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Database: UniProt
Entry: A0A2G5UJU6_9PELO
LinkDB: A0A2G5UJU6_9PELO
Original site: A0A2G5UJU6_9PELO 
ID   A0A2G5UJU6_9PELO        Unreviewed;       429 AA.
AC   A0A2G5UJU6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Neurotransmitter-gated ion-channel ligand-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=Cnig_chr_III.g11392 {ECO:0000313|EMBL:PIC39824.1};
GN   ORFNames=B9Z55_011392 {ECO:0000313|EMBL:PIC39824.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC39824.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       {ECO:0000256|RuleBase:RU000687}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIC39824.1}.
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DR   EMBL; PDUG01000003; PIC39824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5UJU6; -.
DR   STRING; 1611254.A0A2G5UJU6; -.
DR   Proteomes; UP000230233; Chromosome iii.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; 1.
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   PANTHER; PTHR18945:SF529; ACETYLCHOLINE RECEPTOR (51.1 KD) (ACR-22)-RELATED; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
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   Ion channel {ECO:0000256|RuleBase:RU000687};
KW   Ion transport {ECO:0000256|RuleBase:RU000687};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW   Signal {ECO:0000256|RuleBase:RU000687};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000687};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU000687}; Transport {ECO:0000256|RuleBase:RU000687}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           17..429
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022255780"
FT   TRANSMEM        237..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        271..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        401..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          35..235
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          242..346
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   429 AA;  50090 MW;  91090B130582D824 CRC64;
     MKLIFLFVVI FNRGICQDNN TLEIDLINYE EKNERTLAKL LLDDYYKYAR PVRNSSSILN
     VTALIQIYNL VEVNEKNEQI QLLLWFPQSW KDEYLTWDPE EWNGIEKIII PKAMIWVPDG
     YIFNTVAEAE TMENHNARVR YDGKVELVDL TCPMSVSSFP FDSQLCALQF GSWSYPNNVL
     SFNVMGAWVH EKEKNSEWDI IDFNATKLVR GYNDTLGGAN VYEEIFYYLE LKRKPHYYIV
     VIIIPTFAIV TVSNIGLFTP HGVHGDREEH VSLGLTTMLT MAVILDMVTG QMPKSSEGIP
     LLGKYVLIEF AISIIAVLVS ILIIFAHERM LYLEKTPPAW IFRIFEKSYF QKVPLAEMEQ
     DDILSKPRDP KEEMKLCLEK VRNYLEDLET QENHEKIWQR FFSLTDILCG FIFSVINVLV
     TFYMFIDYF
//
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