GLUCB_HAECO
ID GLUCB_HAECO Reviewed; 432 AA.
AC P91730;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glutamate-gated chloride channel subunit beta;
DE Short=Glu-Cl subunit beta;
DE AltName: Full=Avermectin-sensitive glutamate-gated chloride channel subunit;
DE AltName: Full=HG4;
DE Flags: Precursor;
OS Haemonchus contortus (Barber pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Trichostrongyloidea; Haemonchidae; Haemonchus.
OX NCBI_TaxID=6289;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9879896; DOI=10.1016/s0166-6851(98)00148-0;
RA Delany N.S., Laughton D.L., Wolstenholme A.J.;
RT "Cloning and localisation of an avermectin receptor-related subunit from
RT Haemonchus contortus.";
RL Mol. Biochem. Parasitol. 97:177-187(1998).
CC -!- FUNCTION: Glutamate-gated chloride channel subunit; channel properties
CC may be modulated by the formation of heteromeric channels. Glutamate
CC binding triggers a rapidly reversible current, while the anti-helmintic
CC drug ivermectin triggers a permanently open channel configuration.
CC {ECO:0000250|UniProtKB:G5EBR3}.
CC -!- SUBUNIT: Pentamer (By similarity). {ECO:0000250|UniProtKB:G5EBR3}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q94900}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q94900}. Cell membrane
CC {ECO:0000250|UniProtKB:Q94900}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q94900}.
CC -!- TISSUE SPECIFICITY: Expressed in motor neuron commissures at the
CC anterior portion of the worms. {ECO:0000269|PubMed:9879896}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glutamate-gated chloride channel (TC 1.A.9.4) subfamily. {ECO:0000305}.
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DR EMBL; Y09796; CAA70929.1; -; mRNA.
DR AlphaFoldDB; P91730; -.
DR SMR; P91730; -.
DR ChEMBL; CHEMBL2363050; -.
DR DrugCentral; P91730; -.
DR TCDB; 1.A.9.4.3; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR CDD; cd19062; LGIC_TM_GluCl; 1.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR015680; Glu_Cl_Channel.
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 PANTHER; PTHR18945; PTHR18945; 1.
DR PANTHER; PTHR18945:SF504; PTHR18945:SF504; 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; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..432
FT /note="Glutamate-gated chloride channel subunit beta"
FT /id="PRO_0000255717"
FT TOPO_DOM 19..249
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 250..272
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 273..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 278..299
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 300..306
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 307..327
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 328..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TRANSMEM 403..426
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT TOPO_DOM 427..432
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 69
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 88
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 155
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT BINDING 184
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..178
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
FT DISULFID 226..237
FT /evidence="ECO:0000250|UniProtKB:G5EBR3"
SQ SEQUENCE 432 AA; 49626 MW; AE6E7342FA8C883B CRC64;
MSQYMMVAVA AVVAVAGSSQ ISRRSTGGTQ EQEILNELLS NYDMRVRPPP SNYSDPMGPV
TVRVNIMIRM LSKIDVVNME YSMQLTFREQ WLDSRLAYAH LGYHNPPKFL TVPHIKSNLW
IPDTFFPTEK AAHRHLIDTD NMFLRIHPDG KVLYSSRISI TSSCHMQLQL YPLDLQFCDF
DLVSYAHTMK DIVYEWDPLA PVQLKPGVGS DLPNFQLTNI TTNDDCTSHT NTGSYACLRM
QLTLKRQFSY YLVQLYGPTT MIVIVSWVSF WIDMHSTAGR VALGVTTLLT MTTMQAAINA
KLPPVSYVKV VDVWLGACQT FVFGALLEYA FVSYQDSQRQ TEQAKSRAAR KAQKRRAKME
LVEREQYQPP CTCHLYQDYE PSFRDRLRRY FTKPDYLPAK IDYYARFCVP LGFLAFNAIY
WTSCLVMVSR LV
