ID Q9TYG6_HAECO Unreviewed; 435 AA.
AC Q9TYG6;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 2.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Glutamate-gated chloride channel {ECO:0000313|EMBL:AAG43233.1, ECO:0000313|EMBL:CAA10355.2};
DE SubName: Full=Glutamate-gated chloride channel; Glutamate-gated chloride channel subunit {ECO:0000313|WBParaSite:HCON_00028600-00001};
GN Name=HG5 {ECO:0000313|EMBL:CAA10355.2};
GN Synonyms=glc-5 {ECO:0000313|EMBL:AAG43233.1};
OS Haemonchus contortus (Barber pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6289 {ECO:0000313|EMBL:CAA10355.2};
RN [1] {ECO:0000313|EMBL:CAA10355.2}
RP NUCLEOTIDE SEQUENCE.
RA Delany N.S.;
RL Thesis (1998), University of Bath, Bath, UK.
RN [2] {ECO:0000313|EMBL:AAG43233.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PF17 {ECO:0000313|EMBL:AAG43233.1};
RA Forrester S.G., Prichard R.K., Beech R.N.;
RT "Glutamate-gated chloride channel subunit allele associated with ivermectin
RT susceptibility in Haemonchus contortus.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAA10355.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11378196; DOI=10.1016/S0166-6851(01)00258-4;
RA Cheeseman C.L., Delany N.S., Woods D.J., Wolstenholme A.J.;
RT "High-affinity ivermectin binding to recombinant subunits of the Haemonchus
RT contortus glutamate-gated chloride channel.";
RL Mol. Biochem. Parasitol. 114:161-168(2001).
RN [4] {ECO:0000313|WBParaSite:HCON_00028600-00001}
RP IDENTIFICATION.
RC STRAIN=MHco3 {ECO:0000313|WBParaSite:HCON_00028600-00001};
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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; AF119792; AAG43233.1; -; mRNA.
DR EMBL; AJ131347; CAA10355.2; -; mRNA.
DR WBParaSite; HCON_00028600-00001; HCON_00028600-00001; HCON_00028600.
DR OMA; IIFNIMY; -.
DR Proteomes; UP000025227; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR CDD; cd18993; LGIC_ECD_GluCl; 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 NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF898; 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 2: Evidence at transcript level;
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..435
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011951414"
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 276..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 312..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 402..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 28..243
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 254..347
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
SQ SEQUENCE 435 AA; 51009 MW; 448546BFF178D9B0 CRC64;
MFALILPFLL HFTRSEGFGY EKLLDEQKII KHLLESPYSD YDWRVRPRGR LGPADDDDYD
SEPVFITVNM YLRSISKVDD VNMEYSLHFT FREEWIDERL YFNSPTLKHI VLSPGQRIWV
PDTFFQNEKD GKKHDIDTPN ILIRIHNGTG KILYSCRLTL TLSCPMRLAD YPLDVQTCVV
DFASYAYTTK DIEYGWKEEK PIQIKDGLRQ SLPSFLLSNV KTGNCTSVTN TGAYSCLRTI
IELKREFSYY LLQLYIPSFM LVAVSWVSFW LDKDSVPARV TLGVTTLLTM TTQASGVNAN
LPPVSYTKAI DIWIGVCLAF IFGALLEFAL VNWAARQDLV AHSRARYRQS PLFFRNPDSR
QENSHHFYAP IQQEVTLEDL PFSWWDKIWK IRYKERSRRI DLISRVMFPL CFIIFNIMYW
WRYLIPYMAV QAQLE
//
