ID A8XZA9_CAEBR Unreviewed; 466 AA.
AC A8XZA9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Protein CBR-LGC-9 {ECO:0000313|EMBL:CAP37976.1};
GN Name=lgc-9 {ECO:0000313|WormBase:CBG21050};
GN Synonyms=Cbr-lgc-9 {ECO:0000313|EMBL:CAP37976.1};
GN ORFNames=CBG21050 {ECO:0000313|WormBase:CBG21050}, CBG_21050
GN {ECO:0000313|EMBL:CAP37976.1};
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:CAP37976.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP37976.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP37976.1,
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}.
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DR EMBL; HE601035; CAP37976.1; -; Genomic_DNA.
DR RefSeq; XP_002634730.1; XM_002634684.1.
DR AlphaFoldDB; A8XZA9; -.
DR STRING; 6238.A8XZA9; -.
DR EnsemblMetazoa; CBG21050.1; CBG21050.1; WBGene00039930.
DR GeneID; 8576723; -.
DR KEGG; cbr:CBG_21050; -.
DR CTD; 8576723; -.
DR WormBase; CBG21050; CBP05004; WBGene00039930; Cbr-lgc-9.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_3_0_1; -.
DR InParanoid; A8XZA9; -.
DR OMA; YRAEVHY; -.
DR OrthoDB; 5489962at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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; cd18989; LGIC_ECD_cation; 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 PANTHER; PTHR18945:SF869; 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; 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 Ion channel {ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|RuleBase:RU000687};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687}; Transport {ECO:0000256|RuleBase:RU000687}.
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 313..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 432..454
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 42..245
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 252..347
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 466 AA; 53513 MW; D20DEAAF7D7E4FBF CRC64;
MYFLQLISVL ISMKIGHVRS SRLLQQHNHY NHDDGYVKAE PTHLIETIQR RYDKRVRPFA
ETNRPVIVHM TIVLGILTEV RENQQVASFV ISHVQKWRDP KLAWNPADHS GLTQVVMPRS
LVWVPKLFIY NSMDTKDMLT DDRYDVRIQH TGHVKVNSPQ FVSTLCRINI DLFPFDTQFC
AIALASPLLS VEEMDVNATQ PPVDSYFSGN AEWQVMNVTV KQMKFMEEGE YRAEVHYILH
LNRRPTYYIT VIVVPTFLIS ALSILGIFSP GSNDGPRNEK VSLGLGSLLA MTVLLDIVAG
AMPKSDAIPL LGYYIMLVIL LCAIGVAVSM AMLSMSRSCI QTSKMPPVHY YRLLFLNVCR
VVKQNGGGVN GVGEMNEKPT TITPRFPDLI SIYNQLIEVA RAQRTYRERI EKQKWQHRVE
IEWNKIFARI DFFFLFLFEM FNVLVLVLFL RYAFLPVPPL PENFSI
//
