NP_113796.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Related Accession #
NCBI Official Full Name
glutamate receptor 1
NCBI Official Synonym Full Names
glutamate receptor, ionotropic, AMPA 1
NCBI Protein Information
glutamate receptor 1; GluR1; gluR-1; gluR-K1; glutamate receptor A; glutamate receptor subunit GluR1; AMPA-selective glutamate receptor 1; glutamate receptor, ionotropic, AMPA1 (alpha 1)
UniProt Protein Name
Glutamate receptor 1
UniProt Synonym Protein Names
AMPA-selective glutamate receptor 1; GluR-A; GluR-K1; Glutamate receptor ionotropic, AMPA 1
UniProt Synonym Gene Names
UniProt Entry Name
GRIA1_RAT
NCBI Summary for GRIA1
mouse homolog may play a role in regulation of neuronal synaptic plasticity and conditioned reinforcement learning [RGD, Feb 2006]
UniProt Comments for GRIA1
Function: Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. Ref.12 Ref.17
Subunit structure: Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with DLG1 via its C-terminus. Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with HIP1, RASGRF2, SYNDIG1 and LRFN1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes. Interacts (via PDZ-binding motif) with SHANK3 (via PDZ domain).
Subcellular location: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density
By similarity. Cell projection › dendrite
By similarity. Cell projection › dendritic spine
By similarity. Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression. Ref.11 Ref.12 Ref.17
Tissue specificity: Detected in cerebellum (at protein level). Ref.11
Domain: The M4 transmembrane segment mediates tetramerization and is required for cell surface expression
By similarity.
Post-translational modification: Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-603 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis
By similarity.
Polymorphism: Both variants Ser-710 and Thr-710 are phosphorylated at this position.
Miscellaneous: The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
Sequence similarities: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA1 subfamily. [View classification]
Product References and Citations for anti-GRIA1 antibody
• Hollmann M, Heinemann S (1994) Cloned glutamate receptors. Annu Rev Neurosci 17:31-108. • Keinänen K, Wisden W, Sommer B, Werner P, Herb A, Verdoorn TA, Sakmann B, Seeburg PH (1990) A family of AMPA-selective glutamate receptors. Science 249:556-560. • Mammen AL, Kameyama K, Roche KW, Huganir RL (1999) Phosphorylation of the a-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II. J Biol Chem 272:32528-32533. • McGlade-McCulloh E, Yamamoto H, Tan S-E, Brickey DA, Soderling TR (1993) Phosphorylation and regulation of glutamate receptors by calcium/calmodulin-dependent protein kinase II. Nature (London) 362:640-642. • Roche KW, O'Brien RJ, Mammen AL, Bernhardt J, Huganir RL (1996) Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. Neuron 16:1179-1188.
Research Articles on GRIA1
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Pathways associated with anti-GRIA1 antibody
Diseases associated with anti-GRIA1 antibody
Organs/Tissues associated with anti-GRIA1 antibody
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