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Q00959 (NMDE1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate receptor ionotropic, NMDA 2A
Short name=GluN2A
Alternative name(s):
Glutamate [NMDA] receptor subunit epsilon-1
N-methyl D-aspartate receptor subtype 2A
Short name=NMDAR2A
Short name=NR2A
Gene names
Name:Grin2a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

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. Interacts with HIP1 and NETO1 By similarity. Interacts with PDZ domains of INADL and DLG4. Interacts with LRFN2. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein Ref.8.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR2A/GRIN2A subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
Metal-binding
Zinc
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to amino acid stimulus

Inferred from mutant phenotype PubMed 19154422. Source: RGD

cellular response to dsRNA

Inferred from expression pattern PubMed 19958814. Source: RGD

cellular response to growth factor stimulus

Inferred from expression pattern PubMed 19958814. Source: RGD

cellular response to lipid

Inferred from expression pattern PubMed 19819306. Source: RGD

cellular response to magnesium ion

Inferred from expression pattern PubMed 19154422. Source: RGD

cellular response to manganese ion

Inferred from expression pattern PubMed 19643132. Source: RGD

cellular response to zinc ion

Inferred from mutant phenotype PubMed 19240037. Source: RGD

cerebral cortex development

Inferred from expression pattern PubMed 19409459. Source: RGD

hippocampus development

Inferred from expression pattern PubMed 19535712. Source: RGD

memory

Inferred from direct assay PubMed 16157280. Source: UniProtKB

positive regulation of cell death

Inferred from direct assay PubMed 20168047. Source: RGD

positive regulation of excitatory postsynaptic membrane potential

Inferred from direct assay PubMed 12930820. Source: BHF-UCL

protein tetramerization

Inferred from direct assay PubMed 22493736. Source: RGD

regulation of action potential

Inferred from mutant phenotype PubMed 16904707PubMed 17655746. Source: RGD

regulation of long-term neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 16904707PubMed 17655746. Source: RGD

response to amine stimulus

Inferred from expression pattern PubMed 19918184. Source: RGD

response to calcium ion

Inferred from expression pattern PubMed 19761817. Source: RGD

response to carbohydrate stimulus

Inferred from expression pattern PubMed 19695778. Source: RGD

response to cocaine

Inferred from expression pattern PubMed 19322657. Source: RGD

response to drug

Inferred from expression pattern PubMed 20084674PubMed 20417256. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 19673743. Source: RGD

response to fungicide

Inferred from expression pattern PubMed 19591855. Source: RGD

response to light stimulus

Inferred from expression pattern PubMed 19850826. Source: RGD

response to methylmercury

Inferred from expression pattern PubMed 19409459. Source: RGD

response to other organism

Inferred from expression pattern PubMed 19563853. Source: RGD

rhythmic process

Inferred from direct assay PubMed 16477151. Source: RGD

spinal cord development

Inferred from expression pattern PubMed 19446017. Source: RGD

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from direct assay PubMed 8702950. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

outer membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

postsynaptic density

Inferred from direct assay PubMed 19339621. Source: RGD

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

presynaptic membrane

Inferred from direct assay PubMed 16157280. Source: UniProtKB

terminal bouton

Inferred from direct assay PubMed 19666514. Source: RGD

   Molecular_functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from direct assay PubMed 16477151PubMed 22098737Ref.3. Source: RGD

extracellular-glutamate-gated ion channel activity

Inferred from electronic annotation. Source: InterPro

glutamate binding

Inferred from mutant phenotype PubMed 9425000. Source: UniProtKB

neurotransmitter binding

Inferred from direct assay PubMed 16477151. Source: RGD

protein heterodimerization activity

Inferred from direct assay PubMed 21544205. Source: RGD

voltage-gated cation channel activity

Inferred from mutant phenotype PubMed 17050728. Source: RGD

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 14641442Glutamate receptor ionotropic, NMDA 2A
PRO_0000011576

Regions

Topological domain23 – 555533Extracellular Potential
Transmembrane556 – 57621Helical; Potential
Topological domain577 – 63357Cytoplasmic Potential
Transmembrane634 – 65421Helical; Potential
Topological domain655 – 816162Extracellular Potential
Transmembrane817 – 83721Helical; Potential
Topological domain838 – 1464627Cytoplasmic Potential
Region511 – 5133Glutamate binding
Region689 – 6902Glutamate binding
Motif1462 – 14643PDZ-binding

Sites

Metal binding1281Zinc By similarity
Metal binding2831Zinc By similarity
Binding site5181Glutamate
Binding site7311Glutamate; via amide nitrogen
Site6141Functional determinant of NMDA receptors By similarity

Amino acid modifications

Modified residue8881Phosphothreonine By similarity
Modified residue9171Phosphoserine By similarity
Modified residue9291Phosphoserine By similarity
Modified residue9431Phosphotyrosine By similarity
Modified residue10251Phosphoserine By similarity
Modified residue14591Phosphoserine By similarity
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation5411N-linked (GlcNAc...) Potential
Disulfide bond87 ↔ 320 By similarity

Experimental info

Sequence conflict2461L → F in BAA02498. Ref.3
Sequence conflict7581S → T in BAA02498. Ref.3
Sequence conflict7581S → T in AAB58801. Ref.4
Sequence conflict9901E → D in AAB58801. Ref.4

Secondary structure

1 ........................................................ 1464
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00959 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: DC1528E1898DECA4

FASTA1,464165,469
        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

« Hide

References

[1]"Heteromeric NMDA receptors: molecular and functional distinction of subtypes."
Monyer H., Sprengel R., Schoepfer R., Herb A., Higuchi M., Lomeli H., Burnashev N., Sakmann B., Seeburg P.H.
Science 256:1217-1221(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]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
Cited for: SEQUENCE REVISION TO 595 AND 597-598.
[3]"Molecular characterization of the family of the N-methyl-D-aspartate receptor subunits."
Ishii T., Moriyoshi K., Sugihara H., Sakurada K., Kadotani H., Yokoi M., Akazawa C., Shigemoto R., Mizuno N., Masu M., Nakanishi S.
J. Biol. Chem. 268:2836-2843(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Forebrain.
[4]"Nucleotide sequence of rat NMDA receptor gene NMDAR2A."
Boulter J.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[5]"Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95."
Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H.
Science 269:1737-1740(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG4.
[6]"A novel multiple PDZ domain-containing molecule interacting with N-methyl-d-aspartate receptors and neuronal cell adhesion proteins."
Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M., Toyoda A., Suedhof T.C., Takai Y.
J. Biol. Chem. 273:21105-21110(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AIP1.
[7]"CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins."
Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.
Mol. Cell. Neurosci. 11:161-172(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INADL.
[8]"Assembly with the NR1 subunit is required for surface expression of NR3A-containing NMDA receptors."
Perez-Otano I., Schulteis C.T., Contractor A., Lipton S.A., Trimmer J.S., Sucher N.J., Heinemann S.F.
J. Neurosci. 21:1228-1237(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
[9]"An NMDA receptor signaling complex with protein phosphatase 2A."
Chan S.F., Sucher N.J.
J. Neurosci. 21:7985-7992(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1; GRIN3A AND PPP2CB.
[10]"Association of NR3A with the N-methyl-D-aspartate receptor NR1 and NR2 subunits."
Al-Hallaq R.A., Jarabek B.R., Fu Z., Vicini S., Wolfe B.B., Yasuda R.P.
Mol. Pharmacol. 62:1119-1127(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
[11]"Characterization and comparison of the NR3A subunit of the NMDA receptor in recombinant systems and primary cortical neurons."
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.
J. Neurophysiol. 87:2052-2063(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3A.
[12]"A novel family of adhesion-like molecules that interacts with the NMDA receptor."
Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.
J. Neurosci. 26:2174-2183(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LRFN2.
[13]"Subunit arrangement and function in NMDA receptors."
Furukawa H., Singh S.K., Mancusso R., Gouaux E.
Nature 438:185-192(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 401-802 IN COMPLEXES WITH GRIN1 AND GLUTAMATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M91561 mRNA. Translation: AAC03565.1.
D13211 mRNA. Translation: BAA02498.1.
AF001423 mRNA. Translation: AAB58801.1.
IPIIPI00326054.
PIRA43274.
RefSeqNP_036705.3. NM_012573.3.
UniGeneRn.9710.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A5SX-ray1.70A401-802[»]
2A5TX-ray2.00B401-802[»]
ProteinModelPortalQ00959.
SMRQ00959. Positions 404-801.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-34031N.
IntActQ00959. 1 interaction.
MINTMINT-93314.

Protein family/group databases

TCDB1.A.10.1.6. glutamate-gated ion channel (GIC) family of neurotransmitter receptors.

PTM databases

PhosphoSiteQ00959.

Proteomic databases

PaxDbQ00959.
PRIDEQ00959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24409.
KEGGrno:24409.
UCSCRGD:2737. rat.

Organism-specific databases

CTD2903.
RGD2737. Grin2a.

Phylogenomic databases

eggNOGNOG282132.
HOGENOMHOG000113802.
HOVERGENHBG052635.
InParanoidQ00959.
KOK05209.
OrthoDBEOG4X0MRG.

Gene expression databases

ArrayExpressQ00959.
GenevestigatorQ00959.
GermOnlineENSRNOG00000033942. Rattus norvegicus.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR018884. NMDAR2_C.
IPR001638. SBP_bac_3.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10565. NMDAR2_C. 1 hit.
PF00497. SBP_bac_3. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ00959.
ChEMBLCHEMBL310.
EvolutionaryTraceQ00959.
NextBio603227.

Entry information

Entry nameNMDE1_RAT
AccessionPrimary (citable) accession number: Q00959
Secondary accession number(s): O08948, Q63728
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents