Gria1
entrez
50592
canonical
uniprot
P19490
canonical
ensembl
ENSRNOG00000045816
resolver
ensembl
ENSRNOG00055029717
resolver
ensembl
ENSRNOG00060022487
resolver
ensembl
ENSRNOG00065006524
resolver
ensp
ENSRNOP00000074119
resolver
ensp
ENSRNOP00000101986
resolver
genesymbol
Gria1
resolver
genesymbol_syn
GluA1
resolver
genesymbol_syn
Glur1
resolver
uniprot_entry
GRIA1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Glutamate-gated receptor activity inhibited by DNQX (6,7-dinitroquinoxaline-2,3-dione). {ECO:0000269|PubMed:2166337}.
uniprot
proteins
amino_acid_sequence
MPYIFAFFCTGFLGAVVGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQLRPELQEALISIIDHYKWQTFVYIYDADRGLSVLQRVLDTAAEKNWQVTAVNILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPARIMQQWRTSDSRDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAATDAQAGGDNSSVQNRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEGRDQTTSDQSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRNSGAGASGGGGSGENGRVVSQDFPKSMQSIPCMSHSSGMPLGATGL
uniprot
proteins
function
FUNCTION: Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (PubMed:2166337, PubMed:2168579). 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 upon entry of monovalent and divalent cations such as sodium and calcium (PubMed:11773314, PubMed:18817736). The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist (PubMed:16793768, PubMed:19265014). In the presence of CACNG2 or CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate (PubMed:16793768, PubMed:19265014). Resensitization is blocked by CNIH2 through interaction with CACNG8 in the CACNG8-containing AMPA receptors complex (By similarity). Calcium (Ca(2+)) permeability depends on subunits composition and, heteromeric channels containing edited GRIA2 subunit are calcium-impermeable (PubMed:1709304). Also permeable to other divalents cations such as strontium(2+) and magnesium(2+) and monovalent cations such as potassium(1+) and lithium(1+) (PubMed:11773314). {ECO:0000250|UniProtKB:P42261, ECO:0000269|PubMed:11773314, ECO:0000269|PubMed:16793768, ECO:0000269|PubMed:1709304, ECO:0000269|PubMed:18817736, ECO:0000269|PubMed:19265014, ECO:0000269|PubMed:2166337, ECO:0000269|PubMed:2168579}.
uniprot
proteins
mass_dalton
101579
uniprot
proteins
mutagenesis
MUTAGEN 645; /note="S->A: No effect on phosphorylation by CaMK2."; /evidence="ECO:0000269|PubMed:9405465"; MUTAGEN 849; /note="S->A: Abolishes phosphorylation by CaMK2."; /evidence="ECO:0000269|PubMed:9405465"; MUTAGEN 855; /note="R->A: Decreases binding efficiency to PRKG2."; MUTAGEN 855; /note="R->E: Abolishes binding to PRKG2."; /evidence="ECO:0000269|PubMed:18031684"; MUTAGEN 863; /note="S->A: Decreases synaptic insertion during chemical-induced long term potentiation."; /evidence="ECO:0000269|PubMed:18031684"; MUTAGEN 905; /note="T->A: Loss of interaction with DLG1."; /evidence="ECO:0000269|PubMed:12070168"; MUTAGEN 907; /note="L->A: Loss of interaction with DLG1."; /evidence="ECO:0000269|PubMed:12070168
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-645 (PubMed:7877986). Phosphorylated at Ser-710 by PKC (PubMed:8848293). Phosphorylated at Ser-849 by PKC, PKA and CAMK2 (PubMed:9405465). Phosphorylated at Ser-863 by PKC, PKA and PRKG2 (PubMed:18031684, PubMed:9405465). Phosphorylation of Ser-863 is reduced by induction of long-term depression and increased by induction of long-term potentiation (By similarity). {ECO:0000250|UniProtKB:P23818, ECO:0000269|PubMed:18031684, ECO:0000269|PubMed:7877986, ECO:0000269|PubMed:8848293, ECO:0000269|PubMed:9405465}.; PTM: Palmitoylated. Depalmitoylated by CPT1C and upon L-glutamate stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-603, which leads to Golgi retention and decreased cell surface expression (By similarity). In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis (By similarity). {ECO:0000250|UniProtKB:P23818, ECO:0000250|UniProtKB:P42261}.
uniprot
proteins
protein_family
GRIA1 subfamily
uniprot
proteins
protein_family
Glutamate-gated ion channel (TC 1.A.10.1) family
uniprot
proteins
pubmed
11773314
uniprot
proteins
pubmed
12070168
uniprot
proteins
pubmed
15456832
uniprot
proteins
pubmed
16630835
uniprot
proteins
pubmed
16793768
uniprot
proteins
pubmed
1699275
uniprot
proteins
pubmed
17069616
uniprot
proteins
pubmed
1709304
uniprot
proteins
pubmed
18031684
uniprot
proteins
pubmed
18817736
uniprot
proteins
pubmed
19234459
uniprot
proteins
pubmed
19265014
uniprot
proteins
pubmed
20805473
uniprot
proteins
pubmed
21639859
uniprot
proteins
pubmed
2166337
uniprot
proteins
pubmed
2168579
uniprot
proteins
pubmed
2480522
uniprot
proteins
pubmed
7877986
uniprot
proteins
pubmed
8848293
uniprot
proteins
pubmed
9405465
uniprot
proteins
pubmed
9677374
uniprot
proteins
sequence_length
907
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23818}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15456832}; Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23818}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:P23818}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P23818}. Early endosome membrane {ECO:0000269|PubMed:15456832}; Multi-pass membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:15456832}; Multi-pass membrane protein {ECO:0000305}. Presynapse {ECO:0000250|UniProtKB:P23818}. Synapse {ECO:0000250|UniProtKB:P23818}. Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression (PubMed:19265014). Colocalizes with PDLIM4 in early endosomes (PubMed:15456832). Displays a somatodendritic localization and is excluded from axons in neurons (By similarity). Localized to cone photoreceptor pedicles (By similarity). {ECO:0000250|UniProtKB:P23818, ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:19265014}.
uniprot
proteins
transmembrane_region
TRANSMEM 537..557; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 610..630; /note="Helical"; /evidence="ECO:0000250"; TRANSMEM 806..826; /note="Helical; Name=M4"; /evidence="ECO:0000250
uniprot
proteins