular component: neuron projection (inferred from direct assay from UniProtKB).
GO:0042734; Cellular component: presynaptic membrane (inferred from direct assay from UniProtKB).
GO:0016595; Molecular function: glutamate binding (inferred from mutant phenotype from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0007613; Biological process: memory (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR015683; Glutamate_receptor-rel.
IPR001320; Iontro_glu_rcpt.
IPR001508; NMDA_rcpt.
Graphical view of domain structure.
PANTHER PTHR18966; Glut_Rec_Related; 1.
Pfam PF00060; Lig_chan; 1.
Pfam graphical view of domain structure.
PRINTS PR00177; NMDARECEPTOR.
SMART SM00079; PBPe; 1.
SMART graphical view of domain structure.
BLOCKS Q00959.
Genome annotation databases
Ensembl ENSRNOG00000033942; Rattus norvegicus. [Contig view]
GeneID 24409; -.
KEGG rno:24409; -.
Phylogenomic databases
HOVERGEN Q00959; -.
Other
ProtoNet Q00959.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Cell junction; Cell membrane; Glycoprotein; Ion transport; Ionic channel; Magnesium; Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     22  22     Potential. 
CHAIN   23   1464  1442     Glutamate [NMDA] receptor subunit epsilon-1. PRO_0000011576
TOPO_DOM   23    555  533     Extracellular (Potential). 
TRANSMEM   556    576  21     Potential. 
TOPO_DOM   577    633  57     Cytoplasmic (Potential). 
TRANSMEM   634    654  21     Potential. 
TOPO_DOM   655    816  162     Extracellular (Potential). 
TRANSMEM   817    837  21     Potential. 
TOPO_DOM   838   1464  627     Cytoplasmic (Potential). 
REGION   511    513  3     Glutamate binding. 
REGION   689    690  2     Glutamate binding. 
MOTIF   1462   1464  3     PDZ-binding. 
BINDING   518    518        Glutamate. 
BINDING   731    731        Glutamate; via amide nitrogen. 
SITE   614    614  1     Functional determinant of NMDA receptors (By similarity). 
MOD_RES   888    888        Phosphothreonine (By similarity). 
MOD_RES   912    912        Phosphoserine (By similarity). 
MOD_RES   917    917        Phosphoserine (By similarity). 
MOD_RES   929    929        Phosphoserine (By similarity). 
MOD_RES   943    943        Phosphotyrosine (By similarity). 
MOD_RES   1025   1025        Phosphoserine (By similarity). 
MOD_RES   1459   1459        Phosphoserine (By similarity). 
CARBOHYD   75     75        N-linked (GlcNAc...) (Potential). 
CARBOHYD   340    340        N-linked (GlcNAc...) (Potential). 
CARBOHYD   443    443        N-linked (GlcNAc...) (Potential). 
CARBOHYD   444    444        N-linked (GlcNAc...) (Potential). 
CARBOHYD   541    541        N-linked (GlcNAc...) (Potential). 
CONFLICT   246    246        L -> F (in Ref. 3; BAA02498). 
CONFLICT   758    758        S -> T (in Ref. 3; BAA02498 and 4; AAB58801). 
CONFLICT   990    990        E -> D (in Ref. 4; AAB58801). 
STRAND   406    410  5      
TURN   414    416  3      
STRAND   417    421  5      
STRAND   434    447  14      
STRAND   449    458  10      
HELIX   459    471  13      
STRAND   475    479  5      
STRAND   482    485  4      
HELIX   495    501  7      
STRAND   506    508  3      
HELIX   516    519  4      
STRAND   522    524  3      
STRAND   529    531  3      
STRAND   533    538  6      
HELIX   668    671  4      
HELIX   673    675  3      
STRAND   676    678  3      
HELIX   689    695  7      
HELIX   699    705  7      
HELIX   706    708  3      
HELIX   713    721  9      
STRAND   726    731  6      
HELIX   732    740  9      
STRAND   747    751  5      
HELIX   755    757  3      
STRAND   759    761  3      
STRAND   764    766  3      
HELIX   772    784  13      
HELIX   787    795  9      
Sequence information
Length: 1464 AA [This is the length of the unprocessed precursor] Molecular weight: 165469 Da [This is the MW of the unprocessed precursor] CRC64: DC1528E1898DECA4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGRLGYWTLL VLPALLVWRD PAQNAAAEKG PPALNIAVLL GHSHDVTERE LRNLWGPEQA 

        70         80         90        100        110        120 
TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSQT 

       130        140        150        160        170        180 
FIPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY 

       190        200        210        220        230        240 
RDFISFIKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL 

       250        260        270        280        290        300 
SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT 

       310        320        330        340        350        360 
TAASSMLEKF SYIPEAKASC YGQAEKPETP LHTLHQFMVN VTWDGKDLSF TEEGYQVHPR 

       370        380        390        400        410        420 
LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE PDDNHLSIVT LEEAPFVIVE 

       430        440        450        460        470        480 
DIDPLTETCV RNTVPCRKFV KINNSTNEGM NVKKCCKGFC IDILKKLSRT VKFTYDLYLV 

       490        500        510        520        530        540 
TNGKHGKKVN NVWNGMIGEV VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS 

       550        560        570        580        590        600 
NGTVSPSAFL EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT 

       610        620        630        640        650        660 
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA AFMIQEEFVD 

       670        680        690        700        710        720 
QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY MHQYMTRFNQ RGVEDALVSL 

       730        740        750        760        770        780 
KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFASTG YGIALQKGSP WKRQIDLALL 

       790        800        810        820        830        840 
QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL 

       850        860        870        880        890        900 
FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS 

       910        920        930        940        950        960 
AKNISNMSNM NSSRMDSPKR ATDFIQRGSL IVDMVSDKGN LIYSDNRSFQ GKDSIFGDNM 

       970        980        990       1000       1010       1020 
NELQTFVANR HKDNLSNYVF QGQHPLTLNE SNPNTVEVAV STESKGNSRP RQLWKKSMES 

      1030       1040       1050       1060       1070       1080 
LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR YLPEEVAHSD ISETSSRATC HREPDNNKNH 

      1090       1100       1110       1120       1130       1140 
KTKDNFKRSM ASKYPKDCSD VDRTYMKTKA SSPRDKIYTI DGEKEPSFHL DPPQFVENIT 

      1150       1160       1170       1180       1190       1200 
LPENVGFPDT YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH 

      1210       1220       1230       1240       1250       1260 
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGNP 

      1270       1280       1290       1300       1310       1320 
ATREEVYQQD WSQNNALQFQ KNKLRINRQH SYDNILDKPR EIDLSRPSRS ISLKDRERLL 

      1330       1340       1350       1360       1370       1380 
EGNLYGSLFS VPSSKLLGNK SSLFPQGLED SKRSKSLLPD HASDNPFLHT YGDDQRLVIG 

      1390       1400       1410       1420       1430       1440 
RCPSDPYKHS LPSQAVNDSY LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNTMYS 

      1450       1460 
TPRVLNSCSN RRVYKKMPSI ESDV 

Q00959 in FASTA format

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View entry in raw text format (no links)
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