GLRK_LITBE
ID GLRK_LITBE Reviewed; 487 AA.
AC P20262;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable glutamate receptor;
DE AltName: Full=Kainate-binding protein;
DE Short=KBP;
DE Flags: Precursor;
OS Lithobates berlandieri (Rio Grande leopard frog) (Rana berlandieri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=30360;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 150-175.
RC TISSUE=Brain;
RX PubMed=2556640; DOI=10.1038/342684a0;
RA Wada K., Dechesne C.J., Shimasaki S., King R.G., Kusano K., Buonanno A.,
RA Hampson D.R., Banner C., Wenthold R.J., Nakatani Y.;
RT "Sequence and expression of a frog brain complementary DNA encoding a
RT kainate-binding protein.";
RL Nature 342:684-689(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; X17314; CAA35193.1; -; mRNA.
DR PIR; S07061; S07061.
DR AlphaFoldDB; P20262; -.
DR SMR; P20262; -.
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 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; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..487
FT /note="Probable glutamate receptor"
FT /id="PRO_0000011558"
FT TOPO_DOM 18..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 464..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 97
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 487 AA; 54278 MW; 442E31E1E7224572 CRC64;
MEKALMLFLA VSLLSLGHTD GKENAETLLK ERTKRQIPKT LTVTTILEKP FAMKTESDAL
EGYAIDLLSE LTQSLGFNYT LHIVKDGKYG SKDQEGNWSG MVGEIIRKEA DLAIAPLTIT
SVRENAISFT KPFMQTGIGI LLKKDTAAES SYMFGFLNPF SKELWIGIII SYVITSLCLF
LVGRLSPCEW TEPASEQNQF TLLNSLWYGV GALTLQGAEP QPKALSARII AVIWWVFSIT
LLAAYIGSFA SYINSNTNQT PNIQSVEDLL KQDKLDFGTL SNSSTLNFFK NSKNPTFQMI
YEYMDKRKDR VLVKTFSEGV QRVRESNYAF LGESISQDFV VAKHCDLIRA PEMIGGRGYG
IAAELDSPLI RPLTIAILEL FESGKLEYLR QKWWENTCST QDQTGWVPVQ PHTLGGIFLI
LGIGLALGLI VSFMELMCKS RSNAEQQKKS CCSAFSEEIA QRFGKTQNQE GLEKKSPTSN
SCDEVKA