ID   P92039_HAECO            Unreviewed;       512 AA.
AC   P92039;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   18-JUN-2025, entry version 121.
DE   SubName: Full=Acetylcholine receptor alpha subunit {ECO:0000313|EMBL:AAB51667.1};
GN   Name=AChR {ECO:0000313|EMBL:AAB51667.1};
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:AAB51667.1};
RN   [1] {ECO:0000313|EMBL:AAB51667.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hoekstra R.R.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAB51667.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9084038; DOI=10.1016/S0166-6851(96)02793-4;
RA   Hoekstra R., Visser A., Wiley L.J., Weiss A.S., Sangster N.C., Roos M.H.;
RT   "Characterization of an acetylcholine receptor gene of Haemonchus contortus
RT   in relation to levamisole resistance.";
RL   Mol. Biochem. Parasitol. 84:179-187(1997).
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034104}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily.
CC       {ECO:0000256|ARBA:ARBA00009237}.
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DR   EMBL; U72490; AAB51667.1; -; mRNA.
DR   AlphaFoldDB; P92039; -.
DR   SMR; P92039; -.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   CDD; cd19031; LGIC_ECD_nAChR_proto_alpha-like; 1.
DR   CDD; cd19064; LGIC_TM_nAChR; 1.
DR   FunFam; 2.70.170.10:FF:000044; AcetylCholine Receptor; 1.
DR   FunFam; 1.20.58.390:FF:000030; Acetylcholine receptor subunit alpha-L1; 1.
DR   FunFam; 1.20.58.390:FF:000001; Neuronal nicotinic acetylcholine receptor subunit 3; 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; 2.
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   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   NCBIfam; TIGR00860; LIC; 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; PR00254; NICOTINICR.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU000687};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:AAB51667.1};
KW   Signal {ECO:0000256|RuleBase:RU000687};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
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..19
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           20..512
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022272731"
FT   TRANSMEM        254..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        285..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        319..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          24..253
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          260..485
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   512 AA;  59540 MW;  CABE7A264200DB03 CRC64;
     MRHLLSFVIS FVSFYYIYAN EDAKRLYDDL MVNYNRHRRP ASGPHEPLTI KLKLRLSQII
     DVHEIDQIMT CSVWLKQVWI DKKLSWDPES YGGVSVLYVP YEMIWVPDIV LYNNADSNYN
     ITISTKATLH YSGEVTWEPP AIFKSMCQID VRWFPFDEQQ CHLKFGSWTN SENLLNLELL
     ENNVRYEEEV NEQGIVDNIT IADDGIDLSD YYPSVEWDIM SRVARRRSKN YPSCCPQSAY
     IDIMYYLELR RKPLFYTVNL VFPCVGISFL TILVFYLPSD SGEKVTLCIS ILVALTIFFL
     LLTEIIPATS ITLPLIGKYL LFTMVMVTLS VVVTVISLNL HFRTPTTHLM PKWVKLVFLK
     WLPKVLFMRR PLDDGDESFR RVSSRKGIGP TTFDGKIPLN LHEHRVSRDI GKSLANAAID
     ERIQKLYYSP QVVKAFENIC FIAELLKKKD RDDKIDEDWK YVAMVLDRLF LLIFSFACFI
     GTVLILLQAP TLYDDRKPID LQYRPANLSA LF
//