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Database: UniProt
Entry: P54247
LinkDB: P54247
Original site: P54247 
ID   ACHX_ONCVO              Reviewed;         436 AA.
AC   P54247;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-MAY-2023, entry version 104.
DE   RecName: Full=Acetylcholine receptor non-alpha chain;
DE   Flags: Fragment;
OS   Onchocerca volvulus.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=6282;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8026747; DOI=10.1016/0378-1119(94)90216-x;
RA   Ajuh P.M., Egwang T.G.;
RT   "Cloning of a cDNA encoding a putative nicotinic acetylcholine receptor
RT   subunit of the human filarial parasite Onchocerca volvulus.";
RL   Gene 144:127-129(1994).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and leads to
CC       opening of an ion-conducting channel across the plasma membrane.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000305}.
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DR   EMBL; L20465; AAA21823.1; -; mRNA.
DR   EMBL; L12543; AAA29415.1; -; mRNA.
DR   AlphaFoldDB; P54247; -.
DR   SMR; P54247; -.
DR   STRING; 6282.P54247; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   Proteomes; UP000024404; Unassembled WGS sequence.
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; cd19064; LGIC_TM_nAChR; 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   PANTHER; PTHR18945:SF911; ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-TYPE UNC-38; 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; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           <1..436
FT                   /note="Acetylcholine receptor non-alpha chain"
FT                   /id="PRO_0000076982"
FT   TOPO_DOM        <1..195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..404
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        405..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        89..103
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   436 AA;  51340 MW;  58051BFE59A4555F CRC64;
     IIDVHEIDQI MTCSVWLKQV WIDKKLSWNP EIYGGVSVLY VPYEMVWVPD IVLYNTVDSN
     YNITISTKAT LRYDGQVTWD SPAIFKTLCQ IDVRWFPFDE QNCHFKFGSW TYTEDLLNLE
     LLDSDARYEL EMNENGELNN ITIFEEGIDL SDYYPSVEWD IMSRIAKRRT KNYLTSFSDE
     AFIDIIFYLE LRRKPLFYTV NLVFPCVGIS FLTIVAFYLP PRSGEKVTLC ILILVALTVF
     YLLLKDIIPA TSIALPLFGK YLLFTMIMVS LSVLVTVISL NLHFRRPSTH RMPIWVKWLF
     LRILPKILFM RRPTLIKVDE AVRRVADYRR GYNMIINRYE QKVNCDSCRN VNKRITQEIQ
     KIYRSPHVIK AFENVCFIAQ LLKKKDREAM IDEDWKFVAR VLDRLFLLLF SIACFLGTIL
     ILFQAPSLYD TRQAIN
//
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