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P35436 (NMDE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 and GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB. Interacts with PDZ domains of AIP1, INADL 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. Ref.3 Ref.4 Ref.5 Ref.7 Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein Ref.4.

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Inferred from mutant phenotype PubMed 11160454PubMed 14645471. Source: GOC

calcium ion transport

Inferred from mutant phenotype PubMed 11160454PubMed 14645471PubMed 16045501. Source: MGI

directional locomotion

Inferred from genetic interaction PubMed 8987814. Source: MGI

dopamine metabolic process

Inferred from mutant phenotype PubMed 11160454. Source: MGI

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from mutant phenotype PubMed 11160454PubMed 11487658PubMed 12754515PubMed 14750973PubMed 7816096PubMed 8699248PubMed 9427357PubMed 9512392. Source: GOC

learning

Inferred from mutant phenotype PubMed 11160454PubMed 9427357. Source: MGI

learning or memory

Inferred from mutant phenotype PubMed 16045501PubMed 9712642. Source: MGI

locomotion

Inferred from mutant phenotype PubMed 11160454PubMed 14750973. Source: MGI

locomotory behavior

Traceable author statement PubMed 12427824. Source: UniProtKB

memory

Inferred from mutant phenotype PubMed 9458051. Source: MGI

negative regulation of protein catabolic process

Inferred from genetic interaction PubMed 15317856. Source: MGI

neurogenesis

Inferred from mutant phenotype PubMed 12941447. Source: MGI

positive regulation of apoptotic process

Inferred from genetic interaction PubMed 17803966. Source: MGI

protein localization

Inferred from mutant phenotype PubMed 15317856. Source: MGI

regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 11530236PubMed 14645471PubMed 16045501PubMed 16157280PubMed 8699248PubMed 8987814PubMed 9147327. Source: MGI

regulation of membrane potential

Inferred from mutant phenotype PubMed 7816096PubMed 9712642. Source: MGI

regulation of postsynaptic membrane potential

Inferred from mutant phenotype PubMed 16157280. Source: MGI

regulation of sensory perception of pain

Inferred from mutant phenotype PubMed 10771345. Source: MGI

regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 12427824. Source: UniProtKB

regulation of synaptic transmission

Inferred from mutant phenotype PubMed 12427824. Source: UniProtKB

response to amphetamine

Inferred from mutant phenotype PubMed 15731593. Source: MGI

response to drug

Inferred from mutant phenotype PubMed 14750973. Source: MGI

response to ethanol

Inferred from mutant phenotype PubMed 11530236. Source: MGI

response to wounding

Inferred from mutant phenotype PubMed 9822733. Source: MGI

sensory perception of pain

Inferred from mutant phenotype PubMed 10694228. Source: MGI

serotonin metabolic process

Inferred from mutant phenotype PubMed 11160454. Source: MGI

sleep

Inferred from mutant phenotype PubMed 12754515. Source: MGI

startle response

Inferred from mutant phenotype PubMed 11488959. Source: MGI

synaptic transmission

Inferred from mutant phenotype PubMed 9147327. Source: MGI

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

visual learning

Inferred from mutant phenotype PubMed 7816096. Source: MGI

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from physical interaction PubMed 7929101PubMed 9003035. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 17229826. Source: BHF-UCL

dendritic spine

Inferred from sequence alignment PubMed 16221859. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 16814779. Source: MGI

membrane

Inferred from direct assay PubMed 18054859PubMed 8840015PubMed 9003035. Source: MGI

neuron projection

Inferred from direct assay PubMed 21558424. Source: BHF-UCL

neuronal postsynaptic density

Inferred from direct assay PubMed 21664258. Source: BHF-UCL

postsynaptic density

Inferred from direct assay PubMed 15317856. Source: MGI

postsynaptic membrane

Inferred from direct assay PubMed 12103442PubMed 12890763. Source: MGI

presynaptic membrane

Inferred from direct assay PubMed 16157280. Source: UniProtKB

synapse

Inferred from direct assay PubMed 14622577PubMed 14645471PubMed 16710293. Source: MGI

synaptic vesicle

Inferred from direct assay PubMed 20418887. Source: MGI

   Molecular_functionN-methyl-D-aspartate selective glutamate receptor activity

Inferred from mutant phenotype PubMed 11160454PubMed 11487658PubMed 12754515PubMed 14750973PubMed 7816096PubMed 8699248PubMed 9427357PubMed 9512392. Source: MGI

calcium channel activity

Inferred from mutant phenotype PubMed 11160454PubMed 14645471. Source: MGI

cation channel activity

Inferred from mutant phenotype PubMed 8699248PubMed 9427357. Source: MGI

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.5Ref.7. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 14641442Glutamate receptor ionotropic, NMDA 2A
PRO_0000011574

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 By similarity
Region689 – 6902Glutamate binding By similarity
Motif1462 – 14643PDZ-binding

Sites

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

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation5411N-linked (GlcNAc...) Potential
Disulfide bond87 ↔ 320 By similarity

Sequences

Sequence LengthMass (Da)Tools
P35436 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 438986DD5666C152

FASTA1,464165,421
        10         20         30         40         50         60 
MGRLGYWTLL VLPALLVWHG PAQNAAAEKG TPALNIAVLL 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 YGQTEKPETP 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 MHQYMTKFNQ RGVEDALVSL 

       730        740        750        760        770        780 
KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFATTG 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 AADFIQRGSL IVDMVSDKGN LIYSDNRSFQ GKDSIFGENM 

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

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

      1090       1100       1110       1120       1130       1140 
KTKDNFKRSM ASKYPKDCSE VERTYVKTKA SSPRDKIYTI DGEKEPSFHL DPPQFIENIV 

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

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

      1270       1280       1290       1300       1310       1320 
ATREEAYQQD WSQNNALQFQ KNKLKINRQH SYDNILDKPR EIDLSRPSRS ISLKDRERLL 

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

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

      1450       1460 
TPRVLNSCSN RRVYKKMPSI ESDV 

« Hide

References

« Hide 'large scale' references
[1]"Functional characterization of a heteromeric NMDA receptor channel expressed from cloned cDNAs."
Meguro H., Mori H., Araki K., Kushiya E., Kutsuwada T., Yamazaki M., Kumanishi T., Arakawa M., Sakimura K., Mishina M.
Nature 357:70-74(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]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
Cited for: SEQUENCE REVISION TO 384.
[3]"Cloning and characterization of a novel NMDA receptor subunit NR3B: a dominant subunit that reduces calcium permeability."
Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.
Brain Res. Mol. Brain Res. 100:43-52(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
[4]"Specific assembly with the NMDA receptor 3B subunit controls surface expression and calcium permeability of NMDA receptors."
Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.
J. Neurosci. 23:10064-10073(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
[5]"NMDA receptor function and NMDA receptor-dependent phosphorylation of huntingtin is altered by the endocytic protein HIP1."
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.
J. Neurosci. 27:2298-2308(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIP1.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
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.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[7]"Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for synaptic plasticity and learning."
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.
PLoS Biol. 7:E41-E41(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NETO1.
[8]"Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down's syndrome."
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. expand/collapse author list , Zhang Y.W., Lipton S.A., Hong W., Xu H.
Nat. Med. 19:473-480(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX27.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10217 mRNA. Translation: BAA01069.2.
CCDSCCDS27943.1.
PIRS29159.
RefSeqNP_032196.2. NM_008170.2.
XP_006521857.1. XM_006521794.1.
UniGeneMm.2953.

3D structure databases

ProteinModelPortalP35436.
SMRP35436. Positions 32-392, 404-841.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200068. 13 interactions.
DIPDIP-31567N.
IntActP35436. 6 interactions.
MINTMINT-103939.
STRING10090.ENSMUSP00000111501.

Chemistry

BindingDBP35436.
GuidetoPHARMACOLOGY456.

PTM databases

PhosphoSiteP35436.

Proteomic databases

PaxDbP35436.
PRIDEP35436.

Protocols and materials databases

DNASU14811.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032331; ENSMUSP00000032331; ENSMUSG00000059003.
ENSMUST00000115835; ENSMUSP00000111501; ENSMUSG00000059003.
GeneID14811.
KEGGmmu:14811.
UCSCuc007ydc.1. mouse.

Organism-specific databases

CTD2903.
MGIMGI:95820. Grin2a.

Phylogenomic databases

eggNOGNOG282132.
GeneTreeENSGT00540000070221.
HOGENOMHOG000113802.
HOVERGENHBG052635.
InParanoidP35436.
KOK05209.
OMADYDWHVF.
OrthoDBEOG72ZCD1.
PhylomeDBP35436.
TreeFamTF314731.

Gene expression databases

BgeeP35436.
GenevestigatorP35436.

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.
IPR028082. Peripla_BP_I.
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]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

NextBio286999.
PROP35436.
SOURCESearch...

Entry information

Entry nameNMDE1_MOUSE
AccessionPrimary (citable) accession number: P35436
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot