GRIK3_MOUSE
ID GRIK3_MOUSE Reviewed; 919 AA.
AC B1AS29; Q17R20; Q9JIA8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Glutamate receptor ionotropic, kainate 3;
DE Short=GluK3;
DE AltName: Full=Glutamate receptor 7;
DE Short=GluR-7;
DE Short=GluR7;
DE Flags: Precursor;
GN Name=Grik3; Synonyms=Glur7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-897.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 403-919, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11124978; DOI=10.1523/jneurosci.20-24-09025.2000;
RA Schiffer H.H., Swanson G.T., Masliah E., Heinemann S.F.;
RT "Unequal expression of allelic kainate receptor GluR7 mRNAs in human
RT brains.";
RL J. Neurosci. 20:9025-9033(2000).
RN [4]
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).
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. The
CC postsynaptic actions of Glu are mediated by a variety of receptors that
CC are named according to their selective agonists. This receptor binds
CC domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with either GRIK4 or GRIK5.
CC Interacts with PRKCABP (By similarity). Interacts with NETO2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in whole brain, cerebellum, brain cortex
CC and hippocampus. {ECO:0000269|PubMed:11124978}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIK3 subfamily. {ECO:0000305}.
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DR EMBL; AL607090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118004; AAI18005.1; -; mRNA.
DR EMBL; AF245444; AAF90049.1; -; mRNA.
DR CCDS; CCDS38878.1; -.
DR RefSeq; NP_001074566.1; NM_001081097.2.
DR AlphaFoldDB; B1AS29; -.
DR SMR; B1AS29; -.
DR BioGRID; 200065; 3.
DR IntAct; B1AS29; 1.
DR STRING; 10090.ENSMUSP00000030676; -.
DR GlyConnect; 2348; 5 N-Linked glycans (1 site).
DR GlyGen; B1AS29; 10 sites, 5 N-linked glycans (1 site).
DR iPTMnet; B1AS29; -.
DR PhosphoSitePlus; B1AS29; -.
DR SwissPalm; B1AS29; -.
DR MaxQB; B1AS29; -.
DR PaxDb; B1AS29; -.
DR PeptideAtlas; B1AS29; -.
DR PRIDE; B1AS29; -.
DR ProteomicsDB; 269630; -.
DR Antibodypedia; 3095; 187 antibodies from 28 providers.
DR DNASU; 14807; -.
DR Ensembl; ENSMUST00000030676; ENSMUSP00000030676; ENSMUSG00000001985.
DR GeneID; 14807; -.
DR KEGG; mmu:14807; -.
DR UCSC; uc008usa.2; mouse.
DR CTD; 2899; -.
DR MGI; MGI:95816; Grik3.
DR VEuPathDB; HostDB:ENSMUSG00000001985; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000159465; -.
DR HOGENOM; CLU_007257_1_1_1; -.
DR InParanoid; B1AS29; -.
DR OMA; EREQVFV; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; B1AS29; -.
DR TreeFam; TF334668; -.
DR Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR BioGRID-ORCS; 14807; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Grik3; mouse.
DR PRO; PR:B1AS29; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AS29; protein.
DR Bgee; ENSMUSG00000001985; Expressed in median eminence of neurohypophysis and 134 other tissues.
DR Genevisible; B1AS29; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; ISO:MGI.
DR GO; GO:0008066; F:glutamate receptor activity; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISS:UniProtKB.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; ISO:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
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; IBA:GO_Central.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
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 Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Isopeptide bond; Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..919
FT /note="Glutamate receptor ionotropic, kainate 3"
FT /id="PRO_0000416793"
FT TOPO_DOM 32..563
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..820
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 842..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 520
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 525
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 690..692
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 739
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
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 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..350
FT /evidence="ECO:0000250"
FT CROSSLNK 887
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
SQ SEQUENCE 919 AA; 104051 MW; DD543E45951ACB87 CRC64;
MTAPWRRLRS LVWEYWAGFL VCAFWIPDSR GMPHVIRIGG IFEYADGPNA QVMNAEEHAF
RFSANIINRN RTLLPNTTLT YDIQRIHFHD SFEATKKACD QLALGVVAIF GPSQGSCTNA
VQSICNALEV PHIQLRWKHH PLDNKDTFYV NLYPDYASLS HAILDLVQSL KWRSATVVYD
DSTGLIRLQE LIMAPSRYNI RLKIRQLPID SDDSRPLLKE MKRGREFRII FDCSHTMAAQ
ILKQAMAMGM MTEYYHFIFT TLDLYALDLE PYRYSGVNLT GFRILNVDNP HVSAIVEKWA
MERLQAAPRA ESGLLDGVMM TDAALLYDAV HIVSVCYQRA PQMTVNSLQC HRHKAWRFGG
RFMNFIKEAQ WEGLTGRIVF NKTSGLRTDF DLDIISLKED GLEKVGVWSP ADGLNITEVA
KGRGPNVTDS LTNRSLIVTT VLEEPFVMFR KSDRTLYGND RFEGYCIDLL KELAHILGFS
YEIRLVEDGK YGAQDDKGQW NGMVKELIDH KADLAVAPLT ITHVREKAID FSKPFMTLGV
SILYRKPNGT NPSVFSFLNP LSPDIWMYVL LAYLGVSCVL FVIARFSPYE WYDAHPCNPG
SEVVENNFTL LNSFWFGMGS LMQQGSELMP KALSTRIIGG IWWFFTLIII SSYTANLAAF
LTVERMESPI DSADDLAKQT KIEYGAVKDG ATMTFFKKSK ISTFEKMWAF MSSKPSALVK
NNEEGIQRTL TADYALLMES TTIEYITQRN CNLTQIGGLI DSKGYGIGTP MGSPYRDKIT
IAILQLQEED KLHIMKEKWW RGSGCPEEEN KEASALGIQK IGGIFIVLAA GLVLSVLVAV
GEFIYKLRKT AEREQRSFCS TVADEIRFSL TCQRRLKHKP QPPMMVKTDA VINMHTFNDR
RLPGKDSMSC STSLAPVFP
