ID   A0A1I7UJL3_9PELO        Unreviewed;       645 AA.
AC   A0A1I7UJL3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Glutamate receptor {ECO:0000313|WBParaSite:Csp11.Scaffold629.g9981.t2};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g9981.t2};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g9981.t2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC       family. {ECO:0000256|ARBA:ARBA00008685}.
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DR   AlphaFoldDB; A0A1I7UJL3; -.
DR   STRING; 1561998.A0A1I7UJL3; -.
DR   WBParaSite; Csp11.Scaffold629.g9981.t2; Csp11.Scaffold629.g9981.t2; Csp11.Scaffold629.g9981.
DR   Proteomes; UP000095282; Unplaced.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
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   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR18966:SF588; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE GLR-3; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
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; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        396..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        471..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        594..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          273..575
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          283..340
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   645 AA;  73171 MW;  160FEF7EEA6BA5CC CRC64;
     MGVSAIILPQ QYEGHMAAAA IVQSIADRTN VPCVSLHLSP PVSIHPSTHL HPHLNAKSLA
     VAAFIKREKW RDVVVVFEES DELLEVTDMI TAGHFDPDSF SSQLVRLKHG DDYGNELKHI
     KNKLDRYRIV INIPLTRALH FLEQAANLSM CGVLYHYVIM DMYTTSIWID TLRLLIRSMK
     SVHVWDEPRC GMTWAAGSDI KRKFFEGFLA GVSGDLYWAP SGERSNYTLH VYRRKLSTFQ
     KFAEWSSRTR RIASSDAVVI SNSTEKLTLE GKHLKISVYL EAPFVMMTSN GSYEGYCIDL
     LHKIANILKF TYTIQKVRDN AYGSKESNGK WSGMVGELQR GDADLAVASL TISYGRSEVI
     DFTVPYMHLG ISILFKKPRI TDSDWFKFMD PLSTQVWIMT FASYFIVSIA IWIIAKISPY
     EQFEKDENNG QYKPVDNQFS LRNSFWFTVC SLMQQGSELC PRAASTRLLT AIWWFFALIL
     ISSYTANLAA VLTTRRMETP IENADDLAAQ TKIKYGTLGR GSTMSFFNIG GLIDQKGYGI
     GLPKGSPYRE LISTAILRLQ EKTELTELKE KWWKDKSVVC EQPKRKDQDD GESIGGIFII
     LVVGLFLTAI LVIFELITTR KPSPAQSQVI RHVNVIPTFR FDFFK
//