Q61625 · GRID2_MOUSE

  • Protein
    Glutamate receptor ionotropic, delta-2
  • Gene
    Grid2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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. 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.

Features

Showing features for site.

110071002003004005006007008009001,000
TypeIDPosition(s)Description
Site76Essential for dimerization

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentdendritic spine
Cellular Componentglutamatergic synapse
Cellular Componentionotropic glutamate receptor complex
Cellular Componentmembrane
Cellular Componentparallel fiber to Purkinje cell synapse
Cellular Componentplasma membrane
Cellular Componentpostsynaptic density membrane
Cellular Componentpostsynaptic membrane
Cellular Componentsomatodendritic compartment
Cellular Componentsynapse
Molecular Functionglutamate receptor activity
Molecular Functionidentical protein binding
Molecular FunctionPDZ domain binding
Molecular Functionscaffold protein binding
Molecular Functiontransmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential
Biological Processcerebellar granule cell differentiation
Biological Processexcitatory postsynaptic potential
Biological Processexcitatory synapse assembly
Biological Processheterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
Biological Processmodulation of chemical synaptic transmission
Biological Processpositive regulation of long-term synaptic depression
Biological Processpositive regulation of synapse assembly
Biological Processprepulse inhibition
Biological Processprotein localization
Biological Processregulation of neuron apoptotic process
Biological Processregulation of neuron projection development
Biological Processregulation of postsynaptic density assembly
Biological Processregulation of postsynaptic membrane neurotransmitter receptor levels
Biological Processregulation of presynapse assembly
Biological Processsynaptic transmission, glutamatergic

Keywords

Protein family/group databases

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

Names & Taxonomy

Protein names

  • Recommended name
    Glutamate receptor ionotropic, delta-2
  • Short names
    GluD2; GluR delta-2 subunit

Gene names

    • Name
      Grid2

Organism names

  • Taxonomic identifier
  • Strain
    • ICR
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q61625
  • Secondary accessions
    • A4QPG1

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain24-566Extracellular
Transmembrane567-587Helical
Topological domain588-635Cytoplasmic
Transmembrane636-656Helical
Topological domain657-830Extracellular
Transmembrane831-851Helical
Topological domain852-1007Cytoplasmic

Keywords

Phenotypes & Variants

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

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variant654in Lurcher
Mutagenesis920Abolishes interaction with SHANK1 and SHANK2.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 38 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-23
ChainPRO_000001156524-1007Glutamate receptor ionotropic, delta-2
Disulfide bond83↔355
Disulfide bond99↔131
Glycosylation293N-linked (GlcNAc...) asparagine
Disulfide bond298↔310
Glycosylation426N-linked (GlcNAc...) asparagine
Glycosylation713N-linked (GlcNAc...) asparagine
Glycosylation716N-linked (GlcNAc...) asparagine
Modified residue883Phosphoserine
Modified residue886Phosphothreonine
Modified residue890Phosphoserine
Modified residue1006Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

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

Gene expression databases

Interaction

Subunit

Tetramer; dimer of dimers (By similarity).
Interacts with EML2, MAGI2 (via PDZ domains) and AP4M1 (By similarity).
Interacts with BECN1, GOPC, GRID2IP, SHANK1 and SHANK2 (PubMed:12372286, PubMed:15207857, PubMed:17027646).
Interacts with CBLN2, but not with CBLN4 (PubMed:22220752).
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 (PubMed:20395510, PubMed:21410790, PubMed:22220752, PubMed:29782851).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, motif.

TypeIDPosition(s)Description
Region24-345Interaction with CBLN1 homotrimer
Region921-991Interaction with AP4M1
Motif1005-1007PDZ-binding

Domain

The PDZ-binding motif mediates interaction with GOPC.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,007
  • Mass (Da)
    113,082
  • Last updated
    1996-11-01 v1
  • Checksum
    A456166CC782A44B
MEVFPLLLFLSFCWSRTWDLATADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVNGLTGDLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTDIPYGTVLDSAVYQHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQSGDMDILKHKWWPKNGQCDLYSSVDAKQKGGALDIKSLAGVFCILAAGIVLSCLIAVLETWWSRRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFAFGSVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1B0GRX8A0A1B0GRX8_MOUSEGrid2123

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D13266
EMBL· GenBank· DDBJ
BAA02524.1
EMBL· GenBank· DDBJ
mRNA
BC139823
EMBL· GenBank· DDBJ
AAI39824.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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