GRIK1_MACFA
ID GRIK1_MACFA Reviewed; 918 AA.
AC Q38PU4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=16943768;
RA Hanna M.C., Calkins D.J.;
RT "Expression and sequences of genes encoding glutamate receptors and
RT transporters in primate retina determined using 3'-end amplification
RT polymerase chain reaction.";
RL Mol. Vis. 12:961-976(2006).
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 -!- 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; DQ159933; ABA47257.1; -; mRNA.
DR RefSeq; NP_001271466.1; NM_001284537.1.
DR AlphaFoldDB; Q38PU4; -.
DR SMR; Q38PU4; -.
DR STRING; 9541.XP_005548912.1; -.
DR Ensembl; ENSMFAT00000018112; ENSMFAP00000043822; ENSMFAG00000039272.
DR GeneID; 102132739; -.
DR CTD; 2897; -.
DR VEuPathDB; HostDB:ENSMFAG00000039272; -.
DR eggNOG; KOG1052; Eukaryota.
DR GeneTree; ENSGT00940000156253; -.
DR Proteomes; UP000233100; Chromosome 3.
DR Bgee; ENSMFAG00000039272; Expressed in temporal lobe and 2 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
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; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..918
FT /note="Glutamate receptor ionotropic, kainate 1"
FT /id="PRO_0000271756"
FT TOPO_DOM 31..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..834
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 856..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 531..533
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 704..705
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 753
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT MOD_RES 725
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 761
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
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 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 918 AA; 103957 MW; AA902AA3D021E46D CRC64;
MELGTLLAQP GLWTRDTSWA LLYFLCYILP QTAPQVLRIG GIFETVENEP VNVEELAFKF
AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ
SICNALEVPH IQTRWKHPSV DNKDLFYINL YPDYAAISRA ILDLVLYYNW KTVTVVYEDS
TGLIRLQELI KAPSRYNIKI KIRQLPSGNK DAKPLLKEMK KGKEFYVIFD CSHETAAEIL
KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RLLNIDNPHV SSIIEKWSME
RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPWRLGPRF
MNLIKEARWD GLTGHITFNK TNGLRKDFDL DIISLKEEGT EKAAGEVSKH LYKVWKKIGI
WNSNSGLNMT DSNKDKSSNI TDSLANRTLI VTTILEEPYV MYRKSDKPLY GNDRFEGYCL
DLLKELSNIL GFIYDVKLVP DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK
VIDFSKPFMT LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT
PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL
IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV RDGSTMTFFK KSKISTYEKM
WAFMSSRQQT ALVRNSDEGI QRVLTTDYAL LMESTSIEYV TQRNCNLTQI GGLIDSKGYG
VGTPIGSPYR DKITIAILQL QEEGKLHMMK EKWWRGNGCP EEDNKEASAL GVENIGGIFI
VLAAGLVLSV FVAIGEFIYK SRKNNDIEQA FCFFYGLQCK QTHPTNSTSG TTLSTDLECG
KLIREERGIR KQSSVHTV
