GRIA1_MOUSE
ID GRIA1_MOUSE Reviewed; 907 AA.
AC P23818;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Glutamate receptor 1;
DE Short=GluR-1;
DE AltName: Full=AMPA-selective glutamate receptor 1;
DE AltName: Full=GluR-A;
DE AltName: Full=GluR-K1;
DE AltName: Full=Glutamate receptor ionotropic, AMPA 1;
DE Short=GluA1;
DE Flags: Precursor;
GN Name=Gria1; Synonyms=Glur1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1699805; DOI=10.1016/0014-5793(90)80452-o;
RA Sakimura K., Bujo H., Kushiya E., Araki K., Yamazaki M., Yamazaki M.,
RA Meguro H., Warashina A., Numa S., Mishina M.;
RT "Functional expression from cloned cDNAs of glutamate receptor species
RT responsive to kainate and quisqualate.";
RL FEBS Lett. 272:73-80(1990).
RN [2]
RP INTERACTION WITH HIP1.
RX PubMed=12839988; DOI=10.1093/emboj/cdg334;
RA Metzler M., Li B., Gan L., Georgiou J., Gutekunst C.A., Wang Y., Torre E.,
RA Devon R.S., Oh R., Legendre-Guillemin V., Rich M., Alvarez C.,
RA Gertsenstein M., McPherson P.S., Nagy A., Wang Y.T., Roder J.C.,
RA Raymond L.A., Hayden M.R.;
RT "Disruption of the endocytic protein HIP1 results in neurological deficits
RT and decreased AMPA receptor trafficking.";
RL EMBO J. 22:3254-3266(2003).
RN [3]
RP PALMITOYLATION AT CYS-603 AND CYS-829.
RX PubMed=16129400; DOI=10.1016/j.neuron.2005.06.035;
RA Hayashi T., Rumbaugh G., Huganir R.L.;
RT "Differential regulation of AMPA receptor subunit trafficking by
RT palmitoylation of two distinct sites.";
RL Neuron 47:709-723(2005).
RN [4]
RP INTERACTION WITH RASGRF2.
RX PubMed=16407208; DOI=10.1074/jbc.m512060200;
RA Tian X., Feig L.A.;
RT "Age-dependent participation of Ras-GRF proteins in coupling calcium-
RT permeable AMPA glutamate receptors to Ras/Erk signaling in cortical
RT neurons.";
RL J. Biol. Chem. 281:7578-7582(2006).
RN [5]
RP INTERACTION WITH SHANK3, AND MUTAGENESIS OF 905-THR--LEU-907.
RX PubMed=16606358; DOI=10.1111/j.1471-4159.2006.03831.x;
RA Uchino S., Wada H., Honda S., Nakamura Y., Ondo Y., Uchiyama T.,
RA Tsutsumi M., Suzuki E., Hirasawa T., Kohsaka S.;
RT "Direct interaction of post-synaptic density-95/Dlg/ZO-1 domain-containing
RT synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-5-methyl-4-
RT isoxazole propionic acid receptor.";
RL J. Neurochem. 97:1203-1214(2006).
RN [6]
RP INTERACTION WITH CACNG3, AND SUBCELLULAR LOCATION.
RX PubMed=18341993; DOI=10.1016/j.neuron.2008.02.012;
RA Matsuda S., Miura E., Matsuda K., Kakegawa W., Kohda K., Watanabe M.,
RA Yuzaki M.;
RT "Accumulation of AMPA receptors in autophagosomes in neuronal axons lacking
RT adaptor protein AP-4.";
RL Neuron 57:730-745(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH SYNDIG1 AND GRIA2.
RX PubMed=20152115; DOI=10.1016/j.neuron.2009.12.021;
RA Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B., Ishimaru T.,
RA Trimmer J.S., Mohapatra D.P., Diaz E.;
RT "SynDIG1: an activity-regulated, AMPA- receptor-interacting transmembrane
RT protein that regulates excitatory synapse development.";
RL Neuron 65:80-93(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21172611; DOI=10.1016/j.neuron.2010.11.026;
RA Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H.,
RA Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.;
RT "Hippocampal AMPA receptor gating controlled by both TARP and cornichon
RT proteins.";
RL Neuron 68:1082-1096(2010).
RN [10]
RP PHOSPHORYLATION AT SER-863.
RX PubMed=23676497; DOI=10.1172/jci65401;
RA Marcello E., Saraceno C., Musardo S., Vara H., de la Fuente A.G.,
RA Pelucchi S., Di Marino D., Borroni B., Tramontano A., Perez-Otano I.,
RA Padovani A., Giustetto M., Gardoni F., Di Luca M.;
RT "Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's
RT disease.";
RL J. Clin. Invest. 123:2523-2538(2013).
RN [11]
RP INTERACTION WITH SNX27.
RX PubMed=23524343; DOI=10.1038/nm.3117;
RA Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y., Loo L.S., Cai L.,
RA Thompson R.C., Yang B., Chen Y., Johnson P.F., Wu C., Bu G., Mobley W.C.,
RA Zhang D., Gage F.H., Ranscht B., Zhang Y.W., Lipton S.A., Hong W., Xu H.;
RT "Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by
RT modulating glutamate receptor recycling in Down's syndrome.";
RL Nat. Med. 19:473-480(2013).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28334377; DOI=10.1167/iovs.16-20745;
RA Neuille M., Cao Y., Caplette R., Guerrero-Given D., Thomas C., Kamasawa N.,
RA Sahel J.A., Hamel C.P., Audo I., Picaud S., Martemyanov K.A., Zeitz C.;
RT "LRIT3 Differentially Affects Connectivity and Synaptic Transmission of
RT Cones to ON- and OFF-Bipolar Cells.";
RL Invest. Ophthalmol. Vis. Sci. 58:1768-1778(2017).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=28642476; DOI=10.1038/s41598-017-04355-8;
RA Vigil F.A., Mizuno K., Lucchesi W., Valls-Comamala V., Giese K.P.;
RT "Prevention of long-term memory loss after retrieval by an endogenous
RT CaMKII inhibitor.";
RL Sci. Rep. 7:4040-4040(2017).
RN [14]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31651360; DOI=10.1186/s40478-019-0812-5;
RA Xiao S., McKeever P.M., Lau A., Robertson J.;
RT "Synaptic localization of C9orf72 regulates post-synaptic glutamate
RT receptor 1 levels.";
RL Acta Neuropathol. Commun. 7:161-161(2019).
CC -!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an
CC excitatory neurotransmitter at many synapses in the central nervous
CC system. Binding of the excitatory neurotransmitter L-glutamate induces
CC a conformation change, leading to the opening of the cation channel,
CC and thereby converts the chemical signal to an electrical impulse. The
CC receptor then desensitizes rapidly and enters a transient inactive
CC state, characterized by the presence of bound agonist. In the presence
CC of CACNG4 or CACNG7 or CACNG8, shows resensitization which is
CC characterized by a delayed accumulation of current flux upon continued
CC application of glutamate.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits (By similarity). Tetramers may be formed by the
CC dimerization of dimers (By similarity). Found in a complex with GRIA2,
CC GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and
CC CACNG8 (By similarity). Interacts with HIP1 and RASGRF2
CC (PubMed:12839988, PubMed:16407208). Interacts with SYNDIG1 and GRIA2
CC (PubMed:20152115). Interacts with DLG1 (via C-terminus). Interacts with
CC LRFN1. Interacts with PRKG2. Interacts with CNIH2 and CACNG2. Interacts
CC with CACNG5. Interacts (via C-terminus) with PDLIM4 (via LIM domain);
CC this interaction as well as the interaction of PDLIM4 with alpha-
CC actinin is required for their colocalization in early endosomes. Found
CC in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3,
CC CACNG4, CACNG5, CACNG7 and CACNG8 (By similarity). Interacts with SNX27
CC (via PDZ domain); the interaction is required for recycling to the
CC plasma membrane when endocytosed and prevent degradation in lysosomes
CC (PubMed:23524343). Interacts (via PDZ-binding motif) with SHANK3 (via
CC PDZ domain) (PubMed:16606358). Interacts with CACNG3; associates GRIA1
CC with the adapter protein complex 4 (AP-4) to target GRIA1 to the
CC somatodendritic compartment of neurons (PubMed:18341993).
CC {ECO:0000250|UniProtKB:P19490, ECO:0000250|UniProtKB:P42261,
CC ECO:0000269|PubMed:12839988, ECO:0000269|PubMed:16407208,
CC ECO:0000269|PubMed:16606358, ECO:0000269|PubMed:18341993,
CC ECO:0000269|PubMed:20152115, ECO:0000269|PubMed:23524343}.
CC -!- INTERACTION:
CC P23818; O88602: Cacng2; NbExp=2; IntAct=EBI-445486, EBI-770326;
CC P23818; P23819: Gria2; NbExp=4; IntAct=EBI-445486, EBI-77538;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21172611};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21172611}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P19490}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:21172611, ECO:0000269|PubMed:28334377,
CC ECO:0000269|PubMed:31651360}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21172611}. Postsynaptic density membrane
CC {ECO:0000269|PubMed:21172611}; Multi-pass membrane protein
CC {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:21172611}.
CC Cell projection, dendritic spine {ECO:0000269|PubMed:21172611}. Early
CC endosome membrane {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P19490}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P19490}. Presynapse
CC {ECO:0000269|PubMed:31651360}. Synapse {ECO:0000269|PubMed:28642476}.
CC Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface
CC expression. Colocalizes with PDLIM4 in early endosomes. Displays a
CC somatodendritic localization and is excluded from axons in neurons
CC (PubMed:18341993). Localized to cone photoreceptor pedicles
CC (PubMed:28334377). {ECO:0000250|UniProtKB:P19490,
CC ECO:0000269|PubMed:18341993, ECO:0000269|PubMed:28334377}.
CC -!- TISSUE SPECIFICITY: Expressed in the outer plexiform layer of the
CC retina of the eye (at protein level) (PubMed:28334377). Expressed in
CC the forebrain and hippocampus (at protein level) (PubMed:31651360).
CC {ECO:0000269|PubMed:28334377, ECO:0000269|PubMed:31651360}.
CC -!- DOMAIN: The M4 transmembrane segment mediates tetramerization and is
CC required for cell surface expression. {ECO:0000250}.
CC -!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation.
CC ZDHHC3/GODZ specifically palmitoylates Cys-603, which leads to Golgi
CC retention and decreased cell surface expression. In contrast, Cys-829
CC palmitoylation does not affect cell surface expression but regulates
CC stimulation-dependent endocytosis. {ECO:0000269|PubMed:16129400}.
CC -!- PTM: Phosphorylated at Ser-645. Phosphorylated at Ser-710 by PKC.
CC Phosphorylated at Ser-849 by PKC, PKA and CAMK2. Phosphorylated at Ser-
CC 863 by PKC, PKA and PRKG2 (By similarity). Phosphorylation of Ser-863
CC is reduced by induction of long-term depression and increased by
CC induction of long-term potentiation (PubMed:23676497).
CC {ECO:0000250|UniProtKB:P19490, ECO:0000269|PubMed:23676497}.
CC -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
CC variety of receptors that are named according to their selective
CC agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIA1 subfamily. {ECO:0000305}.
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DR EMBL; X57497; CAA40734.1; -; mRNA.
DR CCDS; CCDS48800.1; -.
DR PIR; S12874; S12874.
DR RefSeq; NP_001106796.1; NM_001113325.2.
DR PDB; 7LDD; EM; 3.40 A; A/C=1-907.
DR PDB; 7LDE; EM; 3.90 A; A/C=1-907.
DR PDBsum; 7LDD; -.
DR PDBsum; 7LDE; -.
DR AlphaFoldDB; P23818; -.
DR SMR; P23818; -.
DR BioGRID; 200058; 21.
DR DIP; DIP-31970N; -.
DR IntAct; P23818; 12.
DR MINT; P23818; -.
DR STRING; 10090.ENSMUSP00000044494; -.
DR BindingDB; P23818; -.
DR ChEMBL; CHEMBL3502; -.
DR GlyConnect; 2341; 4 N-Linked glycans (3 sites).
DR GlyGen; P23818; 6 sites, 4 N-linked glycans (3 sites).
DR iPTMnet; P23818; -.
DR PhosphoSitePlus; P23818; -.
DR SwissPalm; P23818; -.
DR MaxQB; P23818; -.
DR PaxDb; P23818; -.
DR PRIDE; P23818; -.
DR ProteomicsDB; 271017; -.
DR ABCD; P23818; 1 sequenced antibody.
DR Antibodypedia; 28276; 1038 antibodies from 46 providers.
DR DNASU; 14799; -.
DR Ensembl; ENSMUST00000036315; ENSMUSP00000044494; ENSMUSG00000020524.
DR GeneID; 14799; -.
DR KEGG; mmu:14799; -.
DR UCSC; uc007izs.3; mouse.
DR CTD; 2890; -.
DR MGI; MGI:95808; Gria1.
DR VEuPathDB; HostDB:ENSMUSG00000020524; -.
DR eggNOG; KOG1054; Eukaryota.
DR GeneTree; ENSGT00940000157342; -.
DR InParanoid; P23818; -.
DR PhylomeDB; P23818; -.
DR TreeFam; TF315232; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-399710; Activation of AMPA receptors.
DR Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 14799; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Gria1; mouse.
DR PRO; PR:P23818; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P23818; protein.
DR Bgee; ENSMUSG00000020524; Expressed in lateral septal nucleus and 133 other tissues.
DR ExpressionAtlas; P23818; baseline and differential.
DR Genevisible; P23818; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0044308; C:axonal spine; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; IDA:BHF-UCL.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0032591; C:dendritic spine membrane; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0044309; C:neuron spine; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
DR GO; GO:0099544; C:perisynaptic space; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0098793; C:presynapse; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; IDA:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISO:MGI.
DR GO; GO:0035254; F:glutamate receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019865; F:immunoglobulin binding; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IMP:SynGO.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0051018; F:protein kinase A binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0071242; P:cellular response to ammonium ion; IDA:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR GO; GO:0060292; P:long-term synaptic depression; IGI:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0045838; P:positive regulation of membrane potential; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; IMP:UniProtKB.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IMP:SynGO.
DR GO; GO:0001919; P:regulation of receptor recycling; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; ISO:MGI.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Disulfide bond;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..907
FT /note="Glutamate receptor 1"
FT /id="PRO_0000011530"
FT TOPO_DOM 19..536
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 558..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 585..600
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 601..603
FT /evidence="ECO:0000250"
FT TOPO_DOM 604..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 631..805
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 806..826
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 827..907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 857..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 904..907
FT /note="PDZ-binding"
FT BINDING 464
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 492..494
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 668..669
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19490"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19490"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19490"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23676497"
FT LIPID 603
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:16129400"
FT LIPID 829
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:16129400"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..323
FT /evidence="ECO:0000250"
FT DISULFID 732..787
FT /evidence="ECO:0000250"
FT MUTAGEN 905..907
FT /note="TGL->AGA: Almost abolishes interaction with SHANK3."
FT /evidence="ECO:0000269|PubMed:16606358"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 51..61
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 151..155
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 261..276
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 289..309
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 415..422
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 438..450
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 537..557
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 588..598
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 610..642
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 650..655
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 658..667
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 668..674
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 679..689
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 700..710
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 712..719
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 720..728
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 733..738
FT /evidence="ECO:0007829|PDB:7LDD"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 758..769
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 773..781
FT /evidence="ECO:0007829|PDB:7LDD"
FT TURN 782..784
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 804..806
FT /evidence="ECO:0007829|PDB:7LDD"
FT HELIX 807..829
FT /evidence="ECO:0007829|PDB:7LDD"
SQ SEQUENCE 907 AA; 101569 MW; F0FF7031DADD7CEB CRC64;
MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID
IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ
FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT
TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL
NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDARDHTR VDWKRPKYTS ALTYDGVKVM
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR
RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV
MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE
LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW
MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA
YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES
TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRGPV NLAVLKLSEQ GVLDKLKSKW
WYDKGECGSK DSGSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK
GFCLIPQQSI NEAIRTSTLP RNSGAGASGG SGSGENGRVV SQDFPKSMQS IPCMSHSSGM
PLGATGL
