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 27-MAR-2024, entry version 149.
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 GlyCosmos; P19439; 1 site, No reported glycans.
DR PaxDb; 9031-ENSGALP00000001774; -.
DR GeneID; 396300; -.
DR KEGG; gga:396300; -.
DR CTD; 396300; -.
DR VEuPathDB; HostDB:geneid_396300; -.
DR eggNOG; KOG1052; Eukaryota.
DR HOGENOM; CLU_007257_0_0_1; -.
DR InParanoid; P19439; -.
DR OMA; DFSHSFY; -.
DR OrthoDB; 511851at2759; -.
DR PhylomeDB; P19439; -.
DR TreeFam; TF315232; -.
DR PRO; PR:P19439; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0004971; F:AMPA glutamate receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated monoatomic 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 CDD; cd13685; PBP2_iGluR_non_NMDA_like; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_Glu_rcpt_met.
DR InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR PANTHER; PTHR18966:SF417; GLUTAMATE RECEPTOR-RELATED; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE 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; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 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
//