ID   GLRK_XENLA              Reviewed;         479 AA.
AC   Q91756; Q4PKI4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Glutamate receptor U1;
DE   AltName: Full=Kainate-binding protein;
DE   AltName: Full=Unitary non-NMDA glutamate receptor subunit 1;
DE   AltName: Full=XENU1;
DE   Flags: Precursor;
GN   Name=kbp;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8723645;
RA   Ishimaru H., Kamboj R., Ambrosini A., Henley J.M., Soloviev M.M., Sudan H.,
RA   Rossier J., Abutidze K., Rampersad V., Usherwood P.N.R., Bateson A.N.,
RA   Barnard E.A.;
RT   "A unitary non-NMDA receptor short subunit from Xenopus: DNA cloning and
RT   expression.";
RL   Recept. Channels 4:31-49(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bull L., Hollmann M.;
RL   Submitted (MAY-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 (By similarity). This
CC       receptor binds domoate > kainate > AMPA > NBQX > glutamate.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homomeric.
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. {ECO:0000305}.
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DR   EMBL; X93491; CAA63760.1; -; mRNA.
DR   EMBL; DQ073428; AAY81921.1; -; mRNA.
DR   RefSeq; NP_001081086.2; NM_001087617.1.
DR   AlphaFoldDB; Q91756; -.
DR   SMR; Q91756; -.
DR   GeneID; 394374; -.
DR   KEGG; xla:394374; -.
DR   CTD; 394374; -.
DR   Xenbase; XB-GENE-18005836; grik5-like.1.L.
DR   OMA; FRTEVWL; -.
DR   OrthoDB; 188544at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 394374; Expressed in brain and 9 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; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_rcpt_met.
DR   InterPro; IPR001320; Iontro_rcpt.
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.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..479
FT                   /note="Glutamate receptor U1"
FT                   /id="PRO_0000011559"
FT   TOPO_DOM        18..163
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..414
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        436..479
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   479 AA;  53406 MW;  588D4B3E1057C620 CRC64;
     MEKSLLFLFA VTLLSVGCTD AGESKGSIHK EKERSKRQAL KHLTVTTIME QPFSMKSESG
     MEGFCIDLLS ELSQSLGFNY TIKEVKDGRY GAKDQDGNWN GMVGEVLRKE VDLAVAPLTI
     TANRERELAF TKPFMQTGIS ILLRKEDASE NSFLFGFLTP FSKETWIGIL VAYMVTSLCL
     FLVGRLSPCE WTELSTEQNN FTFLNSLWFG AGAFTLQGAE PHPKSVSARI IAVIWWIFSI
     VLVAAYIASF AAFLNSDSVQ TTNIQTFEDL VNQRTLEFGT INSSSTFQFF KNSKNPTYRM
     IYEYMDKRKD ELLVKSFAEG VRRVRESNYA FLGESVMQDI MVAKHCELAR APQIIAGRGY
     GIAASIDSQL IKQLSIAILE QTESGNIEYL RKKWWDNTCS MKRSAGWNPV QPHTLGGIFL
     ILGIGLALGV IAALIELVLK ARNNADQQKK SCCSAFSEEM GERLGTNKEN QGAVDSVKS