GRIK4_PANTR
ID GRIK4_PANTR Reviewed; 956 AA.
AC Q5IS46;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Glutamate receptor ionotropic, kainate 4;
DE Short=GluK4;
DE Flags: Precursor;
GN Name=GRIK4;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a heteromeric channel with GRIK1 or GRIK3.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
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; AY665282; AAV74320.1; -; mRNA.
DR RefSeq; NP_001029331.1; NM_001034159.1.
DR RefSeq; XP_016775333.1; XM_016919844.1.
DR AlphaFoldDB; Q5IS46; -.
DR SMR; Q5IS46; -.
DR STRING; 9598.ENSPTRP00000050940; -.
DR Ensembl; ENSPTRT00000057998; ENSPTRP00000050940; ENSPTRG00000004394.
DR GeneID; 451620; -.
DR KEGG; ptr:451620; -.
DR CTD; 2900; -.
DR VGNC; VGNC:50382; GRIK4.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000159111; -.
DR InParanoid; Q5IS46; -.
DR OMA; PAXVELE; -.
DR OrthoDB; 188544at2759; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000004394; Expressed in dorsolateral prefrontal cortex and 8 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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_0000011550"
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"
SQ SEQUENCE 956 AA; 107265 MW; B7CE1B7A8D022B7A 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 DSRLYASNIS 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
