GRIK4_HUMAN
ID GRIK4_HUMAN Reviewed; 956 AA.
AC Q16099; A8K9L1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Glutamate receptor ionotropic, kainate 4;
DE Short=GluK4;
DE AltName: Full=Excitatory amino acid receptor 1;
DE Short=EAA1;
DE AltName: Full=Glutamate receptor KA-1;
DE Short=KA1;
DE Flags: Precursor;
GN Name=GRIK4; Synonyms=GRIK;
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], AND VARIANT ILE-528.
RC TISSUE=Hippocampus;
RX PubMed=8263508; DOI=10.1046/j.1471-4159.1994.62010001.x;
RA Kamboj R.K., Schoepp D.D., Nutt S., Shekter L., Korczak B., True R.A.,
RA Rampersad V., Zimmerman D.M., Wosnick M.A.;
RT "Molecular cloning, expression, and pharmacological characterization of
RT humEAA1, a human kainate receptor subunit.";
RL J. Neurochem. 62:1-9(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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.
CC -!- SUBUNIT: Forms a heteromeric channel with GRIK1 or GRIK3.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
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; S67803; AAB29311.1; -; mRNA.
DR EMBL; AK292726; BAF85415.1; -; mRNA.
DR EMBL; CH471065; EAW67512.1; -; Genomic_DNA.
DR CCDS; CCDS8433.1; -.
DR PIR; JH0826; JH0826.
DR RefSeq; NP_001269399.1; NM_001282470.2.
DR RefSeq; NP_055434.2; NM_014619.4.
DR AlphaFoldDB; Q16099; -.
DR SMR; Q16099; -.
DR BioGRID; 109157; 3.
DR STRING; 9606.ENSP00000435648; -.
DR BindingDB; Q16099; -.
DR ChEMBL; CHEMBL2109241; -.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00273; Topiramate.
DR DrugCentral; Q16099; -.
DR TCDB; 1.A.10.1.9; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; Q16099; 9 sites.
DR iPTMnet; Q16099; -.
DR PhosphoSitePlus; Q16099; -.
DR BioMuta; GRIK4; -.
DR DMDM; 209572625; -.
DR MassIVE; Q16099; -.
DR PaxDb; Q16099; -.
DR PeptideAtlas; Q16099; -.
DR PRIDE; Q16099; -.
DR ProteomicsDB; 60831; -.
DR Antibodypedia; 32769; 158 antibodies from 29 providers.
DR DNASU; 2900; -.
DR Ensembl; ENST00000438375.2; ENSP00000404063.2; ENSG00000149403.13.
DR Ensembl; ENST00000527524.8; ENSP00000435648.2; ENSG00000149403.13.
DR Ensembl; ENST00000638419.1; ENSP00000492086.1; ENSG00000149403.13.
DR GeneID; 2900; -.
DR KEGG; hsa:2900; -.
DR MANE-Select; ENST00000527524.8; ENSP00000435648.2; NM_014619.5; NP_055434.2.
DR UCSC; uc001pxn.4; human.
DR CTD; 2900; -.
DR DisGeNET; 2900; -.
DR GeneCards; GRIK4; -.
DR HGNC; HGNC:4582; GRIK4.
DR HPA; ENSG00000149403; Tissue enhanced (brain).
DR MIM; 600282; gene.
DR neXtProt; NX_Q16099; -.
DR OpenTargets; ENSG00000149403; -.
DR PharmGKB; PA28976; -.
DR VEuPathDB; HostDB:ENSG00000149403; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000159111; -.
DR HOGENOM; CLU_007257_1_0_1; -.
DR InParanoid; Q16099; -.
DR OMA; PAXVELE; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q16099; -.
DR TreeFam; TF334668; -.
DR PathwayCommons; Q16099; -.
DR Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
DR SignaLink; Q16099; -.
DR SIGNOR; Q16099; -.
DR BioGRID-ORCS; 2900; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; GRIK4; human.
DR GenomeRNAi; 2900; -.
DR Pharos; Q16099; Tclin.
DR PRO; PR:Q16099; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q16099; protein.
DR Bgee; ENSG00000149403; Expressed in secondary oocyte and 105 other tissues.
DR Genevisible; Q16099; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0099055; C:integral component of postsynaptic 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; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
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:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; TAS:ProtInc.
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_0000011549"
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 863..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 VARIANT 528
FT /note="V -> I (in dbSNP:rs2230298)"
FT /evidence="ECO:0000269|PubMed:8263508"
FT /id="VAR_046998"
FT VARIANT 824
FT /note="M -> T (in dbSNP:rs9988907)"
FT /id="VAR_046999"
FT CONFLICT 255
FT /note="M -> T (in Ref. 1; AAB29311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 107246 MW; B7CBEA402A79397A CRC64;
MPRVSAPLVL LPAWLVMVAC SPHSLRIAAI LDDPMECSRG ERLSITLAKN RINRAPERLG
KAKVEVDIFE LLRDSEYETA ETMCQILPKG VVAVLGPSSS PASSSIISNI CGEKEVPHFK
VAPEEFVKFQ FQRFTTLNLH PSNTDISVAV AGILNFFNCT TACLICAKAE CLLNLEKLLR
QFLISKDTLS VRMLDDTRDP TPLLKEIRDD KTATIIIHAN ASMSHTILLK AAELGMVSAY
YTYIFTNLEF SLQRMDSLVD DRVNILGFSI FNQSHAFFQE FAQSLNQSWQ ENCDHVPFTG
PALSSALLFD AVYAVVTAVQ ELNRSQEIGV KPLSCGSAQI WQHGTSLMNY LRMVELEGLT
GHIEFNSKGQ RSNYALKILQ FTRNGFRQIG QWHVAEGLSM DSHLYASNIS DTLFNTTLVV
TTILENPYLM LKGNHQEMEG NDRYEGFCVD MLKELAEILR FNYKIRLVGD GVYGVPEANG
TWTGMVGELI ARKADLAVAG LTITAEREKV IDFSKPFMTL GISILYRVHM GRKPGYFSFL
DPFSPGVWLF MLLAYLAVSC VLFLVARLTP YEWYSPHPCA QGRCNLLVNQ YSLGNSLWFP
VGGFMQQGST IAPRALSTRC VSGVWWAFTL IIISSYTANL AAFLTVQRMD VPIESVDDLA
DQTAIEYGTI HGGSSMTFFQ NSRYQTYQRM WNYMYSKQPS VFVKSTEEGI ARVLNSNYAF
LLESTMNEYY RQRNCNLTQI GGLLDTKGYG IGMPVGSVFR DEFDLAILQL QENNRLEILK
RKWWEGGKCP KEEDHRAKGL GMENIGGIFV VLICGLIVAI FMAMLEFLWT LRHSEATEVS
VCQEMVTELR SIILCQDSIH PRRRRAAVPP PRPPIPEERR PRGTATLSNG KLCGAGEPDQ
LAQRLAQEAA LVARGCTHIR VCPECRRFQG LRARPSPARS EESLEWEKTT NSSEPE
