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Protein

Glutamate receptor ionotropic, NMDA 2A

Gene

Grin2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi128ZincBy similarity1
Metal bindingi283ZincBy similarity1
Binding sitei518Glutamate1
Sitei614Functional determinant of NMDA receptorsBy similarity1
Binding sitei731Glutamate; via amide nitrogen1

GO - Molecular functioni

  • ATPase binding Source: RGD
  • cell adhesion molecule binding Source: RGD
  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • glutamate binding Source: UniProtKB
  • glutamate receptor binding Source: RGD
  • ionotropic glutamate receptor activity Source: RGD
  • neurotransmitter binding Source: RGD
  • NMDA glutamate receptor activity Source: RGD
  • protein complex binding Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD
  • scaffold protein binding Source: BHF-UCL
  • voltage-gated cation channel activity Source: RGD
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • action potential Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to dsRNA Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to lipid Source: RGD
  • cellular response to magnesium ion Source: RGD
  • cellular response to manganese ion Source: RGD
  • cellular response to zinc ion Source: RGD
  • cerebral cortex development Source: RGD
  • chemical synaptic transmission Source: RGD
  • excitatory postsynaptic potential Source: RGD
  • hippocampus development Source: RGD
  • ionotropic glutamate receptor signaling pathway Source: RGD
  • memory Source: UniProtKB
  • positive regulation of cell death Source: RGD
  • positive regulation of excitatory postsynaptic potential Source: BHF-UCL
  • protein tetramerization Source: RGD
  • regulation of long-term neuronal synaptic plasticity Source: RGD
  • response to amine Source: RGD
  • response to ammonium ion Source: RGD
  • response to calcium ion Source: RGD
  • response to carbohydrate Source: RGD
  • response to cocaine Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to fungicide Source: RGD
  • response to light stimulus Source: RGD
  • response to manganese ion Source: RGD
  • response to methylmercury Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to other organism Source: RGD
  • rhythmic process Source: RGD
  • spinal cord development Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Protein family/group databases

TCDBi1.A.10.1.6. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Grin2a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2737. Grin2a.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 555ExtracellularSequence analysisAdd BLAST533
Transmembranei556 – 576HelicalSequence analysisAdd BLAST21
Topological domaini577 – 633CytoplasmicSequence analysisAdd BLAST57
Transmembranei634 – 654HelicalSequence analysisAdd BLAST21
Topological domaini655 – 816ExtracellularSequence analysisAdd BLAST162
Transmembranei817 – 837HelicalSequence analysisAdd BLAST21
Topological domaini838 – 1464CytoplasmicSequence analysisAdd BLAST627

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • dendritic spine Source: MGI
  • neuron projection Source: UniProtKB
  • NMDA selective glutamate receptor complex Source: UniProtKB
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: UniProtKB-SubCell
  • presynaptic membrane Source: UniProtKB
  • synapse Source: UniProtKB
  • terminal bouton Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL310.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001157623 – 1464Glutamate receptor ionotropic, NMDA 2AAdd BLAST1442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi75N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi87 ↔ 320By similarity
Glycosylationi340N-linked (GlcNAc...)Sequence analysis1
Glycosylationi443N-linked (GlcNAc...)Sequence analysis1
Glycosylationi444N-linked (GlcNAc...)Sequence analysis1
Glycosylationi541N-linked (GlcNAc...)Sequence analysis1
Modified residuei882PhosphoserineCombined sources1
Modified residuei890PhosphoserineCombined sources1
Modified residuei929PhosphoserineCombined sources1
Modified residuei1025PhosphoserineCombined sources1
Modified residuei1059PhosphoserineCombined sources1
Modified residuei1062PhosphoserineCombined sources1
Modified residuei1198PhosphoserineCombined sources1
Modified residuei1291PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ00959.
PRIDEiQ00959.

PTM databases

iPTMnetiQ00959.
PhosphoSitePlusiQ00959.
SwissPalmiQ00959.
UniCarbKBiQ00959.

Interactioni

Subunit structurei

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. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes (By similarity). Interacts with PDZ domains of PATJ and DLG4. Interacts with LRFN2.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4P310165EBI-630970,EBI-375655
SrcP054805EBI-630970,EBI-298680From a different organism.

GO - Molecular functioni

  • ATPase binding Source: RGD
  • cell adhesion molecule binding Source: RGD
  • glutamate receptor binding Source: RGD
  • protein complex binding Source: RGD
  • protein dimerization activity Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • receptor binding Source: RGD
  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi246574. 6 interactors.
DIPiDIP-34031N.
IntActiQ00959. 5 interactors.
MINTiMINT-93314.
STRINGi10116.ENSRNOP00000042235.

Chemistry databases

BindingDBiQ00959.

Structurei

Secondary structure

11464
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi406 – 410Combined sources5
Turni414 – 416Combined sources3
Beta strandi417 – 421Combined sources5
Turni424 – 426Combined sources3
Beta strandi434 – 447Combined sources14
Beta strandi449 – 458Combined sources10
Helixi459 – 471Combined sources13
Beta strandi475 – 479Combined sources5
Beta strandi482 – 485Combined sources4
Beta strandi488 – 491Combined sources4
Helixi495 – 501Combined sources7
Beta strandi506 – 508Combined sources3
Helixi516 – 519Combined sources4
Beta strandi522 – 524Combined sources3
Beta strandi529 – 531Combined sources3
Beta strandi533 – 538Combined sources6
Helixi668 – 671Combined sources4
Helixi673 – 675Combined sources3
Beta strandi676 – 678Combined sources3
Beta strandi686 – 688Combined sources3
Helixi689 – 697Combined sources9
Helixi699 – 705Combined sources7
Helixi706 – 708Combined sources3
Helixi713 – 721Combined sources9
Beta strandi726 – 731Combined sources6
Helixi732 – 740Combined sources9
Helixi743 – 745Combined sources3
Beta strandi747 – 751Combined sources5
Helixi752 – 754Combined sources3
Helixi755 – 757Combined sources3
Beta strandi759 – 761Combined sources3
Beta strandi764 – 766Combined sources3
Helixi772 – 784Combined sources13
Helixi787 – 795Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A5SX-ray1.70A401-539[»]
2A5TX-ray2.00B401-539[»]
4JWXX-ray1.50A404-801[»]
4NF4X-ray2.00B402-539[»]
B661-802[»]
4NF5X-ray1.90B402-539[»]
B661-802[»]
4NF6X-ray2.10B402-539[»]
B661-802[»]
4NF8X-ray1.86B402-539[»]
B661-802[»]
5DDNX-ray2.11B402-539[»]
B661-802[»]
5DDXX-ray1.95B402-539[»]
B661-802[»]
5DE4X-ray2.40B402-539[»]
B661-802[»]
5DEXX-ray2.40B402-539[»]
B661-802[»]
5I56X-ray2.28B402-539[»]
B661-800[»]
5I57X-ray1.70B402-539[»]
B661-800[»]
5I58X-ray2.52B402-539[»]
B661-800[»]
5I59X-ray2.25B402-539[»]
B661-800[»]
5JTYX-ray2.72B402-539[»]
B661-800[»]
ProteinModelPortaliQ00959.
SMRiQ00959.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00959.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni511 – 513Glutamate binding3
Regioni689 – 690Glutamate binding2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1462 – 1464PDZ-binding3

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00959.
KOiK05209.
PhylomeDBiQ00959.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRLGYWTLL VLPALLVWRD PAQNAAAEKG PPALNIAVLL GHSHDVTERE
60 70 80 90 100
LRNLWGPEQA TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF
110 120 130 140 150
GDDTDQEAVA QMLDFISSQT FIPILGIHGG ASMIMADKDP TSTFFQFGAS
160 170 180 190 200
IQQQATVMLK IMQDYDWHVF SLVTTIFPGY RDFISFIKTT VDNSFVGWDM
210 220 230 240 250
QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL SEARSLGLTG
260 270 280 290 300
YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
310 320 330 340 350
TAASSMLEKF SYIPEAKASC YGQAEKPETP LHTLHQFMVN VTWDGKDLSF
360 370 380 390 400
TEEGYQVHPR LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE
410 420 430 440 450
PDDNHLSIVT LEEAPFVIVE DIDPLTETCV RNTVPCRKFV KINNSTNEGM
460 470 480 490 500
NVKKCCKGFC IDILKKLSRT VKFTYDLYLV TNGKHGKKVN NVWNGMIGEV
510 520 530 540 550
VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS NGTVSPSAFL
560 570 580 590 600
EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT
610 620 630 640 650
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA
660 670 680 690 700
AFMIQEEFVD QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY
710 720 730 740 750
MHQYMTRFNQ RGVEDALVSL KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI
760 770 780 790 800
GSGYIFASTG YGIALQKGSP WKRQIDLALL QFVGDGEMEE LETLWLTGIC
810 820 830 840 850
HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL FYWKLRFCFT
860 870 880 890 900
GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
910 920 930 940 950
AKNISNMSNM NSSRMDSPKR ATDFIQRGSL IVDMVSDKGN LIYSDNRSFQ
960 970 980 990 1000
GKDSIFGDNM NELQTFVANR HKDNLSNYVF QGQHPLTLNE SNPNTVEVAV
1010 1020 1030 1040 1050
STESKGNSRP RQLWKKSMES LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR
1060 1070 1080 1090 1100
YLPEEVAHSD ISETSSRATC HREPDNNKNH KTKDNFKRSM ASKYPKDCSD
1110 1120 1130 1140 1150
VDRTYMKTKA SSPRDKIYTI DGEKEPSFHL DPPQFVENIT LPENVGFPDT
1160 1170 1180 1190 1200
YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
1210 1220 1230 1240 1250
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE
1260 1270 1280 1290 1300
DQMLQETGNP ATREEVYQQD WSQNNALQFQ KNKLRINRQH SYDNILDKPR
1310 1320 1330 1340 1350
EIDLSRPSRS ISLKDRERLL EGNLYGSLFS VPSSKLLGNK SSLFPQGLED
1360 1370 1380 1390 1400
SKRSKSLLPD HASDNPFLHT YGDDQRLVIG RCPSDPYKHS LPSQAVNDSY
1410 1420 1430 1440 1450
LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNTMYS TPRVLNSCSN
1460
RRVYKKMPSI ESDV
Length:1,464
Mass (Da):165,469
Last modified:December 15, 1998 - v2
Checksum:iDC1528E1898DECA4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti246L → F in BAA02498 (PubMed:8428958).Curated1
Sequence conflicti758S → T in BAA02498 (PubMed:8428958).Curated1
Sequence conflicti758S → T in AAB58801 (Ref. 4) Curated1
Sequence conflicti990E → D in AAB58801 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91561 mRNA. Translation: AAC03565.1.
D13211 mRNA. Translation: BAA02498.1.
AF001423 mRNA. Translation: AAB58801.1.
PIRiA43274.
RefSeqiNP_036705.3. NM_012573.3.
UniGeneiRn.9710.

Genome annotation databases

GeneIDi24409.
KEGGirno:24409.
UCSCiRGD:2737. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91561 mRNA. Translation: AAC03565.1.
D13211 mRNA. Translation: BAA02498.1.
AF001423 mRNA. Translation: AAB58801.1.
PIRiA43274.
RefSeqiNP_036705.3. NM_012573.3.
UniGeneiRn.9710.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A5SX-ray1.70A401-539[»]
2A5TX-ray2.00B401-539[»]
4JWXX-ray1.50A404-801[»]
4NF4X-ray2.00B402-539[»]
B661-802[»]
4NF5X-ray1.90B402-539[»]
B661-802[»]
4NF6X-ray2.10B402-539[»]
B661-802[»]
4NF8X-ray1.86B402-539[»]
B661-802[»]
5DDNX-ray2.11B402-539[»]
B661-802[»]
5DDXX-ray1.95B402-539[»]
B661-802[»]
5DE4X-ray2.40B402-539[»]
B661-802[»]
5DEXX-ray2.40B402-539[»]
B661-802[»]
5I56X-ray2.28B402-539[»]
B661-800[»]
5I57X-ray1.70B402-539[»]
B661-800[»]
5I58X-ray2.52B402-539[»]
B661-800[»]
5I59X-ray2.25B402-539[»]
B661-800[»]
5JTYX-ray2.72B402-539[»]
B661-800[»]
ProteinModelPortaliQ00959.
SMRiQ00959.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246574. 6 interactors.
DIPiDIP-34031N.
IntActiQ00959. 5 interactors.
MINTiMINT-93314.
STRINGi10116.ENSRNOP00000042235.

Chemistry databases

BindingDBiQ00959.
ChEMBLiCHEMBL310.

Protein family/group databases

TCDBi1.A.10.1.6. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

iPTMnetiQ00959.
PhosphoSitePlusiQ00959.
SwissPalmiQ00959.
UniCarbKBiQ00959.

Proteomic databases

PaxDbiQ00959.
PRIDEiQ00959.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24409.
KEGGirno:24409.
UCSCiRGD:2737. rat.

Organism-specific databases

CTDi2903.
RGDi2737. Grin2a.

Phylogenomic databases

eggNOGiKOG1053. Eukaryota.
ENOG410XNUR. LUCA.
HOGENOMiHOG000113802.
HOVERGENiHBG052635.
InParanoidiQ00959.
KOiK05209.
PhylomeDBiQ00959.

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Miscellaneous databases

EvolutionaryTraceiQ00959.
PROiQ00959.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR018884. NMDAR2_C.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PF10565. NMDAR2_C. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNMDE1_RAT
AccessioniPrimary (citable) accession number: Q00959
Secondary accession number(s): O08948, Q63728
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: November 30, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.