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Database: UniProt
Entry: A0A2G5V100_9PELO
LinkDB: A0A2G5V100_9PELO
Original site: A0A2G5V100_9PELO 
ID   A0A2G5V100_9PELO        Unreviewed;       501 AA.
AC   A0A2G5V100;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Ig-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=Cni-glc-4 {ECO:0000313|EMBL:PIC45186.1};
GN   Synonyms=Cnig_chr_II.g5291 {ECO:0000313|EMBL:PIC45186.1};
GN   ORFNames=B9Z55_005291 {ECO:0000313|EMBL:PIC45186.1};
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:PIC45186.1, 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:PIC45186.1}.
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DR   EMBL; PDUG01000002; PIC45186.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5V100; -.
DR   Proteomes; UP000230233; Chromosome ii.
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; cd18993; LGIC_ECD_GluCl; 1.
DR   CDD; cd19062; LGIC_TM_GluCl; 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; IPR044721; GluCl_TM.
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:SF452; GLUTAMATE-GATED CHLORIDE CHANNEL; 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; 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..20
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           21..501
FT                   /note="Ig-like domain-containing protein"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022272899"
FT   TRANSMEM        264..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        296..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        330..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          49..262
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          272..489
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   501 AA;  58006 MW;  3369251840AC9D0B CRC64;
     MKTQLCVSLL LTLSLLSTSA KKAKTKSCKR TAFSRHTTNY QAWREQMTVC DLLQDYDAAV
     RPSGRTPYND TRGAVIVTTS LNIRSISAVS EKNMEFVAQF RFRQEWYDDR LRFIEHQGLL
     SSDYRNFEFI HVARDQSLWI PDTFFQNEKN GWYHMLNQEN RFLKIRSDGK LIYDRRLTLH
     LACSMHLSRY PMDHQNCEIA FASYAYTTAD IEYIWDVPAI QIHEGANGAL PNFEIASFKN
     GSCTSKTNTG TYSCLKVEIR LNRVFSFFLL QLYIPSSMLV GVAWVSYWID WKSTAARVPL
     AIVTLLTMIT TSHAINSNLP PVSYAKSIDI WVGACVVFIF FSLIEYAVVN YMGILDEHRQ
     MKKAACNRSR LSNVIDNDNF GESLQSLTFS PQEKKRLIRR RPKKNMEMQE GDFEAIEMVD
     RGPPRSAGLM EEGWTFHDTT DLVYIGQRKR VELVRWCSVL SSRGRAERID IIARIIFPIA
     FILFNFAYWS IYLEEEDLDE S
//
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