GRIK5_RAT
ID GRIK5_RAT Reviewed; 979 AA.
AC Q63273; Q62643;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Glutamate receptor ionotropic, kainate 5;
DE Short=GluK5;
DE AltName: Full=Glutamate receptor KA-2;
DE Short=KA2;
DE Flags: Precursor;
GN Name=Grik5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1373632; DOI=10.1016/0896-6273(92)90098-x;
RA Herb A., Burnashev N., Werner P., Sakmann B., Wisden W., Seeburg P.H.;
RT "The KA-2 subunit of excitatory amino acid receptors shows widespread
RT expression in brain and forms ion channels with distantly related
RT subunits.";
RL Neuron 8:775-785(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Boulter J., Pecht G.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 20-406, GLYCOSYLATION AT ASN-219;
RP ASN-271; ASN-285; ASN-322 AND ASN-372, AND DISULFIDE BONDS.
RX PubMed=20951142; DOI=10.1016/j.jmb.2010.10.006;
RA Kumar J., Mayer M.L.;
RT "Crystal structures of the glutamate receptor ion channel GluK3 and GluK5
RT amino-terminal domains.";
RL J. Mol. Biol. 404:680-696(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 20-406 IN COMPLEX WITH GRIK2,
RP DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=21791290; DOI=10.1016/j.neuron.2011.05.038;
RA Kumar J., Schuck P., Mayer M.L.;
RT "Structure and assembly mechanism for heteromeric kainate receptors.";
RL Neuron 71:319-331(2011).
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 > glutamate >> AMPA.
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. {ECO:0000269|PubMed:21791290}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: High expression in the cerebral cortex, pyriform
CC cortex, caudate-putamen, hippocampal complex, medial habenulata and
CC granule cell layer of the cerebellum. Weak expression in globus
CC pallidus, thalamus, colliculi and the reticular thalamic nucleus.
CC -!- DEVELOPMENTAL STAGE: From embryonic day 14 through postnatal day 1,
CC high expression in spinal cord, brain and some areas of the PNS. At E17
CC and E19, high expression in spinal cord, mesencephalon and
CC telencephalic structures as in olfactory neurons and in nasal
CC epithelium. Strong expression also in the pituitary.
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; Z11581; CAA77667.1; -; mRNA.
DR EMBL; U08258; AAA17831.1; -; mRNA.
DR PIR; JH0592; JH0592.
DR RefSeq; NP_113696.1; NM_031508.2.
DR PDB; 3OM0; X-ray; 1.40 A; A=20-406.
DR PDB; 3OM1; X-ray; 1.68 A; A/B=20-406.
DR PDB; 3QLU; X-ray; 2.91 A; A/B=20-406.
DR PDB; 3QLV; X-ray; 3.94 A; A/B/E/G/I=20-406.
DR PDB; 7KS0; EM; 5.30 A; A/C=1-827.
DR PDB; 7KS3; EM; 5.80 A; A/C=1-827.
DR PDBsum; 3OM0; -.
DR PDBsum; 3OM1; -.
DR PDBsum; 3QLU; -.
DR PDBsum; 3QLV; -.
DR PDBsum; 7KS0; -.
DR PDBsum; 7KS3; -.
DR AlphaFoldDB; Q63273; -.
DR SMR; Q63273; -.
DR BioGRID; 246572; 2.
DR STRING; 10116.ENSRNOP00000027578; -.
DR BindingDB; Q63273; -.
DR ChEMBL; CHEMBL4041; -.
DR DrugCentral; Q63273; -.
DR GlyGen; Q63273; 11 sites.
DR iPTMnet; Q63273; -.
DR PhosphoSitePlus; Q63273; -.
DR PaxDb; Q63273; -.
DR ABCD; Q63273; 1 sequenced antibody.
DR GeneID; 24407; -.
DR KEGG; rno:24407; -.
DR UCSC; RGD:2735; rat.
DR CTD; 2901; -.
DR RGD; 2735; Grik5.
DR VEuPathDB; HostDB:ENSRNOG00000020310; -.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007257_1_0_1; -.
DR InParanoid; Q63273; -.
DR OMA; PFYLEFV; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q63273; -.
DR TreeFam; TF334668; -.
DR Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
DR PRO; PR:Q63273; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020310; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q63273; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:UniProtKB.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0008066; F:glutamate receptor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IMP:UniProtKB.
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; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0006621; P:protein retention in ER lumen; IMP:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
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 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW 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..979
FT /note="Glutamate receptor ionotropic, kainate 5"
FT /id="PRO_0000011554"
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..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 856..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20951142"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20951142"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20951142"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20951142"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20951142"
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 DISULFID 83..334
FT DISULFID 165..170
FT CONFLICT 887
FT /note="N -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="K -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="D -> N (in Ref. 2; AAA17831)"
FT /evidence="ECO:0000305"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3OM1"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3QLU"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:3OM1"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:3OM0"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:3QLU"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:3OM0"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:3OM0"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 302..321
FT /evidence="ECO:0007829|PDB:3OM0"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:3OM0"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:3OM0"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:3OM0"
SQ SEQUENCE 979 AA; 109276 MW; 313E2862746474B1 CRC64;
MPAELLLLLI VAFANPSCQV LSSLRMAAIL DDQTVCGRGE RLALALAREQ INGIIEVPAK
ARVEVDIFEL QRDSQYETTD TMCQILPKGV VSVLGPSSSP ASASTVSHIC GEKEIPHIKV
GPEETPRLQY LRFASVSLYP SNEDVSLAVS RILKSFNYPS ASLICAKAEC LLRLEELVRG
FLISKETLSV RMLDDSRDPT PLLKEIRDDK VSTIIIDANA SISHLVLRKA SELGMTSAFY
KYILTTMDFP ILHLDGIVED SSNILGFSMF NTSHPFYPEF VRSLNMSWRE NCEASTYPGP
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 MENIGGIFVV LICGLIIAVF VAVMEFIWST RRSAESEEVS
VCQEMLQELR HAVSCRKTSR SRRRRRPGGP SRALLSLRAV REMRLSNGKL YSAGAGGDAG
AHGGPQRLLD DPGPPGGPRP QAPTPCTHVR VCQECRRIQA LRASGAGAPP RGLGTPAEAT
SPPRPRPGPT GPRELTEHE
