GRIK4_RAT
ID GRIK4_RAT Reviewed; 956 AA.
AC Q01812; Q62642;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Glutamate receptor ionotropic, kainate 4;
DE Short=GluK4;
DE AltName: Full=Glutamate receptor KA-1;
DE Short=KA1;
DE Flags: Precursor;
GN Name=Grik4;
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=1648176; DOI=10.1038/351742a0;
RA Werner P., Voigt M., Keinaenen K., Wisden W., Seeburg P.H.;
RT "Cloning of a putative high-affinity kainate receptor expressed
RT predominantly in hippocampal CA3 cells.";
RL Nature 351:742-744(1991).
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.
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: Forms a heteromeric channel with GRIK1 or GRIK3.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Strong expression in hippocampal CA3 pyramidal
CC cells. Low expression in hippocampal dentate granule cells, in layers
CC II, V and VI of the cortex, and in cerebellar Purkinje cells. No
CC expression in the striatum, reticular thalamus, hypothalamus or
CC amygdaloid complex.
CC -!- DEVELOPMENTAL STAGE: Expressed at embryonic day 15 in brain and spinal
CC cord. At embryonic day 19 expression accumulates in the hippocampal
CC formation. Prominent expression in the subicular cortex at postnatal
CC days P1, P8 and P15 but then markedly reduced in the adult.
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; X59996; CAA42615.1; -; mRNA.
DR EMBL; U08257; AAA17830.1; -; mRNA.
DR PIR; JS0685; JS0685.
DR RefSeq; NP_036704.1; NM_012572.1.
DR RefSeq; XP_017450943.1; XM_017595454.1.
DR RefSeq; XP_017450944.1; XM_017595455.1.
DR PDB; 5IKB; X-ray; 2.05 A; A=415-526, A=652-790.
DR PDBsum; 5IKB; -.
DR AlphaFoldDB; Q01812; -.
DR SMR; Q01812; -.
DR STRING; 10116.ENSRNOP00000047794; -.
DR BindingDB; Q01812; -.
DR ChEMBL; CHEMBL3044; -.
DR DrugCentral; Q01812; -.
DR GlyGen; Q01812; 9 sites.
DR PaxDb; Q01812; -.
DR PRIDE; Q01812; -.
DR GeneID; 24406; -.
DR KEGG; rno:24406; -.
DR UCSC; RGD:2734; rat.
DR CTD; 2900; -.
DR RGD; 2734; Grik4.
DR eggNOG; KOG1052; Eukaryota.
DR InParanoid; Q01812; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; Q01812; -.
DR Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
DR PRO; PR:Q01812; -.
DR Proteomes; UP000002494; Unplaced.
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: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:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; TAS:RGD.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; TAS:RGD.
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:RGD.
DR GO; GO:0006811; P:ion transport; TAS:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0031960; P:response to corticosteroid; IEP:RGD.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000011551"
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 539
FT /note="S -> F (in Ref. 2; AAA17830)"
FT /evidence="ECO:0000305"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:5IKB"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 484..490
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 674..680
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 685..696
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 706..715
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 716..723
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 724..732
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:5IKB"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 760..772
FT /evidence="ECO:0007829|PDB:5IKB"
FT HELIX 775..784
FT /evidence="ECO:0007829|PDB:5IKB"
SQ SEQUENCE 956 AA; 107223 MW; 970C9D72C8D74700 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 FTRNGFRQIG QWHVAEGLSM DSRLYASNIS DSLFNTTLVV
TTILENPYLM LKGNHQDMEG NDRYEGFCVD MLKELAEILR FNYKIRLVGD GVYGVPEANG
TWTGMVGELI ARKADLAVAG LTITAEREKV IDFSKPFMTL GISILYRVHM GRRPGYFSSL
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
VCQEMMTELR SIILCQDNIH PRRRRSGGLP PQPPVLEERR PRGTATLSNG KLCGAGEPDQ
LAQRLAQEAA LVARGCTHIR VCPECRRFQG LRARPSPARS EESLEWDKTT NSSEPE
