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Database: UniProt
Entry: A0A2G5TWA0_9PELO
LinkDB: A0A2G5TWA0_9PELO
Original site: A0A2G5TWA0_9PELO 
ID   A0A2G5TWA0_9PELO        Unreviewed;       574 AA.
AC   A0A2G5TWA0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=Neurotransmitter-gated ion-channel ligand-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=Cni-acr-24 {ECO:0000313|EMBL:PIC31538.1};
GN   Synonyms=Cnig_chr_IV.g12208 {ECO:0000313|EMBL:PIC31538.1};
GN   ORFNames=B9Z55_012208 {ECO:0000313|EMBL:PIC31538.1};
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:PIC31538.1, 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:PIC31538.1}.
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DR   EMBL; PDUG01000004; PIC31538.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5TWA0; -.
DR   Proteomes; UP000230233; Chromosome iv.
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; 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; 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:SF462; ACETYLCHOLINE RECEPTOR; 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..17
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           18..574
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022269216"
FT   TRANSMEM        249..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        284..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        314..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        540..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          34..248
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          255..556
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   REGION          461..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  65373 MW;  A796ECDA9F50B1EC CRC64;
     MVRVVGWFLA IIGTVLGARE ALMDDYGEFL PHIRLAKDLM DPRRYDSRVR PVMNHSKPTT
     VSFSMSLYQI LSINEKQQNV DLNVWAIQKW NDDFLGWNPY LYGMINTTIL PFDAIWLPDT
     YLYNSVVMNR EETERYINVV VTTNYWKGEK GAEVKFMYPA LYRTSCLLDI RFFPYDQQAC
     KLTISSWTSS KSDINYEPEY ESVNMDNFLP NEEWVVVSFN IKRVEEKFVC CPEPWVLLEA
     VLVVRRKPLY YIVNLVIPTS VITLVAVTGF FTAASTSSER REKLSLGIDS LLAMSILMMM
     VSEQMPTSSD FVPLFGIFYL SIIFIIFIGT LFTAFILNVH LQKMYAKPVS PIVSFIFFGK
     IAHWLRMRPP TMLLELWNET GVTFGKKDQK KPKRLEIKNQ KMPKVTSSSS GLNLLKSTSG
     SGRAPLAAPI SARSYISMDD MKREAARRNW RRLVKKINSN KQNGVKNNTG GERGQLRQAG
     RKKVPSAIAV PHGEPGPLML SASAISAFSV TGNDATILES KLKRRYALEW EYLASVLDRV
     LLIVFSLVVF TVTSVMILVG EAMHLSYELA AKEF
//
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