ID A8XH20_CAEBR Unreviewed; 548 AA.
AC A8XH20;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Protein CBR-GLC-4 {ECO:0000313|EMBL:CAP31944.2};
GN Name=glc-4 {ECO:0000313|WormBase:CBG13087};
GN Synonyms=Cbr-glc-4 {ECO:0000313|EMBL:CAP31944.2};
GN ORFNames=CBG13087 {ECO:0000313|WormBase:CBG13087}, CBG_13087
GN {ECO:0000313|EMBL:CAP31944.2};
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:CAP31944.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP31944.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP31944.2,
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}.
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DR EMBL; HE601401; CAP31944.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XH20; -.
DR STRING; 6238.A8XH20; -.
DR WormBase; CBG13087; CBP42077; WBGene00033914; Cbr-glc-4.
DR eggNOG; KOG3644; Eukaryota.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; A8XH20; -.
DR OMA; FAYWSIY; -.
DR OrthoDB; 2874057at2759; -.
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; 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:UP000008549};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 TRANSMEM 40..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 311..336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 343..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 377..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 96..309
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 319..536
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 548 AA; 63536 MW; 9384355A5A74C948 CRC64;
MNAMCCTSNT VYKHYQHLAS YRFPPIPTRR ESARNAKKTV SIPLFFVMKT QLCVSLLLTL
SLFPTNAKKA KTKSCKRTAF SRHTTNYQAW REQMTVCDLL QDYDAAVRPS GRTPYNDTRG
AVIVTTSLNI RSISAVSEKN MEFVAQFRFR QEWYDDRLRF IEHQGLLSSD YRNFEFIHVA
RDQSLWIPDT FFQNEKNGWY HMLNQENRFL KIRSDGKLIY DRRLTLHLAC SMHLSRYPMD
HQNCEIAFAS YAYTTADIEY IWDVPAIQIH EGANGALPNF EIASFKNGSC TSKTNTGTYS
CLKVEIRLNR VFSFFLLQLY IPSSMLVGVA WVSYWIDWKS TAARVPLAIV TLLTMITTSH
AINSNLPPVS YAKSIDIWVG ACVVFIFFSL IEYAVVNYMG ILDEHRQMKK AACNRSRLSN
VIDNDNFGES LQSLTFSPQE KKRLIRRRPK KNMEMQEGDF EAIEMVDRGP PRSAGLMEEG
WTFHDTTDLV YIGQRKRVEL VRWCSVLSSR GRAERIDIIA RIIFPIAFIL FNFAYWSIYL
EEEDLDES
//
