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Q61625 (GRID2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. 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, delta-2

Short name=GluD2
Short name=GluR delta-2 subunit
Gene names
Name:Grid2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1007 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with AIP1 and AP4M1 By similarity. Interacts with BECN1, GOPC, GRID2IP, SHANK1 and SHANK2. Interacts with CBLN1 and CBLN2, but not with CBLN4. CBLN1-binding is calcium-independent. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Expressed selectively in cerebellar Purkinje cells where it is localized in dendritic spines. Ref.1 Ref.4

Domain

The PDZ-binding motif mediates interaction with GOPC. Ref.3

Involvement in disease

Defects in Grid2 are the cause of the Lurcher phenotype. Heterozygous animals display a characteristic swaying of the hind quarters and jerky up and down movements following cerebellar Purkinje cell degeneration during postnatal development. Homozygous animals die shortly after birth because of a massive loss of midbrain and hindbrain neurons during late embryogenesis.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRID2 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   DiseaseDisease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein localization

Inferred from direct assay Ref.4. Source: BHF-UCL

cerebellar granule cell differentiation

Inferred from genetic interaction PubMed 20537373. Source: BHF-UCL

heterophilic cell-cell adhesion

Inferred from genetic interaction PubMed 20537373. Source: BHF-UCL

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

ionotropic glutamate receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

prepulse inhibition

Inferred from mutant phenotype PubMed 11488959. Source: MGI

regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 7766857. Source: MGI

regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 10884318. Source: MGI

regulation of neuron projection development

Inferred from mutant phenotype PubMed 7891151. Source: MGI

synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 7766857. Source: MGI

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendritic spine

Inferred from direct assay Ref.4. Source: BHF-UCL

ionotropic glutamate receptor complex

Inferred from direct assay Ref.4. Source: BHF-UCL

membrane

Inferred from direct assay PubMed 15579147. Source: MGI

plasma membrane

Inferred from direct assay Ref.4. Source: BHF-UCL

postsynaptic membrane

Inferred from direct assay Ref.4. Source: BHF-UCL

synapse

Inferred from direct assay Ref.3PubMed 18509461. Source: MGI

   Molecular_functionPDZ domain binding

Inferred from physical interaction Ref.4. Source: BHF-UCL

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ionotropic glutamate receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.3PubMed 20537373. Source: IntAct

scaffold protein binding

Inferred from physical interaction Ref.4. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 1007984Glutamate receptor ionotropic, delta-2
PRO_0000011565

Regions

Topological domain24 – 566543Extracellular Potential
Transmembrane567 – 58721Helical; Potential
Topological domain588 – 63548Cytoplasmic Potential
Transmembrane636 – 65621Helical; Potential
Topological domain657 – 830174Extracellular Potential
Transmembrane831 – 85121Helical; Potential
Topological domain852 – 1007156Cytoplasmic Potential
Region921 – 99171Interaction with AP4M1 By similarity
Motif1005 – 10073PDZ-binding

Amino acid modifications

Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential

Natural variations

Natural variant6541A → T in Lurcher. Ref.9

Experimental info

Mutagenesis9201S → A: Abolishes interaction with SHANK1 and SHANK2. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q61625 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A456166CC782A44B

FASTA1,007113,082
        10         20         30         40         50         60 
MEVFPLLLFL SFCWSRTWDL ATADSIIHIG AIFDESAKKD DEVFRTAVGD LNQNEEILQT 

        70         80         90        100        110        120 
EKITFSVTFV DGNNPFQAVQ EACELMNQGI LALVSSIGCT SAGSLQSLAD AMHIPHLFIQ 

       130        140        150        160        170        180 
RSTAGTPRSG CGLTRSNRND DYTLSVRPPV YLNEVILRVV TEYAWQKFII FYDSEYDIRG 

       190        200        210        220        230        240 
IQEFLDKVSQ QGMDVALQKV ENNINKMITT LFDTMRIEEL NRYRDTLRRA ILVMNPATAK 

       250        260        270        280        290        300 
SFISEVVETN LVAFDCHWII INEEINDVDV QELVRRSIGR LTIIRQTFPV PQNISQRCFR 

       310        320        330        340        350        360 
GNHRISSSLC DPKDPFAQNM EISNLYIYDT VLLLANAFHK KLEDRKWHSM ASLSCIRKNS 

       370        380        390        400        410        420 
KPWQGGRSML ETIKKGGVNG LTGDLEFGEN GGNPNVHFEI LGTNYGEELG RGVRKLGCWN 

       430        440        450        460        470        480 
PVTGLNGSLT DKKLENNMRG VVLRVVTVLE EPFVMVSENV LGKPKKYQGF SIDVLDALSN 

       490        500        510        520        530        540 
YLGFNYEIYV APDHKYGSPQ EDGTWNGLVG ELVFKRADIG ISALTITPDR ENVVDFTTRY 

       550        560        570        580        590        600 
MDYSVGVLLR RAEKTVDMFA CLAPFDLSLW ACIAGTVLLV GLLVYLLNWL NPPRLQMGSM 

       610        620        630        640        650        660 
TSTTLYNSMW FVYGSFVQQG GEVPYTTLAT RMMMGAWWLF ALIVISSYTA NLAAFLTITR 

       670        680        690        700        710        720 
IESSIQSLQD LSKQTDIPYG TVLDSAVYQH VRMKGLNPFE RDSMYSQMWR MINRSNGSEN 

       730        740        750        760        770        780 
NVLESQAGIQ KVKYGNYAFV WDAAVLEYVA INDPDCSFYT VGNTVADRGY GIALQHGSPY 

       790        800        810        820        830        840 
RDVFSQRILE LQQSGDMDIL KHKWWPKNGQ CDLYSSVDAK QKGGALDIKS LAGVFCILAA 

       850        860        870        880        890        900 
GIVLSCLIAV LETWWSRRKG SRVPSKEDDK EIDLEHLHRR VNSLCTDDDS PHKQFSTSSI 

       910        920        930        940        950        960 
DLTPLDIDTL PTRQALEQIS DFRNTHITTT TFIPEQIQTL SRTLSAKAAS GFAFGSVPEH 

       970        980        990       1000 
RTGPFRHRAP NGGFFRSPIK TMSSIPYQPT PTLGLNLGND PDRGTSI 

« Hide

References

« Hide 'large scale' references
[1]"Selective expression of the glutamate receptor channel delta 2 subunit in cerebellar Purkinje cells."
Araki K., Meguro H., Kushiya E., Takayama C., Inoue Y., Mishina M.
Biochem. Biophys. Res. Commun. 197:1267-1276(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: ICR.
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"A novel protein complex linking the delta 2 glutamate receptor and autophagy: implications for neurodegeneration in lurcher mice."
Yue Z., Horton A., Bravin M., DeJager P.L., Selimi F., Heintz N.
Neuron 35:921-933(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GOPC AND BECN1, DOMAIN.
[4]"Direct interaction of GluRdelta2 with Shank scaffold proteins in cerebellar Purkinje cells."
Uemura T., Mori H., Mishina M.
Mol. Cell. Neurosci. 26:330-341(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHANK1 AND SHANK2, MUTAGENESIS OF SER-920, TISSUE SPECIFICITY.
[5]"Binding of glutamate receptor delta2 to its scaffold protein, Delphilin, is regulated by PKA."
Sonoda T., Mochizuki C., Yamashita T., Watanabe-Kaneko K., Miyagi Y., Shigeri Y., Yazama F., Okuda K., Kawamoto S.
Biochem. Biophys. Res. Commun. 350:748-752(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRID2IP.
[6]"Cbln1 is a ligand for an orphan glutamate receptor delta2, a bidirectional synapse organizer."
Matsuda K., Miura E., Miyazaki T., Kakegawa W., Emi K., Narumi S., Fukazawa Y., Ito-Ishida A., Kondo T., Shigemoto R., Watanabe M., Yuzaki M.
Science 328:363-368(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLN1.
[7]"Cbln family proteins promote synapse formation by regulating distinct neurexin signaling pathways in various brain regions."
Matsuda K., Yuzaki M.
Eur. J. Neurosci. 33:1447-1461(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLN1.
[8]"The Cbln family of proteins interact with multiple signaling pathways."
Wei P., Pattarini R., Rong Y., Guo H., Bansal P.K., Kusnoor S.V., Deutch A.Y., Parris J., Morgan J.I.
J. Neurochem. 121:717-729(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLN1 AND CBLN2.
[9]"Neurodegeneration in Lurcher mice caused by mutation in delta2 glutamate receptor gene."
Zuo J., De Jager P.L., Takahashi K.A., Jiang W., Linden D.J., Heintz N.
Nature 388:769-773(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LURCHER THR-654.
Tissue: Purkinje cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13266 mRNA. Translation: BAA02524.1.
BC139823 mRNA. Translation: AAI39824.1.
CCDSCCDS20202.1.
PIRPN0156.
RefSeqNP_032193.1. NM_008167.2.
UniGeneMm.439651.
Mm.447390.

3D structure databases

ProteinModelPortalQ61625.
SMRQ61625. Positions 26-426, 441-809.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200062. 3 interactions.
IntActQ61625. 37 interactions.
MINTMINT-126960.
STRING10090.ENSMUSP00000093536.

Chemistry

BindingDBQ61625.
GuidetoPHARMACOLOGY449.

Protein family/group databases

TCDB1.A.10.1.8. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSiteQ61625.

Proteomic databases

MaxQBQ61625.
PaxDbQ61625.
PRIDEQ61625.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000095852; ENSMUSP00000093536; ENSMUSG00000071424.
GeneID14804.
KEGGmmu:14804.
UCSCuc009cdz.1. mouse.

Organism-specific databases

CTD2895.
MGIMGI:95813. Grid2.

Phylogenomic databases

eggNOGNOG276334.
GeneTreeENSGT00740000115107.
HOGENOMHOG000264260.
HOVERGENHBG051840.
InParanoidA4QPG1.
KOK05207.
OMAHGNYAFV.
OrthoDBEOG7KQ20V.
PhylomeDBQ61625.
TreeFamTF352434.

Gene expression databases

BgeeQ61625.
CleanExMM_GRID2.
GenevestigatorQ61625.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
IPR001638. SBP_bac_3.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 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

ChiTaRSGRID2. mouse.
NextBio286973.
PROQ61625.
SOURCESearch...

Entry information

Entry nameGRID2_MOUSE
AccessionPrimary (citable) accession number: Q61625
Secondary accession number(s): A4QPG1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 135 of the entry and version 1 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