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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//