ID   GLRK_CHICK              Reviewed;         487 AA.
AC   P19439;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Probable glutamate receptor;
DE   AltName: Full=Kainate-binding protein;
DE   Flags: Precursor;
GN   Name=KBP;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Cerebellum;
RX   PubMed=2480525; DOI=10.1038/342689a0;
RA   Gregor P., Mano I., Maoz I., McKeown M., Teichberg V.I.;
RT   "Molecular structure of the chick cerebellar kainate-binding subunit of a
RT   putative glutamate receptor.";
RL   Nature 342:689-692(1989).
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   -!- 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; X17700; CAA35693.1; -; mRNA.
DR   PIR; S07062; S07062.
DR   RefSeq; NP_990684.1; NM_205353.2.
DR   AlphaFoldDB; P19439; -.
DR   SMR; P19439; -.
DR   STRING; 9031.ENSGALP00000001774; -.
DR   PaxDb; P19439; -.
DR   GeneID; 396300; -.
DR   KEGG; gga:396300; -.
DR   CTD; 101799836; -.
DR   VEuPathDB; HostDB:geneid_396300; -.
DR   eggNOG; KOG1052; Eukaryota.
DR   HOGENOM; CLU_007257_0_0_1; -.
DR   InParanoid; P19439; -.
DR   OrthoDB; 188544at2759; -.
DR   PhylomeDB; P19439; -.
DR   TreeFam; TF315232; -.
DR   PRO; PR:P19439; -.
DR   Proteomes; UP000000539; Unplaced.
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; 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   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Glycoprotein; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT   CHAIN           24..487
FT                   /note="Probable glutamate receptor"
FT                   /id="PRO_0000011557"
FT   TOPO_DOM        24..169
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..419
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        441..487
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   487 AA;  54356 MW;  45D71B2A94A27880 CRC64;
     MDKGLHFIFC VVTAVLLLRE SSQTGAMRND DAMIKPNDLR GPEENLPSLT VTTILEDPYV
     MVRSAELEGY CIDLLKALAS MLHFSYKVKV VGDGKYGAIS PSGNWTGMIG EILRQEADIA
     VAPLTVTSAR EEVVSFTTPF LQTGIGILLR KETISQEMSF FHFLAPFSKE TWTGLLFAYV
     LTCVCLFLVA RLSPCEWNEP KNEENHFTFL NSLWFGAGAL TLQGVTPRPK AFSVRVIAAI
     WWLFTIALLA AYIANFTALL SSGSEQLSIQ TFEDLVKQRK LEFGTLDGSS TFYFFKNSKN
     PIHRMVYEYM DKRRDHVLVK TYQEAVQRVM ESNYAFIGES ISQDLAAARH CNLIRAPEVI
     GARGFGIATA QASPWTKKLS VAVLKLRETG DLDYLRNKWW ESSCLHKSRE GWSPLQPQAL
     GGLFLTLAIG LALGVIAAMV ELSNKSRHAA GHIKKSCCSI FTEEMCTRLR IKENTRQTQE
     TSGRANA