ID   ACH6_CAEEL              Reviewed;         502 AA.
AC   Q9N587; Q964N6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Acetylcholine receptor subunit alpha-type unc-63;
DE   AltName: Full=Levamisole-resistant protein 7;
DE   AltName: Full=Uncoordinated protein 63;
DE   Flags: Precursor;
GN   Name=unc-63; Synonyms=lev-7; ORFNames=Y110A7A.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15280391; DOI=10.1074/jbc.m404370200;
RA   Culetto E., Baylis H.A., Richmond J.E., Jones A.K., Fleming J.T.,
RA   Squire M.D., Lewis J.A., Sattelle D.B.;
RT   "The Caenorhabditis elegans unc-63 gene encodes a levamisole-sensitive
RT   nicotinic acetylcholine receptor alpha subunit.";
RL   J. Biol. Chem. 279:42476-42483(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, INTERACTION WITH NICOTINIC ACETYLCHOLINE RECEPTOR, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15990870; DOI=10.1038/sj.emboj.7600741;
RA   Gottschalk A., Almedom R.B., Schedletzky T., Anderson S.D., Yates J.R. III,
RA   Schafer W.R.;
RT   "Identification and characterization of novel nicotinic receptor-associated
RT   proteins in Caenorhabditis elegans.";
RL   EMBO J. 24:2566-2578(2005).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH NICOTINIC ACETYLCHOLINE RECEPTOR.
RX   PubMed=20027209; DOI=10.1371/journal.pbio.1000265;
RA   Jospin M., Qi Y.B., Stawicki T.M., Boulin T., Schuske K.R., Horvitz H.R.,
RA   Bessereau J.L., Jorgensen E.M., Jin Y.;
RT   "A neuronal acetylcholine receptor regulates the balance of muscle
RT   excitation and inhibition in Caenorhabditis elegans.";
RL   PLoS Biol. 7:E1000265-E1000265(2009).
RN   [6]
RP   INTERACTION WITH LEV-10.
RX   PubMed=21252855; DOI=10.1038/emboj.2010.355;
RA   Rapti G., Richmond J., Bessereau J.L.;
RT   "A single immunoglobulin-domain protein required for clustering
RT   acetylcholine receptors in C. elegans.";
RL   EMBO J. 30:706-718(2011).
CC   -!- FUNCTION: Alpha subunit of nicotinic acetylcholine receptor (nAChR)
CC       (PubMed:15280391, PubMed:15990870, PubMed:20027209). Probably acts in
CC       cholinergic motoneurons to regulate presynaptic neurotransmitter
CC       release, thereby ensuring normal level of excitation of cholinergic
CC       motoneurons during locomotion (PubMed:20027209). Involved in nAChR
CC       sensitivity to nicotine and levamisole (PubMed:15280391,
CC       PubMed:15990870). {ECO:0000269|PubMed:15280391,
CC       ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:20027209}.
CC   -!- SUBUNIT: Component of nicotinic acetylcholine receptor
CC       (PubMed:15990870, PubMed:20027209). In muscles, composed of 2 non-alpha
CC       subunits lev-1 and unc-29, and 3 alpha subunits unc-38, unc-63 and lev-
CC       8 (PubMed:15990870). In cholinergic motoneurons, composed of 2 non-
CC       alpha subunits acr-2 and acr-3, and 3 alpha subunits unc-38, unc-63 and
CC       acr-12 (PubMed:20027209). Interacts with lev-10 (PubMed:21252855).
CC       {ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:20027209,
CC       ECO:0000269|PubMed:21252855}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q27218}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q27218}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in body wall muscles, in vulval muscles
CC       and in neurons. {ECO:0000269|PubMed:15280391}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a resistance to
CC       nicotine-mediated paralysis. {ECO:0000269|PubMed:15990870}.
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; AF288374; AAK83056.1; -; mRNA.
DR   EMBL; FO080728; CCD66192.1; -; Genomic_DNA.
DR   RefSeq; NP_491533.2; NM_059132.4.
DR   AlphaFoldDB; Q9N587; -.
DR   SMR; Q9N587; -.
DR   BioGRID; 37611; 3.
DR   DIP; DIP-42343N; -.
DR   IntAct; Q9N587; 1.
DR   MINT; Q9N587; -.
DR   STRING; 6239.Y110A7A.3; -.
DR   DrugBank; DB00848; Levamisole.
DR   DrugCentral; Q9N587; -.
DR   TCDB; 1.A.9.1.13; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   iPTMnet; Q9N587; -.
DR   EPD; Q9N587; -.
DR   PaxDb; Q9N587; -.
DR   EnsemblMetazoa; Y110A7A.3.1; Y110A7A.3.1; WBGene00006797.
DR   GeneID; 172150; -.
DR   KEGG; cel:CELE_Y110A7A.3; -.
DR   UCSC; Y110A7A.3; c. elegans.
DR   CTD; 172150; -.
DR   WormBase; Y110A7A.3; CE30706; WBGene00006797; unc-63.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000166039; -.
DR   HOGENOM; CLU_018074_1_0_1; -.
DR   InParanoid; Q9N587; -.
DR   OMA; IWITVCV; -.
DR   OrthoDB; 381858at2759; -.
DR   PhylomeDB; Q9N587; -.
DR   Reactome; R-CEL-629587; Highly sodium permeable postsynaptic acetylcholine nicotinic receptors.
DR   Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR   Reactome; R-CEL-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR   PRO; PR:Q9N587; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00006797; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:WormBase.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:WormBase.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IDA:WormBase.
DR   GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:WormBase.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IMP:WormBase.
DR   GO; GO:0040011; P:locomotion; IMP:WormBase.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR   GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
DR   GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0006937; P:regulation of muscle contraction; IGI:UniProtKB.
DR   GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR   Gene3D; 1.20.58.390; -; 2.
DR   Gene3D; 2.70.170.10; -; 1.
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; PTHR18945; 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; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..502
FT                   /note="Acetylcholine receptor subunit alpha-type unc-63"
FT                   /id="PRO_0000255715"
FT   TOPO_DOM        24..263
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        347..470
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   DISULFID        151..165
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  57391 MW;  3C09596F529DE6CB CRC64;
     MGPNDHGFAY ILIFLLLSPP THANRDANRL FEDLIADYNK LVRPVSENGE TLVVTFKLKL
     SQLLDVHEKN QIMTTNVWLQ HSWMDYKLRW DPVEYGGVEV LYVPSDTIWL PDVVLYNNAD
     GNYQVTIMTK AKLTYNGTVE WAPPAIYKSM CQIDVEFFPF DRQQCEMKFG SWTYGGLEVD
     LQHRDKHLEK EIEEDVEGVD GPTKEIVWVV DRGIDLSDYY PSVEWDILNV PGKRHSKRYP
     CCESPFIDIT YEIHLRRKTL FYTVNLIFPS VGISFLTALV FYLPSDGGEK ISLCISILIS
     LTVFFLLLVE IIPSTSLVIP LIGKYLLFTM VLVTLSVVVT VVTLNVHYRS PTTHTMPKWM
     KRLFVDFLPK YLLMTRPQPP GHHSKPNRKF DSRASTFSIG VNHVLGQNSE LLSPGLNSNR
     EESSFTLPRD NSPVRSAVES VAYIADHLKN EEDDKQVIED WKYISVVMDR IFLITFTFAC
     AFGTVVIIAR APSIYDNTPA LA