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Database: UniProt
Entry: A0A1I8G3V5_9PLAT
LinkDB: A0A1I8G3V5_9PLAT
Original site: A0A1I8G3V5_9PLAT 
ID   A0A1I8G3V5_9PLAT        Unreviewed;       399 AA.
AC   A0A1I8G3V5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Neur_chan_LBD domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0000662-snap-gene-1.39-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_0000662-snap-gene-1.39-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0000662-snap-gene-1.39-mRNA-1}
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}. Postsynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034104}. Synaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034099}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       {ECO:0000256|RuleBase:RU000687}.
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DR   AlphaFoldDB; A0A1I8G3V5; -.
DR   WBParaSite; maker-uti_cns_0000662-snap-gene-1.39-mRNA-1; maker-uti_cns_0000662-snap-gene-1.39-mRNA-1; maker-uti_cns_0000662-snap-gene-1.39.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   CDD; cd18997; LGIC_ECD_nAChR; 1.
DR   CDD; cd19051; LGIC_TM_cation; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 2.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   PANTHER; PTHR18945:SF895; NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA3, ISOFORM B; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU000687};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
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,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT   TRANSMEM        153..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        184..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        223..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        264..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        372..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          1..152
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          159..388
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   399 AA;  46545 MW;  1D1AF0D32A6B9A1C CRC64;
     EWHDERLHWS PENYSGLAVL RVPCQKLWLP DIVLYNSADD FTTGYMQSKA MVDCNGTVFW
     PPPAKLRSTC KIDITYFPFD DQVCTMKFGS WTYDGFQVNI TKKREEVDFE NYVQSGEWNL
     IRVDVERQET VYPISTVPYP DIKFHIVIQR RTLYYLFNII FPCLWLTVLS LLSFWLPPDS
     GEKITLGITV LLAFSVFMLL IAENMPATSE FVPLIACPVR IAGIYLTVTM STTSLSIVLT
     VFVLHLHHIG PNDKPLPRWL RRFLFKRLAP LLCMTSVARY QRKARRKRRE LRQLDDSDQQ
     PAVDDVTDEA EDELETATCT TTASTFRQQH QLRQSIRLDR HIRRLMRQQL DDEAAQLLIS
     DWRTVAYVMD RLLFWLFLTA AFTSTLVILV VMPLFKKVL
//
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