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Database: UniProt
Entry: A0A2G5TL27_9PELO
LinkDB: A0A2G5TL27_9PELO
Original site: A0A2G5TL27_9PELO 
ID   A0A2G5TL27_9PELO        Unreviewed;       479 AA.
AC   A0A2G5TL27;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIC27943.1};
GN   Name=Cni-mod-1 {ECO:0000313|EMBL:PIC27943.1};
GN   Synonyms=Cnig_chr_V.g20032 {ECO:0000313|EMBL:PIC27943.1};
GN   ORFNames=B9Z55_020032 {ECO:0000313|EMBL:PIC27943.1};
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:PIC27943.1, 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:PIC27943.1}.
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DR   EMBL; PDUG01000005; PIC27943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5TL27; -.
DR   Proteomes; UP000230233; Chromosome v.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; cd18990; LGIC_ECD_GABAAR; 1.
DR   CDD; cd19049; LGIC_TM_anion; 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; IPR006028; GABAA/Glycine_rcpt.
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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   PANTHER; PTHR18945:SF431; SEROTONIN-GATED CHLORIDE CHANNEL MOD-1; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00253; GABAARECEPTR.
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   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   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|ARBA:ARBA00022729, 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};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           25..479
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022259102"
FT   TRANSMEM        243..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        309..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        449..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          39..242
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          251..466
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   479 AA;  54947 MW;  EAF34B5531877A23 CRC64;
     MTIMKFIPKI TLLLLLLFVH TSQAKGKRRK CPEGAWSEGK IMNTIMSNYT KMLPEAEDSV
     QVNIEIHVQD MGSLNEISSD FEIDILFTQL WHDSALSFAH LPACKRNITM ETRLLPKIWS
     PNTCMINSKR TTVHASPSEN VMVILYENGT VWINHRLSVK SPCNLDLRQF PFDTQTCILI
     FESYSHNSEE VELHWMEEAV TLMKPIQLPD FDMVHYSTKK ETLLYPNGYW DQLQVTFTFK
     RRYGFYIIQA YVPTYLTIIV SWVSFCMEPK ALPARTTVGI SSLLALTFQF GNILKNLPRV
     SYVKAMDVWM LGCISFVFGT MVELAFVCYI SRCQNSVRNA ERRRERMRNS QVWANGSCRT
     RSNGYANGGS IISHYHPTSN GNGSNNRQDT PLVTGRGSLH RNGPPSPLNL QMTTFDSEIP
     LTFDQMRPGS PPPPSGCLAR FHPEAVDKFS IVAFPLAFTM FNLVYWWHYL SQTFDQNYQ
//
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