GRIK5_HUMAN
ID GRIK5_HUMAN Reviewed; 980 AA.
AC Q16478; Q8WWG8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Glutamate receptor ionotropic, kainate 5;
DE Short=GluK5;
DE AltName: Full=Excitatory amino acid receptor 2;
DE Short=EAA2;
DE AltName: Full=Glutamate receptor KA-2;
DE Short=KA2;
DE Flags: Precursor;
GN Name=GRIK5; Synonyms=GRIK2;
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=Hippocampus;
RX PubMed=1321949;
RA Kamboj R.K., Schoepp D.D., Nutt S., Shekter L., Korczak B., True R.A.,
RA Zimmerman D.M., Wosnick M.A.;
RT "Molecular structure and pharmacological characterization of humEAA2, a
RT novel human kainate receptor subunit.";
RL Mol. Pharmacol. 42:10-15(1992).
RN [2]
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 [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for glutamate. 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 kainate > quisqualate > domoate > L-glutamate >> AMPA >> NMDA = 1S,3R-
CC ACPD.
CC -!- SUBUNIT: Tetramer of two or more different subunits. Associates with
CC GRIK1 (both edited and unedited versions), GRIK2, or GRIK3 to form
CC functional channels. Homomeric associations do not produce any channel
CC activity (By similarity). {ECO:0000250}.
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 Name=1;
CC IsoId=Q16478-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16478-2; Sequence=VSP_035585;
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIK5 subfamily. {ECO:0000305}.
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DR EMBL; S40369; AAB22591.1; -; mRNA.
DR EMBL; AJ249209; CAC80547.1; -; mRNA.
DR EMBL; CH471126; EAW57090.1; -; Genomic_DNA.
DR CCDS; CCDS12595.1; -. [Q16478-1]
DR CCDS; CCDS77305.1; -. [Q16478-2]
DR PIR; I57936; I57936.
DR RefSeq; NP_001287959.1; NM_001301030.1. [Q16478-2]
DR RefSeq; NP_002079.3; NM_002088.4. [Q16478-1]
DR RefSeq; XP_005258878.1; XM_005258821.3. [Q16478-1]
DR RefSeq; XP_011525165.1; XM_011526863.2. [Q16478-2]
DR AlphaFoldDB; Q16478; -.
DR SMR; Q16478; -.
DR BioGRID; 109158; 13.
DR IntAct; Q16478; 4.
DR STRING; 9606.ENSP00000262895; -.
DR BindingDB; Q16478; -.
DR ChEMBL; CHEMBL2675; -.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00273; Topiramate.
DR DrugCentral; Q16478; -.
DR TCDB; 1.A.10.1.28; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; Q16478; 11 sites.
DR iPTMnet; Q16478; -.
DR PhosphoSitePlus; Q16478; -.
DR BioMuta; GRIK5; -.
DR DMDM; 209572626; -.
DR jPOST; Q16478; -.
DR MassIVE; Q16478; -.
DR PaxDb; Q16478; -.
DR PeptideAtlas; Q16478; -.
DR PRIDE; Q16478; -.
DR Antibodypedia; 30879; 224 antibodies from 33 providers.
DR DNASU; 2901; -.
DR Ensembl; ENST00000262895.7; ENSP00000262895.2; ENSG00000105737.10. [Q16478-1]
DR Ensembl; ENST00000301218.8; ENSP00000301218.3; ENSG00000105737.10. [Q16478-2]
DR Ensembl; ENST00000593562.6; ENSP00000470251.1; ENSG00000105737.10. [Q16478-1]
DR GeneID; 2901; -.
DR KEGG; hsa:2901; -.
DR MANE-Select; ENST00000593562.6; ENSP00000470251.1; NM_002088.5; NP_002079.3.
DR UCSC; uc002osj.3; human. [Q16478-1]
DR CTD; 2901; -.
DR DisGeNET; 2901; -.
DR GeneCards; GRIK5; -.
DR HGNC; HGNC:4583; GRIK5.
DR HPA; ENSG00000105737; Tissue enhanced (brain, testis).
DR MIM; 600283; gene.
DR neXtProt; NX_Q16478; -.
DR OpenTargets; ENSG00000105737; -.
DR PharmGKB; PA28977; -.
DR VEuPathDB; HostDB:ENSG00000105737; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000158852; -.
DR HOGENOM; CLU_007257_1_0_1; -.
DR InParanoid; Q16478; -.
DR OMA; PFYLEFV; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q16478; -.
DR TreeFam; TF334668; -.
DR PathwayCommons; Q16478; -.
DR Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
DR SignaLink; Q16478; -.
DR SIGNOR; Q16478; -.
DR BioGRID-ORCS; 2901; 14 hits in 1071 CRISPR screens.
DR ChiTaRS; GRIK5; human.
DR GeneWiki; GRIK5; -.
DR GenomeRNAi; 2901; -.
DR Pharos; Q16478; Tclin.
DR PRO; PR:Q16478; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q16478; protein.
DR Bgee; ENSG00000105737; Expressed in olfactory bulb and 181 other tissues.
DR ExpressionAtlas; Q16478; baseline and differential.
DR Genevisible; Q16478; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
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:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0006621; P:protein retention in ER lumen; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IEA:Ensembl.
DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..980
FT /note="Glutamate receptor ionotropic, kainate 5"
FT /id="PRO_0000011552"
FT TOPO_DOM 15..544
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..803
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 825..980
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 891..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..292
FT /evidence="ECO:0000250"
FT DISULFID 83..334
FT /evidence="ECO:0000250"
FT DISULFID 165..170
FT /evidence="ECO:0000250"
FT VAR_SEQ 839..980
FT /note="VSVCQEMLQELRHAVSCRKTSRSRRRRRPGGPSRALLSLRAVREMRLSNGKL
FT YSAGAGGDAGSAHGGPQRLLDDPGPPSGARPAAPTPCTHVRVCQECRRIQALRASGAGA
FT PPRGLGVPAEATSPPRPRPGPAGPRELAEHE -> TPALHPAACQCSALGPRTPLKEPS
FT MLLVKVPSTRVQVAFSRTSLRQVCPFLLQHQLSSLYWIQATNVQICCHFSSLKPSPDLT
FT FPPSHRPLSSLLFTALAAVGGLPDASSFFFPPISSCPPLQSGIGPCHSTEATLVTSNFH
FT V (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_035585"
FT CONFLICT 436
FT /note="A -> G (in Ref. 1; AAB22591)"
FT /evidence="ECO:0000305"
FT CONFLICT 459..461
FT /note="RFR -> PFP (in Ref. 1; AAB22591)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="R -> A (in Ref. 1; AAB22591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 109265 MW; 72466FFF64079388 CRC64;
MPAELLLLLI VAFASPSCQV LSSLRMAAIL DDQTVCGRGE RLALALAREQ INGIIEVPAK
ARVEVDIFEL QRDSQYETTD TMCQILPKGV VSVLGPSSSP ASASTVSHIC GEKEIPHIKV
GPEETPRLQY LRFASVSLYP SNEDVSLAVS RILKSFNYPS ASLICAKAEC LLRLEELVRG
FLISKETLSV RMLDDSRDPT PLLKEIRDDK VSTIIIDANA SISHLILRKA SELGMTSAFY
KYILTTMDFP ILHLDGIVED SSNILGFSMF NTSHPFYPEF VRSLNMSWRE NCEASTYLGP
ALSAALMFDA VHVVVSAVRE LNRSQEIGVK PLACTSANIW PHGTSLMNYL RMVEYDGLTG
RVEFNSKGQR TNYTLRILEK SRQGHREIGV WYSNRTLAMN ATTLDINLSQ TLANKTLVVT
TILENPYVMR RPNFQALSGN ERFEGFCVDM LRELAELLRF RYRLRLVEDG LYGAPEPNGS
WTGMVGELIN RKADLAVAAF TITAEREKVI DFSKPFMTLG ISILYRVHMG RKPGYFSFLD
PFSPAVWLFM LLAYLAVSCV LFLAARLSPY EWYNPHPCLR ARPHILENQY TLGNSLWFPV
GGFMQQGSEI MPRALSTRCV SGVWWAFTLI IISSYTANLA AFLTVQRMEV PVESADDLAD
QTNIEYGTIH AGSTMTFFQN SRYQTYQRMW NYMQSKQPSV FVKSTEEGIA RVLNSRYAFL
LESTMNEYHR RLNCNLTQIG GLLDTKGYGI GMPLGSPFRD EITLAILQLQ ENNRLEILKR
KWWEGGRCPK EEDHRAKGLG MENIGGIFIV LICGLIIAVF VAVMEFIWST RRSAESEEVS
VCQEMLQELR HAVSCRKTSR SRRRRRPGGP SRALLSLRAV REMRLSNGKL YSAGAGGDAG
SAHGGPQRLL DDPGPPSGAR PAAPTPCTHV RVCQECRRIQ ALRASGAGAP PRGLGVPAEA
TSPPRPRPGP AGPRELAEHE
