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Protein

Glutamate receptor ionotropic, delta-2

Gene

Grid2

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

Functioni

Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad complex.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei76Essential for dimerizationBy similarity1

GO - Molecular functioni

  • extracellular-glutamate-gated ion channel activity Source: InterPro
  • identical protein binding Source: IntAct
  • ionotropic glutamate receptor activity Source: InterPro
  • PDZ domain binding Source: UniProtKB
  • scaffold protein binding Source: RGD

GO - Biological processi

Keywordsi

Molecular functionIon channel, Ligand-gated ion channel, Receptor
Biological processIon transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor ionotropic, delta-2
Short name:
GluD2
Short name:
GluR delta-2 subunit
Gene namesi
Name:Grid2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68368. Grid2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 566ExtracellularSequence analysisAdd BLAST543
Transmembranei567 – 587HelicalSequence analysisAdd BLAST21
Topological domaini588 – 635CytoplasmicSequence analysisAdd BLAST48
Transmembranei636 – 656HelicalSequence analysisAdd BLAST21
Topological domaini657 – 830ExtracellularSequence analysisAdd BLAST174
Transmembranei831 – 851HelicalSequence analysisAdd BLAST21
Topological domaini852 – 1007CytoplasmicSequence analysisAdd BLAST156

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi945S → A: No effect. 1 Publication1
Mutagenesisi952F → A: Loss of interaction with AP4M1. 1 Publication1
Mutagenesisi954F → A: Loss of interaction with AP4M1. 1 Publication1
Mutagenesisi957V → E: Loss of interaction with AP4M1. 1 Publication1
Mutagenesisi965 – 966FR → AA: Loss of interaction with AP4M1. 1 Publication2
Mutagenesisi975 – 976FR → AA: Loss of interaction with AP4M1. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000001156624 – 1007Glutamate receptor ionotropic, delta-2Add BLAST984

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi83 ↔ 355By similarity
Disulfide bondi99 ↔ 131By similarity
Glycosylationi293N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi298 ↔ 310By similarity
Glycosylationi426N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei883PhosphoserineCombined sources1
Modified residuei886PhosphothreonineBy similarity1
Modified residuei890PhosphoserineCombined sources1
Modified residuei1006PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ63226.
PRIDEiQ63226.

PTM databases

iPTMnetiQ63226.
PhosphoSitePlusiQ63226.
UniCarbKBiQ63226.

Expressioni

Tissue specificityi

Expressed at high levels in the cerebellar Purkinje cell layer, almost absent in the forebrain.1 Publication

Interactioni

Subunit structurei

Tetramer; dimer of dimers (By similarity). Interacts with AP4M1 (PubMed:14572453). Interacts with EML2 (PubMed:11829466). Interacts with MAGI2 (via PDZ domains) (PubMed:12589829). Interacts with BECN1, GOPC, GRID2IP, SHANK1 and SHANK2. Interacts with CBLN2, but not with CBLN4 (By similarity). Interacts with CBLN1 (via C1q domain); the interaction is CBLN1-NRX1 complex formation-dependent; CBLN1-binding is calcium-independent; CBLN1 hexamers anchor GRID2 N-terminal domain dimers to monomeric NRXN1 isoform beta; promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-6988699,EBI-6988699

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • PDZ domain binding Source: UniProtKB
  • scaffold protein binding Source: RGD

Protein-protein interaction databases

DIPiDIP-40709N.
IntActiQ63226. 3 interactors.
MINTiMINT-350054.
STRINGi10116.ENSRNOP00000060322.

Structurei

Secondary structure

11007
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi442 – 447Combined sources6
Turni451 – 453Combined sources3
Beta strandi454 – 457Combined sources4
Beta strandi466 – 469Combined sources4
Helixi470 – 482Combined sources13
Beta strandi485 – 490Combined sources6
Turni501 – 503Combined sources3
Helixi507 – 513Combined sources7
Beta strandi518 – 520Combined sources3
Helixi528 – 531Combined sources4
Beta strandi534 – 536Combined sources3
Beta strandi540 – 543Combined sources4
Beta strandi545 – 550Combined sources6
Helixi668 – 672Combined sources5
Beta strandi675 – 677Combined sources3
Helixi686 – 695Combined sources10
Helixi704 – 712Combined sources9
Helixi714 – 717Combined sources4
Beta strandi722 – 724Combined sources3
Helixi725 – 734Combined sources10
Beta strandi738 – 742Combined sources5
Helixi743 – 752Combined sources10
Beta strandi758 – 761Combined sources4
Beta strandi768 – 770Combined sources3
Beta strandi773 – 775Combined sources3
Helixi781 – 793Combined sources13
Helixi796 – 804Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V3TX-ray2.75A/B440-551[»]
A/B664-813[»]
2V3UX-ray1.74A440-551[»]
A664-813[»]
5CC2X-ray2.50A440-551[»]
A664-813[»]
5L2EX-ray4.15A/B/C24-551[»]
A/B/C664-813[»]
ProteinModelPortaliQ63226.
SMRiQ63226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63226.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 345Interaction with CBLN1 homotrimerBy similarityAdd BLAST322
Regioni921 – 991Interaction with AP4M11 PublicationAdd BLAST71

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1005 – 1007PDZ-bindingBy similarity3

Domaini

The PDZ-binding motif mediates interaction with GOPC.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KDI7. Eukaryota.
ENOG410YYDD. LUCA.
HOGENOMiHOG000264260.
HOVERGENiHBG051840.
InParanoidiQ63226.
KOiK05207.
PhylomeDBiQ63226.
TreeFamiTF352434.

Family and domain databases

InterProiView protein in InterPro
IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
PfamiView protein in Pfam
PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
PRINTSiPR00177. NMDARECEPTOR.
SMARTiView protein in SMART
SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q63226-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVFPLLFFL SFWWSRTWDL ATSDSIIHIG AIFDESAKKD DEVFRTAVGD
60 70 80 90 100
LNQNEEILQT EKITFSVTFV DGNNPFQAVQ EACELMNQGI LALVSSIGCT
110 120 130 140 150
SAGSLQSLAD AMHIPHLFIQ RSTAGTPRSG CGLTRSNRND DYTLSVRPPV
160 170 180 190 200
YLNEVILRVV TEYAWQKFII FYDSEYDIRG IQEFLDKVSQ QGMDVALQKV
210 220 230 240 250
ENNINKMITT LFDTMRIEEL NRYRDTLRRA ILVMNPATAK SFISEVVETN
260 270 280 290 300
LVAFDCHWII INEEINDVDV QELVRRSIGR LTIIRQTFPV PQNISQRCFR
310 320 330 340 350
GNHRISSTLC DPKDPFAQNM EISNLYIYDT VLLLANAFHK KLEDRKWHSM
360 370 380 390 400
ASLSCIRKNS KPWQGGRSML ETIKKGGVNG LTGDLEFGEN GGNPNVHFEI
410 420 430 440 450
LGTNYGEELG RGVRKLGCWN PVTGLNGSLT DKKLENNMRG VVLRVVTVLE
460 470 480 490 500
EPFVMVSENV LGKPKKYQGF SIDVLDALSN YLGFNYEIYV APDHKYGSPQ
510 520 530 540 550
EDGTWNGLVG ELVFKRADIG ISALTITPDR ENVVDFTTRY MDYSVGVLLR
560 570 580 590 600
RAEKTVDMFA CLAPFDLSLW ACIAGTVLLV GLLVYLLNWL NPPRLQMGSM
610 620 630 640 650
TSTTLYNSMW FVYGSFVQQG GEVPYTTLAT RMMMGAWWLF ALIVISSYTA
660 670 680 690 700
NLAAFLTITR IESSIQSLQD LSKQTDIPYG TVLDSAVYQH VRMKGLNPFE
710 720 730 740 750
RDSMYSQMWR MINRSNGSEN NVLESQAGIQ KVKYGNYAFV WDAAVLEYVA
760 770 780 790 800
INDPDCSFYT VGNTVADRGY GIALQHGSPY RDVFSQRILE LQQSGDMDIL
810 820 830 840 850
KHKWWPKNGQ CDLYSSVDAK QKGGALDIKS LAGVFCILAA GIVLSCLIAV
860 870 880 890 900
LETWWSRRKG SRVPSKEDDK EIDLEHLHRR VNSLCTDDDS PHKQFSTSSI
910 920 930 940 950
DLTPLDIDTL PTRQALEQIS DFRNTHITTT TFIPEQIQTL SRTLSAKAAS
960 970 980 990 1000
GFTFGSVPEH RTGPFRHRAP NGGFFRSPIK TMSSIPYQPT PTLGLNLGND

PDRGTSI
Length:1,007
Mass (Da):113,259
Last modified:November 14, 2003 - v2
Checksum:i6583C31357C9402C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti109 – 111ADA → GRLT in CAA78937 (PubMed:8422924).Curated3
Sequence conflicti324 – 326NLY → HLC in CAA78937 (PubMed:8422924).Curated3
Sequence conflicti330T → A in CAA78937 (PubMed:8422924).Curated1
Sequence conflicti343E → Q in AAA17829 (Ref. 2) Curated1
Sequence conflicti950S → F in AAA17829 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z17239 mRNA. Translation: CAA78937.1.
U08256 mRNA. Translation: AAA17829.1.
PIRiS28858.
RefSeqiNP_077355.1. NM_024379.1.
UniGeneiRn.10046.

Genome annotation databases

GeneIDi79220.
KEGGirno:79220.
UCSCiRGD:68368. rat.

Similar proteinsi

Entry informationi

Entry nameiGRID2_RAT
AccessioniPrimary (citable) accession number: Q63226
Secondary accession number(s): Q62641
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: November 22, 2017
This is version 145 of the entry and version 2 of the sequence. See 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