GRIK4_MOUSE
ID GRIK4_MOUSE Reviewed; 956 AA.
AC Q8BMF5; E9QNA2;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Glutamate receptor ionotropic, kainate 4;
DE Short=GluK4;
DE Flags: Precursor;
GN Name=Grik4;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a heteromeric channel with GRIK1 or GRIK3.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIK4 subfamily. {ECO:0000305}.
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DR EMBL; AK032029; BAC27660.1; -; mRNA.
DR EMBL; AC122449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23089.1; -.
DR RefSeq; NP_780690.2; NM_175481.5.
DR RefSeq; XP_006510004.1; XM_006509941.3.
DR RefSeq; XP_011240685.1; XM_011242383.2.
DR AlphaFoldDB; Q8BMF5; -.
DR SMR; Q8BMF5; -.
DR BioGRID; 225773; 2.
DR STRING; 10090.ENSMUSP00000110515; -.
DR GlyGen; Q8BMF5; 9 sites.
DR PhosphoSitePlus; Q8BMF5; -.
DR SwissPalm; Q8BMF5; -.
DR EPD; Q8BMF5; -.
DR PaxDb; Q8BMF5; -.
DR PRIDE; Q8BMF5; -.
DR ProteomicsDB; 269631; -.
DR Antibodypedia; 32769; 158 antibodies from 29 providers.
DR DNASU; 110637; -.
DR Ensembl; ENSMUST00000034515; ENSMUSP00000034515; ENSMUSG00000032017.
DR Ensembl; ENSMUST00000114865; ENSMUSP00000110515; ENSMUSG00000032017.
DR GeneID; 110637; -.
DR KEGG; mmu:110637; -.
DR UCSC; uc009paz.2; mouse.
DR CTD; 2900; -.
DR MGI; MGI:95817; Grik4.
DR VEuPathDB; HostDB:ENSMUSG00000032017; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000159111; -.
DR HOGENOM; CLU_007257_1_0_1; -.
DR InParanoid; Q8BMF5; -.
DR OMA; PAXVELE; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q8BMF5; -.
DR TreeFam; TF334668; -.
DR Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
DR BioGRID-ORCS; 110637; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Grik4; mouse.
DR PRO; PR:Q8BMF5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BMF5; protein.
DR Bgee; ENSMUSG00000032017; Expressed in dentate gyrus of hippocampal formation granule cell and 38 other tissues.
DR Genevisible; Q8BMF5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
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:0032983; C:kainate selective glutamate receptor complex; IPI:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IBA:GO_Central.
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:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
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 Cell membrane; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..956
FT /note="Glutamate receptor ionotropic, kainate 4"
FT /id="PRO_0000042577"
FT TOPO_DOM 21..545
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..804
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 805..825
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 931..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 874
FT /note="P -> Q (in Ref. 1; BAC27660)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="P -> T (in Ref. 1; BAC27660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 107264 MW; 0B1E388C290BA093 CRC64;
MPRVSAPLVL LPAWLLMVAC SPHSLRIAAI LDDPMECSRG ERLSITLAKN RINRAPERLG
KAKVEVDIFE LLRDSEYETA ETMCQILPKG VVAVLGPSSS PASSSIISNI CGEKEVPHFK
VAPEEFVRFQ LQRFTTLNLH PSNTDISVAV AGILNFFNCT TACLICAKAE CLLNLEKLLR
QFLISKDTLS VRMLDDTRDP TPLLKEIRDD KTATIIIHAN ASMSHTILLK AAELGMVSAY
YTYIFTNLEF SLQRMDSLVD DRVNILGFSI FNQSHAFFQE FSQSLNQSWQ ENCDHVPFTG
PALSSALLFD AVYAVVTAVQ ELNRSQEIGV KPLSCGSAQI WQHGTSLMNY LRMVELEGLT
GHIEFNSKGQ RSNYALKILQ FTRNGFQQIG QWHVAEGLSM DSRLYASNIS DSLFNTTLVV
TTILENPYLM LKGNHQEMEG NDRYEGFCVD MLKELAEILR FNYKIRLVGD GVYGVPEANG
TWTGMVGELI ARKADLAVAG LTITAEREKV IDFSKPFMTL GISILYRVHM GRRPGYFSFL
DPFSPGVWLF MLLAYLAVSC VLFLVARLTP YEWYSPHPCA QGRCNLLVNQ YSLGNSLWFP
VGGFMQQGST IAPRALSTRC VSGVWWAFTL IIISSYTANL AAFLTVQRME VPIESVDDLA
DQTAIEYGTI HGGSSMTFFQ NSRYQTYQRM WNYMYSKQPS VFVKSTEEGI ARVLNSNYAF
LLESTMNEYY RQRNCNLTQI GGLLDTKGYG IGMPVGSVFR DEFDLAILQL QENNRLEILK
RKWWEGGKCP KEEDHRAKGL GMENIGGIFV VLICGLIVAI FMAMLEFLWT LRHSEASEVS
VCQEMVTELR NIILCQDNIH PRRRRSGGLP PQPPVLEERR PRGTATLSNG KLCGAGEPDQ
LAQRLAQEAA LVARGCTHIR VCPECRRFQG LRARPSPARS EESLEWDKTT NSSEPE
