ID LGC4_CAEBR Reviewed; 636 AA.
AC A8XNX8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=Ligand-gated ion channel 4 {ECO:0000250|UniProtKB:P54245};
DE Flags: Precursor;
GN Name=lgc-4 {ECO:0000312|EMBL:CAP34218.2}; ORFNames=CBG16183;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP34218.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP34218.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Acetylcholine receptor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P36544}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P36544}. Cell membrane
CC {ECO:0000250|UniProtKB:P36544}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P36544}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000305}.
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DR EMBL; HE600961; CAP34218.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XNX8; -.
DR SMR; A8XNX8; -.
DR STRING; 6238.A8XNX8; -.
DR GlyCosmos; A8XNX8; 5 sites, No reported glycans.
DR EnsemblMetazoa; CBG16183.1; CBG16183.1; WBGene00036209.
DR WormBase; CBG16183; CBP26036; WBGene00036209; Cbr-lgc-4.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_0_3_1; -.
DR InParanoid; A8XNX8; -.
DR OMA; WSHDITE; -.
DR OrthoDB; 2874383at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated monoatomic ion channel activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
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 InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF828; LIGAND-GATED ION CHANNEL 4; 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; PR00254; NICOTINICR.
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; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..636
FT /note="Ligand-gated ion channel 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000365066"
FT TOPO_DOM 26..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 240..254
FT /evidence="ECO:0000250|UniProtKB:P54245"
SQ SEQUENCE 636 AA; 72811 MW; 497D050532A58E00 CRC64;
MVICHSCTTF CILLVIDLVP CRIVGMENVE NRVMFSLLDR SPQTNDTGPK PEKFEIAKGK
FKVLEENSIG ADTVSHLPTT REEHVSAVVP MPNFDPHRLE KALRTKGSID GTEEALYRSL
LDHTVYEKDV RPCIHHSQPT NVTFGFLLNQ IVEMDERNQA LTTRSWLNIN WMDPRLSWNE
SLWSDIKAIY IPHARIWKPD IILVNNAIRE YYASLVSTDV MVTSDGNVTW LFSALFRSSC
PIRVRYYPFD DQQCDLKFAS WSHDITEINL GLNTDKGDLS SYMNNSEFDL VDMTAVREVV
RFPSDTNSDW PTIVIRIHMH RRPLFYVFNH IVPCVLISSM AVLGFLMPPE TGEKINMIIT
TLLSMGVYLQ SITESIPPTS EGVPLIGMYY VSSLLMVCLA TCVNVITLNM HRNGAANQGR
HVPAWMQKWI LGYLATFMRM SIREPDSIAL LKASQSKKST IRRSSILRDL KRVKNMSNVR
AKSKEQNANR ECECMDPLVH IYAESIMTSL VSDPKPMNGS TIREDFASES TFLGRVVSDG
IMPRISASSN SVLTEFETRF RRILKRVYRS LQQHEIREEI LDERSRIQWQ WQQLASVVDR
LLLCLFCTAT LFTIICLLIV PVVYRDNDVL SILNFF
//
