ID A8XQH2_CAEBR Unreviewed; 494 AA.
AC A8XQH2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Protein CBR-LGC-41 {ECO:0000313|EMBL:CAP34897.2};
GN Name=lgc-41 {ECO:0000313|WormBase:CBG17253};
GN Synonyms=Cbr-lgc-41 {ECO:0000313|EMBL:CAP34897.2};
GN ORFNames=CBG17253 {ECO:0000313|WormBase:CBG17253}, CBG_17253
GN {ECO:0000313|EMBL:CAP34897.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP34897.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP34897.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP34897.2,
RC ECO:0000313|Proteomes:UP000008549};
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., 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., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR EMBL; HE601483; CAP34897.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XQH2; -.
DR STRING; 6238.A8XQH2; -.
DR WormBase; CBG17253; CBP44053; WBGene00036943; Cbr-lgc-41.
DR eggNOG; KOG3644; Eukaryota.
DR HOGENOM; CLU_010920_1_2_1; -.
DR InParanoid; A8XQH2; -.
DR OMA; SYAYIAK; -.
DR OrthoDB; 2875315at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; 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 GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR CDD; cd18987; LGIC_ECD_anion; 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 PANTHER; PTHR18945:SF906; LIGAND-GATED ION 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:UP000008549};
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..30
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 31..494
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022254514"
FT TRANSMEM 249..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 275..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 40..240
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 250..389
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 446..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 55992 MW; 89A4849A7C49E47A CRC64;
MKQQSASSFQ TLRIFLILCS ISTTFPLTQP NIYNLLQQAN TRPPTANASI PLGVKLGMYL
ESLGNFRSSE MSFDVDLYVY MSWQDTRLAH NFSNYVLINN DEIRKQIWLP DLYFANARQA
SFQEVTVPNF NLFVAPDGTV AYSCRCTLTV ACSLNLRYYP MDQQLCSIRV LSYAYIAKQV
NVTWFDKNPV RFNEEIGLPE FQIEHVSNAY CNGSYQYALT ADSFKSDDFS CLTGNLYLSR
SIGYNLVQSY IPTGLIVMIS WVSFWIDRRA VPARVTLSFT TLVSLTTLGN GLRFGLPQVS
YAKAIDLWYG ACMFFVFCAL LEFATINSYM RKSEKFDSMA KKIQSVVLTG RTRDYLVRGI
KESMRIAGGA AGNVVEAMSD DWCTYSTENG RLKTEKSPRS YGKPDTVQDI LSERIKFIDN
EFDYDAKEDD GMAMSIYDNV SCRKDDVDSS SEETKFSTKP KKNGANGTRK YIDKSLNQNS
ANESLMVATY FQVL
//
