GRIA3_HUMAN
ID GRIA3_HUMAN Reviewed; 894 AA.
AC P42263; D3DTF1; Q4VXD5; Q4VXD6; Q9HDA0; Q9HDA1; Q9HDA2; Q9P0H1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Glutamate receptor 3;
DE Short=GluR-3;
DE AltName: Full=AMPA-selective glutamate receptor 3;
DE AltName: Full=GluR-C;
DE AltName: Full=GluR-K3;
DE AltName: Full=Glutamate receptor ionotropic, AMPA 3;
DE Short=GluA3;
DE Flags: Precursor;
GN Name=GRIA3; Synonyms=GLUR3, GLURC;
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] (ISOFORMS FLIP AND FLOP), AND VARIANT LEU-525.
RC TISSUE=Hippocampus;
RX PubMed=7918660; DOI=10.1016/0167-4781(94)90090-6;
RA Rampersad V., Elliott C.E., Nutt S.L., Foldes R.L., Kamboj R.K.;
RT "Human glutamate receptor hGluR3 flip and flop isoforms: cloning and
RT sequencing of the cDNAs and primary structure of the proteins.";
RL Biochim. Biophys. Acta 1219:563-566(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA McLaughlin D.P., Kerwin R.W.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-525.
RX PubMed=10644433; DOI=10.1006/geno.1999.6032;
RA Gecz J., Barnett S., Liu J., Hollway G., Donnelly A., Eyre H.,
RA Eshkevari H.S., Baltazar R., Grunn A., Nagaraja R., Gilliam C.,
RA Peltonen L., Sutherland G.R., Baron M., Mulley J.C.;
RT "Characterization of the human glutamate receptor subunit 3 gene (GRIA3), a
RT candidate for bipolar disorder and nonspecific X-linked mental
RT retardation.";
RL Genomics 62:356-368(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-525.
RX PubMed=10602120;
RX DOI=10.1002/(sici)1096-8628(20000103)90:1<69::aid-ajmg12>3.0.co;2-w;
RA Amir R., Dahle E.J., Toriolo D., Zoghbi H.Y.;
RT "Candidate gene analysis in Rett syndrome and the identification of 21 SNPs
RT in Xq.";
RL Am. J. Med. Genet. 90:69-71(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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 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 [8]
RP VARIANTS MRXSW GLN-450; SER-631; THR-706 AND ARG-833, AND CHARACTERIZATION
RP OF VARIANTS MRXSW SER-631; THR-706 AND ARG-833.
RX PubMed=17989220; DOI=10.1073/pnas.0708699104;
RA Wu Y., Arai A.C., Rumbaugh G., Srivastava A.K., Turner G., Hayashi T.,
RA Suzuki E., Jiang Y., Zhang L., Rodriguez J., Boyle J., Tarpey P.,
RA Raymond F.L., Nevelsteen J., Froyen G., Stratton M., Futreal A., Gecz J.,
RA Stevenson R., Schwartz C.E., Valle D., Huganir R.L., Wang T.;
RT "Mutations in ionotropic AMPA receptor 3 alter channel properties and are
RT associated with moderate cognitive impairment in humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18163-18168(2007).
RN [9]
RP VARIANT LYS-224.
RX PubMed=30165711; DOI=10.1055/s-0038-1668141;
RA Fazeli W., Becker K., Herkenrath P., Duechting C., Koerber F., Landgraf P.,
RA Nuernberg P., Altmueller J., Thiele H., Koy A., Liebau M.C., Simon T.,
RA Doetsch J., Cirak S.;
RT "Dominant SCN2A Mutation Causes Familial Episodic Ataxia and Impairment of
RT Speech Development.";
RL Neuropediatrics 49:379-384(2018).
CC -!- FUNCTION: Receptor for glutamate that functions as ligand-gated ion
CC channel in the central nervous system and plays an important role in
CC excitatory synaptic transmission. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system.
CC Binding of the excitatory neurotransmitter L-glutamate induces a
CC conformation change, leading to the opening of the cation channel, and
CC 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:21172611}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits. Tetramers may be formed by the dimerization of
CC dimers. Interacts with PRKCABP, GRIP1 and GRIP2 (By similarity). Found
CC in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3,
CC CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC Note=Interaction with CNIH2 and CNIH3 promotes cell surface expression.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Flop;
CC IsoId=P42263-1; Sequence=Displayed;
CC Name=Flip;
CC IsoId=P42263-2; Sequence=VSP_053351;
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-621
CC palmitoylation leads to Golgi retention and decreased cell surface
CC expression. In contrast, Cys-847 palmitoylation does not affect cell
CC surface expression but regulates stimulation-dependent endocytosis (By
CC similarity). {ECO:0000250}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic, Wu
CC type (MRXSW) [MIM:300699]: A disorder characterized by significantly
CC below average general intellectual functioning associated with
CC impairments in adaptive behavior and manifested during the
CC developmental period. MRXSW patients have moderate intellectual
CC disability, and additional variable features such as macrocephaly,
CC seizures, myoclonic jerks, autistic behavior, asthenic body habitus,
CC distal muscle weakness and hyporeflexia. {ECO:0000269|PubMed:17989220}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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. GRIA3 subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
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DR EMBL; U10302; AAA67923.1; -; mRNA.
DR EMBL; U10301; AAA67922.1; -; mRNA.
DR EMBL; X82068; CAA57567.1; -; mRNA.
DR EMBL; AF159277; AAF61847.1; -; Genomic_DNA.
DR EMBL; AF159262; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159263; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159264; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159265; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159266; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159267; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159268; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159269; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159270; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159271; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159272; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159273; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159274; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF159275; AAF61847.1; JOINED; Genomic_DNA.
DR EMBL; AF166365; AAF97857.1; -; Genomic_DNA.
DR EMBL; AF166362; AAF97857.1; JOINED; Genomic_DNA.
DR EMBL; AF166363; AAF97857.1; JOINED; Genomic_DNA.
DR EMBL; AF166364; AAF97857.1; JOINED; Genomic_DNA.
DR EMBL; AF167332; AAF97858.1; -; Genomic_DNA.
DR EMBL; AF166366; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF166367; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF166368; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF166369; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF166370; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF166371; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF166372; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF166373; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF166375; AAF97858.1; JOINED; Genomic_DNA.
DR EMBL; AF167332; AAF97859.1; -; Genomic_DNA.
DR EMBL; AF166366; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AF166367; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AF166368; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AF166369; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AF166370; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AF166371; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AF166372; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AF166373; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AF166374; AAF97859.1; JOINED; Genomic_DNA.
DR EMBL; AL356213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z83848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471107; EAX11865.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11867.1; -; Genomic_DNA.
DR CCDS; CCDS14604.1; -. [P42263-1]
DR CCDS; CCDS14605.1; -. [P42263-2]
DR PIR; S49460; S49460.
DR PIR; S50128; S50128.
DR PIR; S53696; S53696.
DR RefSeq; NP_000819.3; NM_000828.4. [P42263-1]
DR RefSeq; NP_015564.4; NM_007325.4. [P42263-2]
DR AlphaFoldDB; P42263; -.
DR SMR; P42263; -.
DR BioGRID; 109149; 26.
DR DIP; DIP-46195N; -.
DR IntAct; P42263; 17.
DR MINT; P42263; -.
DR STRING; 9606.ENSP00000481554; -.
DR BindingDB; P42263; -.
DR ChEMBL; CHEMBL3595; -.
DR DrugBank; DB04599; Aniracetam.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB05047; CX-717.
DR DrugBank; DB00898; Ethanol.
DR DrugBank; DB13146; Fluciclovine (18F).
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB14509; Lithium carbonate.
DR DrugBank; DB01356; Lithium cation.
DR DrugBank; DB14507; Lithium citrate.
DR DrugBank; DB14508; Lithium succinate.
DR DrugBank; DB04982; Talampanel.
DR DrugCentral; P42263; -.
DR GuidetoPHARMACOLOGY; 446; -.
DR TCDB; 1.A.10.1.4; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; P42263; 5 sites.
DR iPTMnet; P42263; -.
DR PhosphoSitePlus; P42263; -.
DR SwissPalm; P42263; -.
DR BioMuta; GRIA3; -.
DR DMDM; 77416864; -.
DR EPD; P42263; -.
DR MassIVE; P42263; -.
DR PaxDb; P42263; -.
DR PeptideAtlas; P42263; -.
DR PRIDE; P42263; -.
DR ProteomicsDB; 55501; -. [P42263-1]
DR ProteomicsDB; 55502; -. [P42263-2]
DR Antibodypedia; 29962; 346 antibodies from 30 providers.
DR DNASU; 2892; -.
DR Ensembl; ENST00000620443.2; ENSP00000478489.1; ENSG00000125675.20. [P42263-2]
DR Ensembl; ENST00000622768.5; ENSP00000481554.1; ENSG00000125675.20. [P42263-1]
DR GeneID; 2892; -.
DR KEGG; hsa:2892; -.
DR MANE-Select; ENST00000620443.2; ENSP00000478489.1; NM_007325.5; NP_015564.5. [P42263-2]
DR UCSC; uc033etl.2; human. [P42263-1]
DR CTD; 2892; -.
DR DisGeNET; 2892; -.
DR GeneCards; GRIA3; -.
DR HGNC; HGNC:4573; GRIA3.
DR HPA; ENSG00000125675; Tissue enhanced (brain, retina).
DR MalaCards; GRIA3; -.
DR MIM; 300699; phenotype.
DR MIM; 305915; gene.
DR neXtProt; NX_P42263; -.
DR OpenTargets; ENSG00000125675; -.
DR Orphanet; 364028; X-linked intellectual disability due to GRIA3 mutations.
DR PharmGKB; PA28968; -.
DR VEuPathDB; HostDB:ENSG00000125675; -.
DR eggNOG; KOG1054; Eukaryota.
DR GeneTree; ENSGT00940000156123; -.
DR HOGENOM; CLU_007257_1_2_1; -.
DR InParanoid; P42263; -.
DR OMA; WHRTIAT; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P42263; -.
DR TreeFam; TF315232; -.
DR PathwayCommons; P42263; -.
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-8849932; Synaptic adhesion-like molecules.
DR SignaLink; P42263; -.
DR SIGNOR; P42263; -.
DR BioGRID-ORCS; 2892; 9 hits in 698 CRISPR screens.
DR ChiTaRS; GRIA3; human.
DR GeneWiki; GRIA3; -.
DR GenomeRNAi; 2892; -.
DR Pharos; P42263; Tclin.
DR PRO; PR:P42263; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P42263; protein.
DR Bgee; ENSG00000125675; Expressed in Brodmann (1909) area 23 and 142 other tissues.
DR ExpressionAtlas; P42263; baseline and differential.
DR Genevisible; P42263; 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:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
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:0007215; P:glutamate receptor signaling pathway; 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 Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW Glycoprotein; Intellectual disability; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..894
FT /note="Glutamate receptor 3"
FT /id="PRO_0000011536"
FT TOPO_DOM 29..552
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 574..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 603..618
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250"
FT INTRAMEM 619..621
FT /evidence="ECO:0000250"
FT TOPO_DOM 622..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 649..823
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 824..844
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 845..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 508..510
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 686..687
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 737
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 877
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2W9"
FT MOD_RES 887
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2W9"
FT LIPID 621
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 847
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..340
FT /evidence="ECO:0000250"
FT DISULFID 750..805
FT /evidence="ECO:0000250"
FT VAR_SEQ 776..811
FT /note="NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD -> TPVNLAVLKLSE
FT QGILDKLKNKWWYDKGECGAKDSG (in isoform Flip)"
FT /evidence="ECO:0000303|PubMed:7918660"
FT /id="VSP_053351"
FT VARIANT 224
FT /note="E -> K (found in patients with familial episodic
FT ataxia and impairment of speech development; unknown
FT pathological significance; dbSNP:rs757586471)"
FT /evidence="ECO:0000269|PubMed:30165711"
FT /id="VAR_081437"
FT VARIANT 450
FT /note="R -> Q (in MRXSW; dbSNP:rs368568228)"
FT /evidence="ECO:0000269|PubMed:17989220"
FT /id="VAR_043484"
FT VARIANT 525
FT /note="F -> L (in dbSNP:rs1052538)"
FT /evidence="ECO:0000269|PubMed:10602120,
FT ECO:0000269|PubMed:10644433, ECO:0000269|PubMed:7918660"
FT /id="VAR_023579"
FT VARIANT 631
FT /note="R -> S (in MRXSW; homomers have minimal or no
FT current; heteromers have altered desensitization kinetics;
FT dbSNP:rs137852351)"
FT /evidence="ECO:0000269|PubMed:17989220"
FT /id="VAR_043485"
FT VARIANT 706
FT /note="M -> T (in MRXSW; homomers have minimal or no
FT current; heteromers have altered desensitization kinetics;
FT dbSNP:rs137852352)"
FT /evidence="ECO:0000269|PubMed:17989220"
FT /id="VAR_043486"
FT VARIANT 833
FT /note="G -> R (in MRXSW; reduced receptor expression
FT possibly due to rapid degradation; dbSNP:rs137852350)"
FT /evidence="ECO:0000269|PubMed:17989220"
FT /id="VAR_043487"
FT CONFLICT 195
FT /note="N -> H (in Ref. 3; AAF61847)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="R -> G (in Ref. 1; AAA67922/AAA67923, 2; CAA57567
FT and 3; AAF61847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 101157 MW; 178589A870E0D102 CRC64;
MARQKKMGQS VLRAVFFLVL GLLGHSHGGF PNTISIGGLF MRNTVQEHSA FRFAVQLYNT
NQNTTEKPFH LNYHVDHLDS SNSFSVTNAF CSQFSRGVYA IFGFYDQMSM NTLTSFCGAL
HTSFVTPSFP TDADVQFVIQ MRPALKGAIL SLLGHYKWEK FVYLYDTERG FSILQAIMEA
AVQNNWQVTA RSVGNIKDVQ EFRRIIEEMD RRQEKRYLID CEVERINTIL EQVVILGKHS
RGYHYMLANL GFTDILLERV MHGGANITGF QIVNNENPMV QQFIQRWVRL DEREFPEAKN
APLKYTSALT HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKM
VQVQGMTGNI QFDTYGRRTN YTIDVYEMKV SGSRKAGYWN EYERFVPFSD QQISNDSASS
ENRTIVVTTI LESPYVMYKK NHEQLEGNER YEGYCVDLAY EIAKHVRIKY KLSIVGDGKY
GARDPETKIW NGMVGELVYG RADIAVAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS
KPGVFSFLDP LAYEIWMCIV FAYIGVSVVL FLVSRFSPYE WHLEDNNEEP RDPQSPPDPP
NEFGIFNSLW FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER
MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWSYMKSAE PSVFTKTTAD
GVARVRKSKG KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSALRNAVNL
AVLKLNEQGL LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAMM
VALIEFCYKS RAESKRMKLT KNTQNFKPAP ATNTQNYATY REGYNVYGTE SVKI
