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   27-MAR-2024, entry version 203.
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.
DR   RefSeq; XP_011525165.1; XM_011526863.2.
DR   AlphaFoldDB; Q16478; -.
DR   SMR; Q16478; -.
DR   BioGRID; 109158; 15.
DR   IntAct; Q16478; 4.
DR   STRING; 9606.ENSP00000301218; -.
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   GlyCosmos; Q16478; 11 sites, No reported glycans.
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; 9606-ENSP00000262895; -.
DR   PeptideAtlas; Q16478; -.
DR   Antibodypedia; 30879; 253 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   AGR; HGNC:4583; -.
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; TSANIWQ; -.
DR   OrthoDB; 511851at2759; -.
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 1151 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 183 other cell types or tissues.
DR   ExpressionAtlas; Q16478; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0032983; C:kainate selective glutamate receptor complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
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: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   CDD; cd06394; PBP1_iGluR_Kainate_KA1_2; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 3.
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:SF351; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 5; 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; Q16478; HS.
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
//