UniProt functional annotation for Q63226



	UniProt functional annotation for Q63226

UniProt code: Q63226.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

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. {ECO:0000250|UniProtKB:O43424}.

Subunit: 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). {ECO:0000250|UniProtKB:O43424, ECO:0000250|UniProtKB:Q61625, ECO:0000269|PubMed:11829466, ECO:0000269|PubMed:12589829, ECO:0000269|PubMed:14572453}.

Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.

Tissue specificity: Expressed at high levels in the cerebellar Purkinje cell layer, almost absent in the forebrain. {ECO:0000269|PubMed:8422924}.

Domain: The PDZ-binding motif mediates interaction with GOPC. {ECO:0000250}.

Similarity: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRID2 subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



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. {ECO:0000250\|UniProtKB:O43424}.


Subunit:		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). {ECO:0000250\|UniProtKB:O43424, ECO:0000250\|UniProtKB:Q61625, ECO:0000269\|PubMed:11829466, ECO:0000269\|PubMed:12589829, ECO:0000269\|PubMed:14572453}.
Subcellular location:		Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Tissue specificity:		Expressed at high levels in the cerebellar Purkinje cell layer, almost absent in the forebrain. {ECO:0000269\|PubMed:8422924}.
Domain:		The PDZ-binding motif mediates interaction with GOPC. {ECO:0000250}.
Similarity:		Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRID2 subfamily. {ECO:0000305}.