ID   GRIK1_HUMAN             Reviewed;         918 AA.
AC   P39086; Q13001; Q86SU9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 211.
DE   RecName: Full=Glutamate receptor ionotropic, kainate 1;
DE            Short=GluK1;
DE   AltName: Full=Excitatory amino acid receptor 3;
DE            Short=EAA3;
DE   AltName: Full=Glutamate receptor 5;
DE            Short=GluR-5;
DE            Short=GluR5;
DE   Flags: Precursor;
GN   Name=GRIK1; Synonyms=GLUR5;
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 1).
RC   TISSUE=Retina;
RX   PubMed=8260617; DOI=10.1097/00001756-199309150-00014;
RA   Gregor P., O'Hara B.F., Yang X., Uhl G.R.;
RT   "Expression and novel subunit isoforms of glutamate receptor genes GluR5
RT   and GluR6.";
RL   NeuroReport 4:1343-1346(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=8589992;
RA   Korczak B., Nutt S.L., Fletcher E.J., Hoo K.H., Elliott C.E., Rampersad V.,
RA   McWhinnie E.A., Kamboj R.K.;
RT   "cDNA cloning and functional properties of human glutamate receptor EAA3
RT   (GluR5) in homomeric and heteromeric configuration.";
RL   Recept. Channels 3:41-49(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Erythroleukemia;
RA   Langer A., Xu D., Kuehcke K., Fehse B., Abdallah S., Lother H.;
RT   "Myeloid progenitor cell growth and apoptosis involves known and cell-
RT   specific ionotropic glutamate receptors.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   RNA EDITING OF POSITION 636.
RC   TISSUE=Brain;
RX   PubMed=7696618; DOI=10.1097/00001756-199412000-00055;
RA   Nutt S.L., Kamboj R.K.;
RT   "RNA editing of human kainate receptor subunits.";
RL   NeuroReport 5:2625-2629(1994).
RN   [5]
RP   VARIANTS VAL-332; GLN-862 AND SER-902.
RX   PubMed=11702055; DOI=10.1097/00041444-200109000-00005;
RA   Shibata H., Joo A., Fujii Y., Tani A., Makino C., Hirata N., Kikuta R.,
RA   Ninomiya H., Tashiro N., Fukumaki Y.;
RT   "Association study of polymorphisms in the GluR5 kainate receptor gene
RT   (GRIK1) with schizophrenia.";
RL   Psychiatr. Genet. 11:139-144(2001).
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. May be involved
CC       in the transmission of light information from the retina to the
CC       hypothalamus.
CC   -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC       receptor subunits. Tetramers may be formed by the dimerization of
CC       dimers (Probable). The unedited version (Q) assembles into a functional
CC       kainate-gated homomeric channel, whereas the edited version (R) is
CC       unable to produce channel activity when expressed alone. Both edited
CC       and unedited versions can form functional channels with GRIK4 and
CC       GRIK5. Interacts with KLHL17 (By similarity). {ECO:0000250,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Postsynaptic cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=GluR5-1D;
CC         IsoId=P39086-1; Sequence=Displayed;
CC       Name=2; Synonyms=EAA3A;
CC         IsoId=P39086-2; Sequence=VSP_000127, VSP_000128;
CC   -!- TISSUE SPECIFICITY: Most abundant in the cerebellum and the
CC       suprachiasmatic nuclei (SCN) of the hypothalamus.
CC   -!- RNA EDITING: Modified_positions=636 {ECO:0000269|PubMed:7696618};
CC       Note=Partially edited.;
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 domoate > kainate > L-glutamate =
CC       quisqualate > CNQX = DNQX > AMPA > dihydrokainate > NMDA.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. GRIK1 subfamily. {ECO:0000305}.
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DR   EMBL; L19058; AAA52568.1; -; mRNA.
DR   EMBL; U16125; AAA95961.1; -; mRNA.
DR   EMBL; AJ249208; CAC80546.1; -; mRNA.
DR   CCDS; CCDS33530.1; -. [P39086-2]
DR   CCDS; CCDS42913.1; -. [P39086-1]
DR   PIR; I58178; I58178.
DR   RefSeq; NP_000821.1; NM_000830.4. [P39086-1]
DR   RefSeq; NP_001307545.1; NM_001320616.1.
DR   RefSeq; NP_001307547.1; NM_001320618.1.
DR   RefSeq; NP_783300.1; NM_175611.2. [P39086-2]
DR   PDB; 2ZNS; X-ray; 2.00 A; A=445-559, A=682-820.
DR   PDB; 2ZNT; X-ray; 1.60 A; A=445-559, A=682-820.
DR   PDB; 2ZNU; X-ray; 1.80 A; A=445-559, A=682-820.
DR   PDB; 3FUZ; X-ray; 1.65 A; A/B=445-559, A/B=682-820.
DR   PDB; 3FV1; X-ray; 1.50 A; A/B=445-559, A/B=682-820.
DR   PDB; 3FV2; X-ray; 1.50 A; A/B=445-559, A/B=682-820.
DR   PDB; 3FVG; X-ray; 1.50 A; A/B=445-559, A/B=682-820.
DR   PDB; 3FVK; X-ray; 1.50 A; A/B=445-559, A/B=682-820.
DR   PDB; 3FVN; X-ray; 1.50 A; A/B=445-559, A/B=682-820.
DR   PDB; 3FVO; X-ray; 1.50 A; A/B=445-559, A/B=682-820.
DR   PDB; 4MF3; X-ray; 3.00 A; A/B=443-559, A/B=682-822.
DR   PDBsum; 2ZNS; -.
DR   PDBsum; 2ZNT; -.
DR   PDBsum; 2ZNU; -.
DR   PDBsum; 3FUZ; -.
DR   PDBsum; 3FV1; -.
DR   PDBsum; 3FV2; -.
DR   PDBsum; 3FVG; -.
DR   PDBsum; 3FVK; -.
DR   PDBsum; 3FVN; -.
DR   PDBsum; 3FVO; -.
DR   PDBsum; 4MF3; -.
DR   AlphaFoldDB; P39086; -.
DR   SMR; P39086; -.
DR   BioGRID; 109154; 14.
DR   IntAct; P39086; 22.
DR   MINT; P39086; -.
DR   STRING; 9606.ENSP00000327687; -.
DR   BindingDB; P39086; -.
DR   ChEMBL; CHEMBL1918; -.
DR   DrugBank; DB00237; Butabarbital.
DR   DrugBank; DB00142; Glutamic acid.
DR   DrugBank; DB06354; Tezampanel.
DR   DrugBank; DB00273; Topiramate.
DR   DrugCentral; P39086; -.
DR   GuidetoPHARMACOLOGY; 450; -.
DR   GlyCosmos; P39086; 9 sites, No reported glycans.
DR   GlyGen; P39086; 9 sites.
DR   iPTMnet; P39086; -.
DR   PhosphoSitePlus; P39086; -.
DR   BioMuta; GRIK1; -.
DR   DMDM; 729597; -.
DR   MassIVE; P39086; -.
DR   PaxDb; 9606-ENSP00000382791; -.
DR   PeptideAtlas; P39086; -.
DR   ProteomicsDB; 55314; -. [P39086-1]
DR   ProteomicsDB; 55315; -. [P39086-2]
DR   Antibodypedia; 22450; 316 antibodies from 36 providers.
DR   DNASU; 2897; -.
DR   Ensembl; ENST00000389125.7; ENSP00000373777.3; ENSG00000171189.18. [P39086-2]
DR   Ensembl; ENST00000399907.6; ENSP00000382791.1; ENSG00000171189.18. [P39086-1]
DR   GeneID; 2897; -.
DR   KEGG; hsa:2897; -.
DR   UCSC; uc002ynn.4; human. [P39086-1]
DR   AGR; HGNC:4579; -.
DR   CTD; 2897; -.
DR   DisGeNET; 2897; -.
DR   GeneCards; GRIK1; -.
DR   HGNC; HGNC:4579; GRIK1.
DR   HPA; ENSG00000171189; Group enriched (adrenal gland, brain, retina).
DR   MIM; 138245; gene.
DR   neXtProt; NX_P39086; -.
DR   OpenTargets; ENSG00000171189; -.
DR   PharmGKB; PA28973; -.
DR   VEuPathDB; HostDB:ENSG00000171189; -.
DR   eggNOG; KOG1052; Eukaryota.
DR   GeneTree; ENSGT00940000156253; -.
DR   HOGENOM; CLU_007257_1_2_1; -.
DR   InParanoid; P39086; -.
DR   OMA; TMDMELF; -.
DR   OrthoDB; 511851at2759; -.
DR   PhylomeDB; P39086; -.
DR   TreeFam; TF334668; -.
DR   PathwayCommons; P39086; -.
DR   Reactome; R-HSA-451307; Activation of Na-permeable kainate receptors.
DR   Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
DR   SignaLink; P39086; -.
DR   SIGNOR; P39086; -.
DR   BioGRID-ORCS; 2897; 17 hits in 1149 CRISPR screens.
DR   ChiTaRS; GRIK1; human.
DR   EvolutionaryTrace; P39086; -.
DR   GeneWiki; GRIK1; -.
DR   GenomeRNAi; 2897; -.
DR   Pharos; P39086; Tclin.
DR   PRO; PR:P39086; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P39086; Protein.
DR   Bgee; ENSG00000171189; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 134 other cell types or tissues.
DR   ExpressionAtlas; P39086; baseline and differential.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0032983; C:kainate selective glutamate receptor complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR   GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:UniProtKB.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR   GO; GO:0007215; P:glutamate receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; TAS:UniProtKB.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   CDD; cd06382; PBP1_iGluR_Kainate; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR18966:SF36; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 1; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
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; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   Genevisible; P39086; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Glycoprotein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW   RNA editing; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..918
FT                   /note="Glutamate receptor ionotropic, kainate 1"
FT                   /id="PRO_0000011541"
FT   TOPO_DOM        31..576
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        598..653
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        654..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        675..834
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        835..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        856..918
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         531..533
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         538
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         704..705
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         753
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         725
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         761
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        561
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        766
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         402..416
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8589992, ECO:0000303|Ref.3"
FT                   /id="VSP_000127"
FT   VAR_SEQ         870..918
FT                   /note="AFCFFYGLQCKQTHPTNSTSGTTLSTDLECGKLIREERGIRKQSSVHTV ->
FT                   CLSFNAIMEELGISLKNQKKIKKKSRTKGKSSFTSILTCHQRRTQRKETVA (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8589992, ECO:0000303|Ref.3"
FT                   /id="VSP_000128"
FT   VARIANT         332
FT                   /note="A -> V (in dbSNP:rs143252117)"
FT                   /evidence="ECO:0000269|PubMed:11702055"
FT                   /id="VAR_012751"
FT   VARIANT         636
FT                   /note="Q -> R (in RNA edited version)"
FT                   /id="VAR_000304"
FT   VARIANT         757
FT                   /note="I -> V (in dbSNP:rs363494)"
FT                   /id="VAR_012041"
FT   VARIANT         862
FT                   /note="R -> Q (in dbSNP:rs761410270)"
FT                   /evidence="ECO:0000269|PubMed:11702055"
FT                   /id="VAR_012752"
FT   VARIANT         870
FT                   /note="A -> V (in dbSNP:rs363503)"
FT                   /id="VAR_012042"
FT   VARIANT         902
FT                   /note="L -> S (in dbSNP:rs363504)"
FT                   /evidence="ECO:0000269|PubMed:11702055"
FT                   /id="VAR_012043"
FT   CONFLICT        281
FT                   /note="R -> G (in Ref. 2; AAA95961)"
FT                   /evidence="ECO:0000305"
FT   STRAND          449..453
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   TURN            457..459
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          460..462
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           471..474
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           478..490
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          494..498
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           515..521
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          526..528
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           536..539
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          542..544
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          548..551
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          553..559
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           686..691
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          693..698
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           704..711
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           715..726
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           728..731
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          732..735
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           736..745
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          746..753
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           754..761
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          767..771
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          777..779
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   STRAND          782..784
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           790..802
FT                   /evidence="ECO:0007829|PDB:3FV1"
FT   HELIX           805..814
FT                   /evidence="ECO:0007829|PDB:3FV1"
SQ   SEQUENCE   918 AA;  103981 MW;  0EB8DB6356599002 CRC64;
     MEHGTLLAQP GLWTRDTSWA LLYFLCYILP QTAPQVLRIG GIFETVENEP VNVEELAFKF
     AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ
     SICNALEVPH IQTRWKHPSV DNKDLFYINL YPDYAAISRA ILDLVLYYNW KTVTVVYEDS
     TGLIRLQELI KAPSRYNIKI KIRQLPSGNK DAKPLLKEMK KGKEFYVIFD CSHETAAEIL
     KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RLLNIDNPHV SSIIEKWSME
     RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPWRLGPRF
     MNLIKEARWD GLTGHITFNK TNGLRKDFDL DIISLKEEGT EKAAGEVSKH LYKVWKKIGI
     WNSNSGLNMT DSNKDKSSNI TDSLANRTLI VTTILEEPYV MYRKSDKPLY GNDRFEGYCL
     DLLKELSNIL GFIYDVKLVP DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK
     VIDFSKPFMT LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT
     PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL
     IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV RDGSTMTFFK KSKISTYEKM
     WAFMSSRQQT ALVRNSDEGI QRVLTTDYAL LMESTSIEYV TQRNCNLTQI GGLIDSKGYG
     VGTPIGSPYR DKITIAILQL QEEGKLHMMK EKWWRGNGCP EEDNKEASAL GVENIGGIFI
     VLAAGLVLSV FVAIGEFIYK SRKNNDIEQA FCFFYGLQCK QTHPTNSTSG TTLSTDLECG
     KLIREERGIR KQSSVHTV
//