GRIA1_HUMAN
ID GRIA1_HUMAN Reviewed; 906 AA.
AC P42261; B7Z2S0; B7Z2W8; B7Z3F6; B7Z9G9; D3DQI4; E7ESV8; Q2NKM6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 221.
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=GLUH1, GLUR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP).
RX PubMed=1652753; DOI=10.1073/pnas.88.17.7557;
RA Puckett C., Gomez C.M., Korenberg J.R., Tung H., Meier T.J., Chen X.N.,
RA Hood L.E.;
RT "Molecular cloning and chromosomal localization of one of the human
RT glutamate receptor genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7557-7561(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
RC TISSUE=Hippocampus;
RX PubMed=1320959; DOI=10.3109/10425179209020805;
RA Potier M.-C., Spillantini M.G., Carter N.P.;
RT "The human glutamate receptor cDNA GluR1: cloning, sequencing, expression
RT and localization to chromosome 5.";
RL DNA Seq. 2:211-218(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
RX PubMed=1311100; DOI=10.1073/pnas.89.4.1443;
RA Sun W., Ferrer-Montiel A.V., Schinder A.F., McPherson J.P., Evans G.A.,
RA Montal M.;
RT "Molecular cloning, chromosomal mapping, and functional expression of human
RT brain glutamate receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1443-1447(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5 AND 6).
RC TISSUE=Brain, Cerebellum, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FLOP).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION.
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 [9]
RP FUNCTION, AND 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 [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23739980; DOI=10.1523/jneurosci.2626-12.2013;
RA Salussolia C.L., Gan Q., Kazi R., Singh P., Allopenna J., Furukawa H.,
RA Wollmuth L.P.;
RT "A eukaryotic specific transmembrane segment is required for
RT tetramerization in AMPA receptors.";
RL J. Neurosci. 33:9840-9845(2013).
RN [11]
RP VARIANT THR-636.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
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:20805473,
CC ECO:0000269|PubMed:21172611}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits (By similarity). Tetramers may be formed by the
CC dimerization of dimers (PubMed:23739980). Found in a complex with
CC GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5,
CC CACNG7 and CACNG8 (By similarity). Interacts with HIP1 and RASGRF2.
CC Interacts with SYNDIG1 and GRIA2 (By similarity). Interacts with DLG1
CC (via C-terminus). Interacts with LRFN1. Interacts with PRKG2 (By
CC similarity). Interacts with CNIH2 and CACNG2 (PubMed:20805473).
CC Interacts with CACNG5. 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 Interacts with SNX27 (via PDZ domain); the interaction is required for
CC recycling to the plasma membrane when endocytosed and prevent
CC degradation in lysosomes. Interacts (via PDZ-binding motif) with SHANK3
CC (via PDZ domain) (By similarity). Interacts with CACNG3; associates
CC GRIA1 with the adapter protein complex 4 (AP-4) to target GRIA1 to the
CC somatodendritic compartment of neurons (By similarity).
CC {ECO:0000250|UniProtKB:P19490, ECO:0000250|UniProtKB:P23818,
CC ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:23739980}.
CC -!- INTERACTION:
CC P42261; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-6980805, EBI-10254793;
CC P42261; Q14457: BECN1; NbExp=3; IntAct=EBI-6980805, EBI-949378;
CC P42261; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-6980805, EBI-2796400;
CC P42261; Q15907: RAB11B; NbExp=3; IntAct=EBI-6980805, EBI-722234;
CC P42261; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-6980805, EBI-749023;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23739980};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23739980}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P19490}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:23739980}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23739980}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:P23818}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23818}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P23818}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P23818}. Early endosome membrane
CC {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P19490}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P19490}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P19490}. Presynapse
CC {ECO:0000250|UniProtKB:P23818}. Synapse {ECO:0000250|UniProtKB:P23818}.
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 (By
CC similarity). Localized to cone photoreceptor pedicles (By similarity).
CC {ECO:0000250|UniProtKB:P19490, ECO:0000250|UniProtKB:P23818}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=Flop;
CC IsoId=P42261-1; Sequence=Displayed;
CC Name=Flip;
CC IsoId=P42261-2; Sequence=VSP_053349;
CC Name=3;
CC IsoId=P42261-3; Sequence=VSP_045120;
CC Name=4;
CC IsoId=P42261-4; Sequence=VSP_045119;
CC Name=5;
CC IsoId=P42261-5; Sequence=VSP_047024;
CC Name=6;
CC IsoId=P42261-6; Sequence=VSP_047024, VSP_053349;
CC -!- TISSUE SPECIFICITY: Widely expressed in brain.
CC -!- DOMAIN: The M4 transmembrane segment mediates tetramerization and is
CC required for cell surface expression.
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. 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 (By similarity).
CC {ECO:0000250|UniProtKB:P19490, ECO:0000250|UniProtKB:P23818}.
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; M64752; AAA58613.1; -; mRNA.
DR EMBL; X58633; CAA41491.1; -; mRNA.
DR EMBL; M81886; AAA58395.1; -; mRNA.
DR EMBL; AK295039; BAH11956.1; -; mRNA.
DR EMBL; AK295184; BAH12004.1; -; mRNA.
DR EMBL; AK295827; BAH12192.1; -; mRNA.
DR EMBL; AK315934; BAH14305.1; -; mRNA.
DR EMBL; AC010613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61649.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61650.1; -; Genomic_DNA.
DR EMBL; BC111734; AAI11735.1; -; mRNA.
DR CCDS; CCDS4322.1; -. [P42261-1]
DR CCDS; CCDS47318.1; -. [P42261-2]
DR CCDS; CCDS58986.1; -. [P42261-3]
DR CCDS; CCDS58987.1; -. [P42261-5]
DR CCDS; CCDS58988.1; -. [P42261-6]
DR CCDS; CCDS58989.1; -. [P42261-4]
DR PIR; A40222; A40222.
DR PIR; A41273; A41273.
DR PIR; S25852; S25852.
DR PIR; S38723; S38723.
DR RefSeq; NP_000818.2; NM_000827.3. [P42261-1]
DR RefSeq; NP_001107655.1; NM_001114183.1. [P42261-2]
DR RefSeq; NP_001244948.1; NM_001258019.1. [P42261-3]
DR RefSeq; NP_001244950.1; NM_001258021.1. [P42261-5]
DR RefSeq; NP_001244951.1; NM_001258022.1. [P42261-6]
DR RefSeq; NP_001244952.1; NM_001258023.1. [P42261-4]
DR PDB; 6X5Q; X-ray; 2.14 A; B=836-855.
DR PDBsum; 6X5Q; -.
DR AlphaFoldDB; P42261; -.
DR SMR; P42261; -.
DR BioGRID; 109147; 31.
DR CORUM; P42261; -.
DR DIP; DIP-41487N; -.
DR IntAct; P42261; 6.
DR MINT; P42261; -.
DR STRING; 9606.ENSP00000428994; -.
DR BindingDB; P42261; -.
DR ChEMBL; CHEMBL2009; -.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB05047; CX-717.
DR DrugBank; DB06247; CX516.
DR DrugBank; DB01189; Desflurane.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB13146; Fluciclovine (18F).
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00753; Isoflurane.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB01028; Methoxyflurane.
DR DrugBank; DB08883; Perampanel.
DR DrugBank; DB01236; Sevoflurane.
DR DrugBank; DB04982; Talampanel.
DR DrugBank; DB09289; Tianeptine.
DR DrugCentral; P42261; -.
DR GuidetoPHARMACOLOGY; 444; -.
DR TCDB; 1.A.10.1.23; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; P42261; 8 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P42261; -.
DR PhosphoSitePlus; P42261; -.
DR SwissPalm; P42261; -.
DR BioMuta; GRIA1; -.
DR DMDM; 116242505; -.
DR MassIVE; P42261; -.
DR PaxDb; P42261; -.
DR PeptideAtlas; P42261; -.
DR PRIDE; P42261; -.
DR ProteomicsDB; 18070; -.
DR ProteomicsDB; 55496; -. [P42261-1]
DR ProteomicsDB; 55497; -. [P42261-2]
DR ProteomicsDB; 6455; -.
DR ProteomicsDB; 6517; -.
DR ProteomicsDB; 7030; -.
DR Antibodypedia; 28276; 1038 antibodies from 46 providers.
DR DNASU; 2890; -.
DR Ensembl; ENST00000285900.10; ENSP00000285900.4; ENSG00000155511.18. [P42261-1]
DR Ensembl; ENST00000340592.9; ENSP00000339343.5; ENSG00000155511.18. [P42261-2]
DR Ensembl; ENST00000448073.8; ENSP00000415569.2; ENSG00000155511.18. [P42261-6]
DR Ensembl; ENST00000518142.5; ENSP00000427920.1; ENSG00000155511.18. [P42261-3]
DR Ensembl; ENST00000518783.1; ENSP00000428994.1; ENSG00000155511.18. [P42261-5]
DR Ensembl; ENST00000521843.6; ENSP00000427864.2; ENSG00000155511.18. [P42261-4]
DR GeneID; 2890; -.
DR KEGG; hsa:2890; -.
DR MANE-Select; ENST00000285900.10; ENSP00000285900.4; NM_000827.4; NP_000818.2.
DR UCSC; uc003luy.5; human. [P42261-1]
DR CTD; 2890; -.
DR DisGeNET; 2890; -.
DR GeneCards; GRIA1; -.
DR HGNC; HGNC:4571; GRIA1.
DR HPA; ENSG00000155511; Group enriched (brain, retina).
DR MIM; 138248; gene.
DR neXtProt; NX_P42261; -.
DR OpenTargets; ENSG00000155511; -.
DR PharmGKB; PA28966; -.
DR VEuPathDB; HostDB:ENSG00000155511; -.
DR eggNOG; KOG1054; Eukaryota.
DR GeneTree; ENSGT00940000157342; -.
DR HOGENOM; CLU_007257_1_2_1; -.
DR InParanoid; P42261; -.
DR OMA; MSHTAAM; -.
DR OrthoDB; 1324479at2759; -.
DR PhylomeDB; P42261; -.
DR TreeFam; TF315232; -.
DR PathwayCommons; P42261; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-399710; Activation of AMPA receptors.
DR Reactome; R-HSA-399719; Trafficking of AMPA receptors.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
DR Reactome; R-HSA-9620244; Long-term potentiation.
DR SignaLink; P42261; -.
DR SIGNOR; P42261; -.
DR BioGRID-ORCS; 2890; 6 hits in 1069 CRISPR screens.
DR ChiTaRS; GRIA1; human.
DR GeneWiki; GRIA1; -.
DR GenomeRNAi; 2890; -.
DR Pharos; P42261; Tclin.
DR PRO; PR:P42261; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P42261; protein.
DR Bgee; ENSG00000155511; Expressed in CA1 field of hippocampus and 135 other tissues.
DR Genevisible; P42261; HS.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; ISS:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044308; C:axonal spine; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0032591; C:dendritic spine membrane; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0044309; C:neuron spine; ISS:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0099544; C:perisynaptic space; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; ISS:ARUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
DR GO; GO:0008066; F:glutamate receptor activity; TAS:ProtInc.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISS:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0071242; P:cellular response to ammonium ion; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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..906
FT /note="Glutamate receptor 1"
FT /id="PRO_0000011529"
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 TOPO_DOM 827..906
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 861..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 903..906
FT /note="PDZ-binding"
FT COMPBIAS 861..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:P19490"
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: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 VAR_SEQ 1..69
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045119"
FT VAR_SEQ 1..28
FT /note="MQHIFAFFCTGFLGAVVGANFPNNIQIG -> MCCSTHLFQPLQLAGGLEWP
FT WSNLLCFLTPVKLHPEVW (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047024"
FT VAR_SEQ 74..154
FT /note="FCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVDTSNQFVLQL
FT RPELQDALISIIDHYKWQKFVYIYDADRG -> C (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045120"
FT VAR_SEQ 758..793
FT /note="NPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD -> GPVNLAVLKLSE
FT QGVLDKLKSKWWYDKGECGSKDSG (in isoform Flip and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1652753"
FT /id="VSP_053349"
FT VARIANT 487
FT /note="D -> N (in dbSNP:rs13166146)"
FT /id="VAR_028071"
FT VARIANT 521
FT /note="P -> T (in dbSNP:rs13166161)"
FT /id="VAR_028072"
FT VARIANT 536
FT /note="A -> S (in dbSNP:rs13166438)"
FT /id="VAR_028073"
FT VARIANT 548
FT /note="I -> M (in dbSNP:rs13186241)"
FT /id="VAR_028074"
FT VARIANT 588
FT /note="F -> L (in dbSNP:rs13186534)"
FT /id="VAR_028075"
FT VARIANT 636
FT /note="A -> T (found in patient with severe intellectual
FT disability; unknown pathological significance;
FT dbSNP:rs587776937)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_078689"
FT CONFLICT 345
FT /note="R -> A (in Ref. 2; CAA41491)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="G -> S (in Ref. 3; AAA58395)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="G -> E (in Ref. 4; BAH12004)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="S -> SA (in Ref. 1; AAA58613)"
FT /evidence="ECO:0000305"
FT CONFLICT 865..867
FT /note="AGA -> TAP (in Ref. 1; AAA58613)"
FT /evidence="ECO:0000305"
FT HELIX 837..840
FT /evidence="ECO:0007829|PDB:6X5Q"
SQ SEQUENCE 906 AA; 101506 MW; 03EA1E026D0A9A2F CRC64;
MQHIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID
IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ
FVLQLRPELQ DALISIIDHY KWQKFVYIYD ADRGLSVLQK VLDTAAEKNW QVTAVNILTT
TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIIKLE KNGIGYHYIL ANLGFMDIDL
NKFKESGANV TGFQLVNYTD TIPAKIMQQW KNSDARDHTR 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 RNSGAGASSG GSGENGRVVS HDFPKSMQSI PCMSHSSGMP
LGATGL
