GRIK1_MOUSE
ID GRIK1_MOUSE Reviewed; 836 AA.
AC Q60934;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Glutamate receptor ionotropic, kainate 1;
DE Short=GluK1;
DE AltName: Full=Glutamate receptor 5;
DE Short=GluR-5;
DE Short=GluR5;
DE Flags: Precursor;
GN Name=Grik1; Synonyms=Glur5;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
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 [GENOMIC DNA] OF 584-695, AND RNA EDITING OF POSITION
RP 621.
RC STRAIN=BALB/cJ;
RX PubMed=8700852; DOI=10.1073/pnas.93.5.1875;
RA Herb A., Higuchi M., Sprengel R., Seeburg P.H.;
RT "Q/R site editing in kainate receptor GluR5 and GluR6 pre-mRNAs requires
RT distant intronic sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1875-1880(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 606-622, AND RNA EDITING OF POSITION 621.
RX PubMed=1717158; DOI=10.1016/0092-8674(91)90568-j;
RA Sommer B., Koehler M., Sprengel R., Seeburg P.H.;
RT "RNA editing in brain controls a determinant of ion flow in glutamate-gated
RT channels.";
RL Cell 67:11-19(1991).
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 (By similarity). {ECO:0000250}.
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=1;
CC Comment=At least 2 isoforms are produced.;
CC Name=1;
CC IsoId=Q60934-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Most abundant in the cerebellum. Also present in
CC the suprachiasmatic nuclei of the hypothalamus.
CC -!- RNA EDITING: Modified_positions=621 {ECO:0000269|PubMed:1717158,
CC ECO:0000269|PubMed:8700852}; 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 (By
CC similarity). {ECO:0000250}.
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; X66118; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U31444; AAA85222.1; -; Genomic_DNA.
DR PIR; A41053; A41053.
DR AlphaFoldDB; Q60934; -.
DR SMR; Q60934; -.
DR GlyGen; Q60934; 8 sites.
DR iPTMnet; Q60934; -.
DR PhosphoSitePlus; Q60934; -.
DR PaxDb; Q60934; -.
DR PRIDE; Q60934; -.
DR ProteomicsDB; 269831; -. [Q60934-1]
DR UCSC; uc007zuw.2; mouse. [Q60934-1]
DR MGI; MGI:95814; Grik1.
DR eggNOG; KOG1052; Eukaryota.
DR InParanoid; Q60934; -.
DR Reactome; R-MMU-451307; Activation of Na-permeable kainate receptors.
DR Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
DR ChiTaRS; Grik1; mouse.
DR PRO; PR:Q60934; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60934; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; ISO:MGI.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; IPI:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; ISO:MGI.
DR GO; GO:0016595; F:glutamate binding; ISO:MGI.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; ISO:MGI.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:MGI.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IMP:MGI.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
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:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:MGI.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISO:MGI.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IGI:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; IMP:MGI.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IMP:MGI.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IGI:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; TAS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
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; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; RNA editing;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..836
FT /note="Glutamate receptor ionotropic, kainate 1"
FT /id="PRO_0000011542"
FT TOPO_DOM 31..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..721
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..836
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 516..518
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 689..690
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
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 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 621
FT /note="Q -> R (in RNA edited version)"
SQ SEQUENCE 836 AA; 95202 MW; A8B6EC4B44FFDBFF CRC64;
MERGTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP VNVEELAFKF
AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ
SICNALEVPH IQTRWKHPSV DNRDLFYINL YPDYAAISRA VLDLVLYYNW KTVTVVYEDS
TGLIRLQELI KAPSRYNIKI KIRQLPSGNK DAKPLLKEMK KGKEFYVIFD CSHETAAEIL
KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RLLNIDNPHV SSIIEKWSME
RLQAPPRPET GLLDGVMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPWRLGPRF
MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT EKIGIWNSNS GLNMTDGNRD
RSNNITDSLA NRTLIVTTIL EEPYVMYRKS DKPLYGNDRF EGYCLDLLKE LSNILGFLYD
VKLVPDGKYG AQNDKGEWNG MVKELIDHRA DLAVAPLTIT YVREKVIDFS KPFMTLGISI
LYRKPNGTNP GVFSFLNPLS PDIWMYVLLA CLGVSCVLFV IARFTPYEWY NPHPCNPDSD
VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS YTANLAAFLT
VERMESPIDS ADDLAKQTKI EYGAVRDGST MTFFKKSKIS TYEKMWAFMS SRQPSALGVE
NIGGIFIVLA AGLVLSVFVA IGEFIYKSRK NNDIEQKGKS SRLRFYFRNK VRFHGSKTES
LGVEKCLSFN AIMEELGISL KNQKKIKKKS RTKGKSSFTS ILTCHQRRTQ RKETVA
