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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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68368. Grid2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 566543ExtracellularSequence analysisAdd
BLAST
Transmembranei567 – 58721HelicalSequence analysisAdd
BLAST
Topological domaini588 – 63548CytoplasmicSequence analysisAdd
BLAST
Transmembranei636 – 65621HelicalSequence analysisAdd
BLAST
Topological domaini657 – 830174ExtracellularSequence analysisAdd
BLAST
Transmembranei831 – 85121HelicalSequence analysisAdd
BLAST
Topological domaini852 – 1007156CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • integral component of membrane Source: UniProtKB-KW
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi945 – 9451S → A: No effect. 1 Publication
Mutagenesisi952 – 9521F → A: Loss of interaction with AP4M1. 1 Publication
Mutagenesisi954 – 9541F → A: Loss of interaction with AP4M1. 1 Publication
Mutagenesisi957 – 9571V → E: Loss of interaction with AP4M1. 1 Publication
Mutagenesisi965 – 9662FR → AA: Loss of interaction with AP4M1. 1 Publication
Mutagenesisi975 – 9762FR → AA: Loss of interaction with AP4M1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 1007984Glutamate receptor ionotropic, delta-2PRO_0000011566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence analysis
Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence analysis
Modified residuei883 – 8831PhosphoserineCombined sources
Modified residuei886 – 8861PhosphothreonineBy similarity
Modified residuei890 – 8901PhosphoserineCombined sources
Modified residuei1006 – 10061PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ63226.

PTM databases

iPTMnetiQ63226.
PhosphoSiteiQ63226.
UniCarbKBiQ63226.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Interacts with AIP1, BECN1, GOPC, GRID2IP, SHANK1 and SHANK2 (By similarity). Interacts with CBLN1 and CBLN2, but not with CBLN4. CBLN1-binding is calcium-independent (By similarity). Interacts with AP4M1. Interacts with EML2.By similarity3 Publications

GO - Molecular functioni

  • PDZ domain binding Source: UniProtKB

Protein-protein interaction databases

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

Structurei

Secondary structure

1
1007
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi442 – 4476Combined sources
Turni451 – 4533Combined sources
Beta strandi454 – 4574Combined sources
Beta strandi466 – 4694Combined sources
Helixi470 – 48213Combined sources
Beta strandi485 – 4906Combined sources
Turni501 – 5033Combined sources
Helixi507 – 5137Combined sources
Beta strandi518 – 5203Combined sources
Helixi528 – 5314Combined sources
Beta strandi534 – 5363Combined sources
Beta strandi540 – 5434Combined sources
Beta strandi545 – 5506Combined sources
Helixi668 – 6725Combined sources
Beta strandi675 – 6773Combined sources
Helixi686 – 69510Combined sources
Helixi704 – 7129Combined sources
Helixi714 – 7174Combined sources
Beta strandi722 – 7243Combined sources
Helixi725 – 73410Combined sources
Beta strandi738 – 7425Combined sources
Helixi743 – 75210Combined sources
Beta strandi758 – 7614Combined sources
Beta strandi768 – 7703Combined sources
Beta strandi773 – 7753Combined sources
Helixi781 – 79313Combined sources
Helixi796 – 8049Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V3TX-ray2.75A/B440-551[»]
A/B664-813[»]
2V3UX-ray1.74A440-551[»]
A664-813[»]
5CC2X-ray2.50A440-551[»]
A664-813[»]
ProteinModelPortaliQ63226.
SMRiQ63226. Positions 440-610, 658-806.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63226.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni921 – 99171Interaction with AP4M1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1005 – 10073PDZ-bindingBy similarity

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

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1113ADA → GRLT in CAA78937 (PubMed:8422924).Curated
Sequence conflicti324 – 3263NLY → HLC in CAA78937 (PubMed:8422924).Curated
Sequence conflicti330 – 3301T → A in CAA78937 (PubMed:8422924).Curated
Sequence conflicti343 – 3431E → Q in AAA17829 (Ref. 2) Curated
Sequence conflicti950 – 9501S → F in AAA17829 (Ref. 2) Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V3TX-ray2.75A/B440-551[»]
A/B664-813[»]
2V3UX-ray1.74A440-551[»]
A664-813[»]
5CC2X-ray2.50A440-551[»]
A664-813[»]
ProteinModelPortaliQ63226.
SMRiQ63226. Positions 440-610, 658-806.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ63226.
PhosphoSiteiQ63226.
UniCarbKBiQ63226.

Proteomic databases

PaxDbiQ63226.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2895.
RGDi68368. Grid2.

Phylogenomic databases

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

Miscellaneous databases

EvolutionaryTraceiQ63226.
PROiQ63226.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The rat delta-1 and delta-2 subunits extend the excitatory amino acid receptor family."
    Lomeli H., Sprengel R., Laurie D., Khr G., Herb A., Seeburg P., Wisden W.
    FEBS Lett. 315:318-322(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Nucleotide sequence of rat glutamate receptor subunit gene delta2."
    Boulter J., Pecht G.
    Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Identification of rat EMAP, a delta-glutamate receptor binding protein."
    Ly C.D., Roche K.W., Lee H.K., Wenthold R.J.
    Biochem. Biophys. Res. Commun. 291:85-90(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EML2.
  4. "Adaptor protein complex-4 (AP-4) is expressed in the central nervous system neurons and interacts with glutamate receptor delta2."
    Yap C.C., Murate M., Kishigami S., Muto Y., Kishida H., Hashikawa T., Yano R.
    Mol. Cell. Neurosci. 24:283-295(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP4M1, MUTAGENESIS OF SER-945; PHE-952; PHE-954; VAL-957; 965-PHE-ARG-966 AND 975-PHE-ARG-976.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883; SER-890 AND SER-1006, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 440-813 IN COMPLEX WITH SERINE.

Entry informationi

Entry nameiGRID2_RAT
AccessioniPrimary (citable) accession number: Q63226
Secondary accession number(s): Q62641
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: June 8, 2016
This is version 136 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.