Q61625 · GRID2_MOUSE
- ProteinGlutamate receptor ionotropic, delta-2
- GeneGrid2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1007 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 76 | Essential for dimerization | ||||
Sequence: F |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlutamate receptor ionotropic, delta-2
- Short namesGluD2; GluR delta-2 subunit
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ61625
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Postsynaptic cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 24-566 | Extracellular | ||||
Sequence: DSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVNGLTGDLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFD | ||||||
Transmembrane | 567-587 | Helical | ||||
Sequence: LSLWACIAGTVLLVGLLVYLL | ||||||
Topological domain | 588-635 | Cytoplasmic | ||||
Sequence: NWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMG | ||||||
Transmembrane | 636-656 | Helical | ||||
Sequence: AWWLFALIVISSYTANLAAFL | ||||||
Topological domain | 657-830 | Extracellular | ||||
Sequence: TITRIESSIQSLQDLSKQTDIPYGTVLDSAVYQHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQSGDMDILKHKWWPKNGQCDLYSSVDAKQKGGALDIKS | ||||||
Transmembrane | 831-851 | Helical | ||||
Sequence: LAGVFCILAAGIVLSCLIAVL | ||||||
Topological domain | 852-1007 | Cytoplasmic | ||||
Sequence: ETWWSRRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFAFGSVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI |
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 654 | in Lurcher | ||||
Sequence: A → T | ||||||
Mutagenesis | 920 | Abolishes interaction with SHANK1 and SHANK2. | ||||
Sequence: S → A |
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.
Keywords
- Disease
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MEVFPLLLFLSFCWSRTWDLATA | ||||||
Chain | PRO_0000011565 | 24-1007 | Glutamate receptor ionotropic, delta-2 | |||
Sequence: DSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVNGLTGDLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTDIPYGTVLDSAVYQHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQSGDMDILKHKWWPKNGQCDLYSSVDAKQKGGALDIKSLAGVFCILAAGIVLSCLIAVLETWWSRRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFAFGSVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI | ||||||
Disulfide bond | 83↔355 | |||||
Sequence: CELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSC | ||||||
Disulfide bond | 99↔131 | |||||
Sequence: CTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGC | ||||||
Glycosylation | 293 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 298↔310 | |||||
Sequence: CFRGNHRISSSLC | ||||||
Glycosylation | 426 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 713 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 716 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 883 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 886 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 890 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1006 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q61625 | Cbln1 Q9R171 | 8 | EBI-2794106, EBI-2794140 | |
BINARY | Q61625 | Gopc Q8BH60 | 5 | EBI-2794106, EBI-296357 | |
BINARY | Q61625 | Shank1 D3YZU1 | 3 | EBI-2794106, EBI-2314988 | |
XENO | Q61625 | Shank1 Q9WV48 | 5 | EBI-2794106, EBI-80909 | |
BINARY | Q61625 | Shank2 Q80Z38 | 10 | EBI-2794106, EBI-770338 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 24-345 | Interaction with CBLN1 homotrimer | ||||
Sequence: DSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDR | ||||||
Region | 921-991 | Interaction with AP4M1 | ||||
Sequence: DFRNTHITTTTFIPEQIQTLSRTLSAKAASGFAFGSVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTP | ||||||
Motif | 1005-1007 | PDZ-binding | ||||
Sequence: TSI |
Domain
The PDZ-binding motif mediates interaction with GOPC.
Sequence similarities
Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRID2 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,007
- Mass (Da)113,082
- Last updated1996-11-01 v1
- ChecksumA456166CC782A44B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1B0GRX8 | A0A1B0GRX8_MOUSE | Grid2 | 123 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D13266 EMBL· GenBank· DDBJ | BAA02524.1 EMBL· GenBank· DDBJ | mRNA | ||
BC139823 EMBL· GenBank· DDBJ | AAI39824.1 EMBL· GenBank· DDBJ | mRNA |