ID A0A1I8IYI3_9PLAT Unreviewed; 456 AA.
AC A0A1I8IYI3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate receptor {ECO:0000313|WBParaSite:maker-uti_cns_0045346-snap-gene-1.18-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0045346-snap-gene-1.18-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0045346-snap-gene-1.18-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A1I8IYI3; -.
DR WBParaSite; maker-uti_cns_0045346-snap-gene-1.18-mRNA-1; maker-uti_cns_0045346-snap-gene-1.18-mRNA-1; maker-uti_cns_0045346-snap-gene-1.18.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; IEA:InterPro.
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; IPR015683; Ionotropic_Glu_rcpt.
DR InterPro; IPR001320; Iontro_rcpt_C.
DR PANTHER; PTHR18966:SF108; GLUTAMATE RECEPTOR IONOTROPIC, DELTA-1; 1.
DR PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 4: Predicted;
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 Receptor {ECO:0000256|ARBA:ARBA00023170}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..456
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009321318"
FT TRANSMEM 125..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..355
FT /note="Ionotropic glutamate receptor C-terminal"
FT /evidence="ECO:0000259|SMART:SM00079"
FT DOMAIN 44..103
FT /note="Ionotropic glutamate receptor L-glutamate and
FT glycine-binding"
FT /evidence="ECO:0000259|SMART:SM00918"
SQ SEQUENCE 456 AA; 48966 MW; 9F12EDD272B65CEA CRC64;
MWQDGMLPLL ALLLFAAAPV AMADGSRLDL QGKTLKVATL LEVPFSFKQG DNSSSIRGFY
IDILDLLAEE LNFKYNLYVV PDNKYGAQLP NGTWNGLIRE VIDGELQEAE SYAALFLMPF
APSTWILVIL FYFICTALAF TLWLLSPYEQ GEPQLDQIPI LRRSKKSACS SFMLVTGGLF
SPAIRILASV WWLFTLVTVA CYIGNMGSVL NDRLAIKRLQ PPFESFEELV GQSKIPYGVL
KGAASHNMFK SSKLPSFKRA DKYLRDNPDS LANTVLQGIS RAKTGNYAFL AESLTAEYYT
SINCDLIAAA TGITTLDFAL AVAKNSSLRC ILNEAILKVK MSGQLTATKD IWWTKNRDCS
DQLSFEAKSM ALMPGDFACL YGLVLIGALV ALLALPVEMY IKNALPFKLL PSRGGGTTAA
AAGAGATPAA STAAVAGAAP EAAAAPAAAG PSSSAA
//