GRIA1_RAT
ID GRIA1_RAT Reviewed; 907 AA.
AC P19490;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 212.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
RC TISSUE=Forebrain;
RX PubMed=2480522; DOI=10.1038/342643a0;
RA Hollmann M., O'Shea-Greenfield A., Rogers S.W., Heinemann S.F.;
RT "Cloning by functional expression of a member of the glutamate receptor
RT family.";
RL Nature 342:643-648(1989).
RN [2]
RP SEQUENCE REVISION.
RA Hartley M.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
RC TISSUE=Brain;
RX PubMed=2166337; DOI=10.1126/science.2166337;
RA Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A.,
RA Sakmann B., Seeburg P.H.;
RT "A family of AMPA-selective glutamate receptors.";
RL Science 249:556-560(1990).
RN [4]
RP SEQUENCE REVISION TO 67; 248; 698; 710; 789 AND 893.
RA Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A.,
RA Sakmann B., Seeburg P.H.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
RX PubMed=2168579; DOI=10.1126/science.2168579;
RA Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S.,
RA Maron C., Heinemann S.F.;
RT "Molecular cloning and functional expression of glutamate receptor subunit
RT genes.";
RL Science 249:1033-1037(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), AND VARIANT THR-710.
RC TISSUE=Brain;
RX PubMed=1699275; DOI=10.1126/science.1699275;
RA Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A.,
RA Koehler M., Takagi T., Sakmann B., Seeburg P.H.;
RT "Flip and flop: a cell-specific functional switch in glutamate-operated
RT channels of the CNS.";
RL Science 249:1580-1585(1990).
RN [7]
RP PHOSPHORYLATION AT SER-645.
RX PubMed=7877986; DOI=10.1073/pnas.92.5.1376;
RA Yakel J.L., Vissavajjhala P., Derkach V.A., Brickey D.A., Soderling T.R.;
RT "Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory
RT phosphorylation site in non-N-methyl-D-aspartate glutamate receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1376-1380(1995).
RN [8]
RP VARIANT THR-710, AND PHOSPHORYLATION AT SER-710.
RX PubMed=8848293; DOI=10.1016/0168-0102(95)00977-9;
RA Nakazawa K., Tadakuma T., Nokihara K., Ito M.;
RT "Antibody specific for phosphorylated AMPA-type glutamate receptors at
RT GluR2 Ser-696.";
RL Neurosci. Res. 24:75-86(1995).
RN [9]
RP PHOSPHORYLATION AT SER-849 AND SER-863, AND MUTAGENESIS OF SER-645 AND
RP SER-849.
RX PubMed=9405465; DOI=10.1074/jbc.272.51.32528;
RA Mammen A.L., Kameyama K., Roche K.W., Huganir R.L.;
RT "Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic
RT acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II.";
RL J. Biol. Chem. 272:32528-32533(1997).
RN [10]
RP INTERACTION WITH DLG1.
RX PubMed=9677374; DOI=10.1074/jbc.273.31.19518;
RA Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.;
RT "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-
RT propionic acid receptor GluR1 subunit.";
RL J. Biol. Chem. 273:19518-19524(1998).
RN [11]
RP INTERACTION WITH DLG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF THR-905 AND LEU-907.
RX PubMed=12070168; DOI=10.1074/jbc.m204354200;
RA Cai C., Coleman S.K., Niemi K., Keinaenen K.;
RT "Selective binding of synapse-associated protein 97 to GluR-A alpha-amino-
RT 5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by
RT a novel sequence motif.";
RL J. Biol. Chem. 277:31484-31490(2002).
RN [12]
RP INTERACTION WITH PDLIM4, AND SUBCELLULAR LOCATION.
RX PubMed=15456832; DOI=10.1523/jneurosci.2100-04.2004;
RA Schulz T.W., Nakagawa T., Licznerski P., Pawlak V., Kolleker A., Rozov A.,
RA Kim J., Dittgen T., Koehr G., Sheng M., Seeburg P.H., Osten P.;
RT "Actin/alpha-actinin-dependent transport of AMPA receptors in dendritic
RT spines: role of the PDZ-LIM protein RIL.";
RL J. Neurosci. 24:8584-8594(2004).
RN [13]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH CACNG2.
RX PubMed=16793768; DOI=10.1074/jbc.m600679200;
RA Bedoukian M.A., Weeks A.M., Partin K.M.;
RT "Different domains of the AMPA receptor direct stargazin-mediated
RT trafficking and stargazin-mediated modulation of kinetics.";
RL J. Biol. Chem. 281:23908-23921(2006).
RN [14]
RP INTERACTION WITH LRFN1.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [15]
RP INTERACTION WITH PRKG2, PHOSPHORYLATION AT SER-863, AND MUTAGENESIS OF
RP ARG-855 AND SER-863.
RX PubMed=18031684; DOI=10.1016/j.neuron.2007.09.016;
RA Serulle Y., Zhang S., Ninan I., Puzzo D., McCarthy M., Khatri L.,
RA Arancio O., Ziff E.B.;
RT "A GluR1-cGKII interaction regulates AMPA receptor trafficking.";
RL Neuron 56:670-688(2007).
RN [16]
RP INTERACTION WITH CACNG5.
RX PubMed=18817736; DOI=10.1016/j.neuron.2008.07.034;
RA Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.;
RT "AMPA receptor subunit-specific regulation by a distinct family of type II
RT TARPs.";
RL Neuron 59:986-996(2008).
RN [17]
RP INTERACTION WITH CACNG5.
RX PubMed=19234459; DOI=10.1038/nn.2266;
RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.;
RT "Selective regulation of long-form calcium-permeable AMPA receptors by an
RT atypical TARP, gamma-5.";
RL Nat. Neurosci. 12:277-285(2009).
RN [18]
RP ERRATUM OF PUBMED:19234459.
RX DOI=10.1038/nn0609-808c;
RA Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.;
RL Nat. Neurosci. 12:808-808(2009).
RN [19]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19265014; DOI=10.1126/science.1167852;
RA Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B.,
RA Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.;
RT "Functional proteomics identify cornichon proteins as auxiliary subunits of
RT AMPA receptors.";
RL Science 323:1313-1319(2009).
RN [20]
RP INTERACTION WITH CNIH2 AND CACNG2.
RX PubMed=20805473; DOI=10.1073/pnas.1011706107;
RA Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W.,
RA Nicoll R.A.;
RT "Functional comparison of the effects of TARPs and cornichons on AMPA
RT receptor trafficking and gating.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 890-907 IN COMPLEX WITH DLG1, AND
RP INTERACTION WITH DLG1.
RX PubMed=17069616; DOI=10.1111/j.1742-4658.2006.05521.x;
RA von Ossowski I., Oksanen E., von Ossowski L., Cai C., Sundberg M.,
RA Goldman A., Keinanen K.;
RT "Crystal structure of the second PDZ domain of SAP97 in complex with a
RT GluR-A C-terminal peptide.";
RL FEBS J. 273:5219-5229(2006).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-392, SUBUNIT, GLYCOSYLATION AT
RP ASN-63; ASN-249; ASN-257 AND ASN-363, AND DISULFIDE BOND.
RX PubMed=21639859; DOI=10.1042/bj20110801;
RA Yao G., Zong Y., Gu S., Zhou J., Xu H., Mathews I.I., Jin R.;
RT "Crystal structure of the glutamate receptor GluA1 N-terminal domain.";
RL Biochem. J. 438:255-263(2011).
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. {ECO:0000269|PubMed:16793768,
CC ECO:0000269|PubMed:19265014}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits (PubMed:21639859). 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 (PubMed:16793768, PubMed:19265014). Interacts with HIP1 and
CC RASGRF2. Interacts with SYNDIG1 and GRIA2 (By similarity). Interacts
CC with DLG1 (via C-terminus) (PubMed:12070168, PubMed:17069616,
CC PubMed:9677374). Interacts with LRFN1 (PubMed:16630835). Interacts with
CC PRKG2 (PubMed:18031684). Interacts with CNIH2 and CACNG2
CC (PubMed:20805473). Interacts with CACNG5 (PubMed:18817736,
CC PubMed:19234459). Interacts (via C-terminus) with PDLIM4 (via LIM
CC domain); this interaction as well as the interaction of PDLIM4 with
CC alpha-actinin is required for their colocalization in early endosomes
CC (PubMed:15456832). Interacts with SNX27 (via PDZ domain); the
CC interaction is required for recycling to the plasma membrane when
CC endocytosed and prevent degradation in lysosomes. Interacts (via PDZ-
CC binding motif) with SHANK3 (via PDZ domain) (By similarity). Interacts
CC with CACNG3; associates GRIA1 with the adapter protein complex 4 (AP-4)
CC to target GRIA1 to the somatodendritic compartment of neurons (By
CC similarity). {ECO:0000250|UniProtKB:P23818,
CC ECO:0000250|UniProtKB:P42261, ECO:0000269|PubMed:12070168,
CC ECO:0000269|PubMed:15456832, ECO:0000269|PubMed:16630835,
CC ECO:0000269|PubMed:16793768, ECO:0000269|PubMed:17069616,
CC ECO:0000269|PubMed:18031684, ECO:0000269|PubMed:18817736,
CC ECO:0000269|PubMed:19234459, ECO:0000269|PubMed:19265014,
CC ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21639859,
CC ECO:0000269|PubMed:9677374}.
CC -!- INTERACTION:
CC P19490; P10608: Adrb2; NbExp=3; IntAct=EBI-371642, EBI-7090342;
CC P19490; Q5FVC2: Arhgef2; NbExp=4; IntAct=EBI-371642, EBI-15756732;
CC P19490; Q71RJ2: Cacng2; NbExp=7; IntAct=EBI-371642, EBI-8538384;
CC P19490; P11275: Camk2a; NbExp=3; IntAct=EBI-371642, EBI-2640645;
CC P19490; Q5BJU5: Cnih2; NbExp=3; IntAct=EBI-371642, EBI-15874082;
CC P19490; P31016: Dlg4; NbExp=5; IntAct=EBI-371642, EBI-375655;
CC P19490; P19490: Gria1; NbExp=2; IntAct=EBI-371642, EBI-371642;
CC P19490; P19491: Gria2; NbExp=3; IntAct=EBI-371642, EBI-77718;
CC P19490; B2GV74: Klc2; NbExp=2; IntAct=EBI-371642, EBI-978371;
CC P19490; P70569: Myo5b; NbExp=2; IntAct=EBI-371642, EBI-975940;
CC P19490-2; P19491-2: Gria2; NbExp=2; IntAct=EBI-26900830, EBI-15817825;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23818};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P23818}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:15456832}; Multi-pass membrane
CC protein {ECO:0000305}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23818}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein
CC {ECO:0000305}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P23818}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P23818}. Early endosome membrane
CC {ECO:0000269|PubMed:15456832}; Multi-pass membrane protein
CC {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000269|PubMed:15456832}; Multi-pass membrane protein
CC {ECO:0000305}. Presynapse {ECO:0000250|UniProtKB:P23818}. Synapse
CC {ECO:0000250|UniProtKB:P23818}. Note=Interaction with CACNG2, CNIH2 and
CC CNIH3 promotes cell surface expression (PubMed:19265014). Colocalizes
CC with PDLIM4 in early endosomes (PubMed:15456832). Displays a
CC somatodendritic localization and is excluded from axons in neurons (By
CC similarity). Localized to cone photoreceptor pedicles (By similarity).
CC {ECO:0000250|UniProtKB:P23818, ECO:0000269|PubMed:15456832,
CC ECO:0000269|PubMed:19265014}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Flop;
CC IsoId=P19490-1; Sequence=Displayed;
CC Name=Flip;
CC IsoId=P19490-2; Sequence=VSP_000097, VSP_000098, VSP_000099,
CC VSP_000100, VSP_000101;
CC -!- TISSUE SPECIFICITY: Detected in cerebellum (at protein level).
CC {ECO:0000269|PubMed:12070168}.
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. Cys-603
CC palmitoylation leads to Golgi retention and decreased cell surface
CC expression. In contrast, Cys-829 palmitoylation does not affect cell
CC surface expression but regulates stimulation-dependent endocytosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-645 (PubMed:7877986). Phosphorylated at Ser-
CC 710 by PKC (PubMed:8848293). Phosphorylated at Ser-849 by PKC, PKA and
CC CAMK2 (PubMed:9405465). Phosphorylated at Ser-863 by PKC, PKA and PRKG2
CC (PubMed:18031684, PubMed:9405465). Phosphorylation of Ser-863 is
CC reduced by induction of long-term depression and increased by induction
CC of long-term potentiation (By similarity).
CC {ECO:0000250|UniProtKB:P23818, ECO:0000269|PubMed:18031684,
CC ECO:0000269|PubMed:7877986, ECO:0000269|PubMed:8848293,
CC ECO:0000269|PubMed:9405465}.
CC -!- POLYMORPHISM: Both variants Ser-710 and Thr-710 are phosphorylated at
CC this position.
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; X17184; CAA35050.1; -; mRNA.
DR EMBL; M36418; AAA41243.2; -; mRNA.
DR EMBL; M38060; AAA63479.1; -; mRNA.
DR PIR; A40170; A40170.
DR PIR; S07059; ACRTK1.
DR RefSeq; NP_113796.1; NM_031608.1. [P19490-1]
DR PDB; 2AWW; X-ray; 2.21 A; C=890-907.
DR PDB; 2G2L; X-ray; 2.35 A; C/D=890-907.
DR PDB; 3SAJ; X-ray; 2.50 A; A/B/C/D=22-392.
DR PDB; 6NJL; EM; 6.70 A; A/C=1-907.
DR PDB; 6NJN; EM; 6.50 A; A=1-907.
DR PDB; 6QKC; EM; 4.10 A; A/C=1-907.
DR PDB; 6QKZ; EM; 6.30 A; A/C=20-907.
DR PDB; 7OCA; EM; 3.40 A; A/C=1-907.
DR PDB; 7OCC; EM; 3.40 A; A/C=1-907.
DR PDB; 7OCD; EM; 3.50 A; A/C=1-907.
DR PDB; 7OCE; EM; 3.10 A; A/C=1-907.
DR PDB; 7OCF; EM; 3.60 A; A/C=1-907.
DR PDB; 7QHB; EM; 3.50 A; A/C=1-907.
DR PDB; 7QHH; EM; 3.60 A; A/C=1-907.
DR PDBsum; 2AWW; -.
DR PDBsum; 2G2L; -.
DR PDBsum; 3SAJ; -.
DR PDBsum; 6NJL; -.
DR PDBsum; 6NJN; -.
DR PDBsum; 6QKC; -.
DR PDBsum; 6QKZ; -.
DR PDBsum; 7OCA; -.
DR PDBsum; 7OCC; -.
DR PDBsum; 7OCD; -.
DR PDBsum; 7OCE; -.
DR PDBsum; 7OCF; -.
DR PDBsum; 7QHB; -.
DR PDBsum; 7QHH; -.
DR AlphaFoldDB; P19490; -.
DR SMR; P19490; -.
DR BioGRID; 248399; 15.
DR CORUM; P19490; -.
DR DIP; DIP-30929N; -.
DR ELM; P19490; -.
DR IntAct; P19490; 27.
DR MINT; P19490; -.
DR STRING; 10116.ENSRNOP00000064722; -.
DR BindingDB; P19490; -.
DR ChEMBL; CHEMBL3753; -.
DR DrugCentral; P19490; -.
DR TCDB; 1.A.10.1.1; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; P19490; 6 sites.
DR iPTMnet; P19490; -.
DR PhosphoSitePlus; P19490; -.
DR SwissPalm; P19490; -.
DR PRIDE; P19490; -.
DR ABCD; P19490; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000071615; ENSRNOP00000064722; ENSRNOG00000045816. [P19490-1]
DR Ensembl; ENSRNOT00000081136; ENSRNOP00000074119; ENSRNOG00000045816. [P19490-2]
DR GeneID; 50592; -.
DR KEGG; rno:50592; -.
DR UCSC; RGD:621531; rat. [P19490-1]
DR CTD; 2890; -.
DR RGD; 621531; Gria1.
DR eggNOG; KOG1054; Eukaryota.
DR GeneTree; ENSGT00940000157342; -.
DR InParanoid; P19490; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P19490; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-399710; Activation of AMPA receptors.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR EvolutionaryTrace; P19490; -.
DR PRO; PR:P19490; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0044308; C:axonal spine; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0032590; C:dendrite membrane; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:ARUK-UCL.
DR GO; GO:0032591; C:dendritic spine membrane; ISO:RGD.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0044309; C:neuron spine; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0099544; C:perisynaptic space; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO-UCL.
DR GO; GO:0097060; C:synaptic membrane; IDA:ARUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0008179; F:adenylate cyclase binding; IDA:RGD.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:ARUK-UCL.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IDA:RGD.
DR GO; GO:0035254; F:glutamate receptor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0019865; F:immunoglobulin binding; IPI:UniProtKB.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0031489; F:myosin V binding; IPI:RGD.
DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:ARUK-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0051018; F:protein kinase A binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:SynGO-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0071418; P:cellular response to amine stimulus; IEP:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEP:RGD.
DR GO; GO:0071242; P:cellular response to ammonium ion; ISO:RGD.
DR GO; GO:0071359; P:cellular response to dsRNA; IEP:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007616; P:long-term memory; IMP:RGD.
DR GO; GO:0060292; P:long-term synaptic depression; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:UniProtKB.
DR GO; GO:0019228; P:neuronal action potential; IMP:UniProtKB.
DR GO; GO:0045838; P:positive regulation of membrane potential; IMP:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0001919; P:regulation of receptor recycling; IMP:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0060992; P:response to fungicide; IEP:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; NAS:UniProtKB.
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; Alternative splicing; Cell membrane; Cell projection;
KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..907
FT /note="Glutamate receptor 1"
FT /id="PRO_0000011531"
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:0000269|PubMed:7877986"
FT MOD_RES 710
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:8848293"
FT MOD_RES 849
FT /note="Phosphoserine; by PKC, PKA and CAMK2"
FT /evidence="ECO:0000269|PubMed:7877986,
FT ECO:0000269|PubMed:9405465"
FT MOD_RES 863
FT /note="Phosphoserine; by PKC, PKA and PKG/PRKG2"
FT /evidence="ECO:0000269|PubMed:18031684,
FT ECO:0000269|PubMed:9405465"
FT LIPID 603
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 829
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21639859"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21639859"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21639859"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21639859"
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:0000269|PubMed:21639859"
FT DISULFID 732..787
FT /evidence="ECO:0000250"
FT VAR_SEQ 758
FT /note="N -> G (in isoform Flip)"
FT /evidence="ECO:0000303|PubMed:1699275"
FT /id="VSP_000097"
FT VAR_SEQ 768
FT /note="N -> S (in isoform Flip)"
FT /evidence="ECO:0000303|PubMed:1699275"
FT /id="VSP_000098"
FT VAR_SEQ 772
FT /note="L -> V (in isoform Flip)"
FT /evidence="ECO:0000303|PubMed:1699275"
FT /id="VSP_000099"
FT VAR_SEQ 778
FT /note="N -> S (in isoform Flip)"
FT /evidence="ECO:0000303|PubMed:1699275"
FT /id="VSP_000100"
FT VAR_SEQ 790..793
FT /note="GGGD -> KDSG (in isoform Flip)"
FT /evidence="ECO:0000303|PubMed:1699275"
FT /id="VSP_000101"
FT VARIANT 710
FT /note="S -> T"
FT /evidence="ECO:0000269|PubMed:1699275,
FT ECO:0000269|PubMed:8848293"
FT MUTAGEN 645
FT /note="S->A: No effect on phosphorylation by CaMK2."
FT /evidence="ECO:0000269|PubMed:9405465"
FT MUTAGEN 849
FT /note="S->A: Abolishes phosphorylation by CaMK2."
FT /evidence="ECO:0000269|PubMed:9405465"
FT MUTAGEN 855
FT /note="R->A: Decreases binding efficiency to PRKG2."
FT MUTAGEN 855
FT /note="R->E: Abolishes binding to PRKG2."
FT /evidence="ECO:0000269|PubMed:18031684"
FT MUTAGEN 863
FT /note="S->A: Decreases synaptic insertion during chemical-
FT induced long term potentiation."
FT /evidence="ECO:0000269|PubMed:18031684"
FT MUTAGEN 905
FT /note="T->A: Loss of interaction with DLG1."
FT /evidence="ECO:0000269|PubMed:12070168"
FT MUTAGEN 907
FT /note="L->A: Loss of interaction with DLG1."
FT /evidence="ECO:0000269|PubMed:12070168"
FT CONFLICT 67
FT /note="S -> T (in Ref. 6; AAA63479)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> R (in Ref. 6; AAA63479)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="R -> L (in Ref. 6; AAA63479)"
FT /evidence="ECO:0000305"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 51..61
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:3SAJ"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:7OCA"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:3SAJ"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:7OCA"
FT HELIX 261..276
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 288..309
FT /evidence="ECO:0007829|PDB:3SAJ"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:3SAJ"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:3SAJ"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:7OCE"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 431..434
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 438..450
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:7OCE"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 487..494
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 497..502
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:7OCE"
FT TURN 531..534
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 537..558
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 587..598
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 610..643
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 650..655
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 668..674
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 679..687
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 690..693
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:7OCD"
FT HELIX 700..709
FT /evidence="ECO:0007829|PDB:7OCE"
FT TURN 710..712
FT /evidence="ECO:0007829|PDB:7OCD"
FT STRAND 714..719
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 720..727
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:7OCD"
FT STRAND 734..738
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 744..751
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 758..770
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 772..781
FT /evidence="ECO:0007829|PDB:7OCE"
FT TURN 782..784
FT /evidence="ECO:0007829|PDB:7OCE"
FT TURN 803..806
FT /evidence="ECO:0007829|PDB:7OCE"
FT HELIX 807..837
FT /evidence="ECO:0007829|PDB:7OCE"
FT STRAND 905..907
FT /evidence="ECO:0007829|PDB:2AWW"
SQ SEQUENCE 907 AA; 101579 MW; 2D4CFA7CCD532838 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 RTSDSRDHTR 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 PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW
WYDKGECGSG GGDSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK
GFCLIPQQSI NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM
PLGATGL
