ACH23_CAEEL
ID ACH23_CAEEL Reviewed; 545 AA.
AC G5EG88;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Betaine receptor acr-23 {ECO:0000303|PubMed:24212673};
DE AltName: Full=Acetylcholine receptor subunit alpha-type acr-23;
DE Flags: Precursor;
GN Name=acr-23 {ECO:0000312|EMBL:CCD72123.1, ECO:0000312|WormBase:F59B1.9a};
GN ORFNames=5E130, F59B1.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CCD72123.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD72123.1};
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 [2] {ECO:0000312|EMBL:AAR89634.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Thierry-Mieg D.,
RA Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=11967372; DOI=10.1110/ps.3040102;
RA Mongan N.P., Jones A.K., Smith G.R., Sansom M.S., Sattelle D.B.;
RT "Novel alpha7-like nicotinic acetylcholine receptor subunits in the
RT nematode Caenorhabditis elegans.";
RL Protein Sci. 11:1162-1171(2002).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ILE-301 AND PRO-311.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:24212673};
RX PubMed=24212673; DOI=10.1038/nn.3575;
RA Peden A.S., Mac P., Fei Y.J., Castro C., Jiang G., Murfitt K.J.,
RA Miska E.A., Griffin J.L., Ganapathy V., Jorgensen E.M.;
RT "Betaine acts on a ligand-gated ion channel in the nervous system of the
RT nematode C. elegans.";
RL Nat. Neurosci. 16:1794-1801(2013).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-112 AND ALA-321.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:23950710};
RX PubMed=23950710; DOI=10.1371/journal.ppat.1003524;
RA Rufener L., Bedoni N., Baur R., Rey S., Glauser D.A., Bouvier J., Beech R.,
RA Sigel E., Puoti A.;
RT "acr-23 encodes a monepantel-sensitive channel in Caenorhabditis elegans.";
RL PLoS Pathog. 9:E1003524-E1003524(2013).
CC -!- FUNCTION: Betaine receptor that functions as a ligand-gated non-
CC selective monovalent cation channel in mechanosensory neurons to
CC maintain basal levels of locomotion. The channel is permeable to Na(+)
CC and K(+) but not to Ba(2+) or Ca(2+) ions. Elicits current in response
CC to betaine, very weak current in response to choline, virtually no
CC current in response to acetylcholine and nicotine, and no current in
CC response to glycine and GABA. {ECO:0000269|PubMed:23950710,
CC ECO:0000269|PubMed:24212673}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23950710,
CC ECO:0000269|PubMed:24212673}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24212673, ECO:0000305|PubMed:23950710}.
CC -!- TISSUE SPECIFICITY: Expressed in the body wall muscles that are
CC arranged into four longitudinal bundles, some mechanosensory neurons,
CC the head muscles and multiple interneurons. Not expressed in motor
CC neurons (at protein level). {ECO:0000269|PubMed:23950710,
CC ECO:0000269|PubMed:24212673}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in embryos and L1 stage but
CC expressed from L2 stage to adulthood in the body wall muscles (at
CC protein level). {ECO:0000269|PubMed:23950710}.
CC -!- DISRUPTION PHENOTYPE: Mutant worms are morphologically similar to the
CC wild-type but exhibit mild swimming defects and are lethargic with
CC their movement being interrupted by frequent pauses when crawling on a
CC food-free environment (PubMed:24212673). On the same environment, in
CC other occasions they display decreased rates of spontaneous reversal
CC and steering, and slightly increased average speed (PubMed:23950710).
CC Homozygotes are fully resistant to monepantel but heterozygotes are
CC partially affected by the drug with reduced fertility and slightly
CC impaired movement. {ECO:0000269|PubMed:23950710,
CC ECO:0000269|PubMed:24212673}.
CC -!- MISCELLANEOUS: Suppresses snf-3 mutant phenotype growth defects.
CC Elicits no current in response to the broad-spectrum antiparasitic
CC medicine ivermectin. This channel is allosterically sensitive to
CC monepantel, an anthelmintic of the amino-acetonitrile derivatives
CC (AADs) class, leading to muscle paralysis upon treatment with
CC monepantel. {ECO:0000269|PubMed:23950710, ECO:0000269|PubMed:24212673}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Acetylcholine receptor (TC 1.A.9.1) subfamily. {ECO:0000255}.
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DR EMBL; FO081512; CCD72123.1; -; Genomic_DNA.
DR EMBL; AY519853; AAR89634.1; -; mRNA.
DR PIR; A89008; A89008.
DR RefSeq; NP_504024.2; NM_071623.4.
DR AlphaFoldDB; G5EG88; -.
DR STRING; 6239.F59B1.9; -.
DR PaxDb; G5EG88; -.
DR PeptideAtlas; G5EG88; -.
DR EnsemblMetazoa; F59B1.9a.1; F59B1.9a.1; WBGene00000062.
DR GeneID; 191606; -.
DR CTD; 191606; -.
DR WormBase; F59B1.9a; CE36939; WBGene00000062; acr-23.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_2_5_1; -.
DR InParanoid; G5EG88; -.
DR OMA; VERWVDQ; -.
DR OrthoDB; 1664236at2759; -.
DR PhylomeDB; G5EG88; -.
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:G5EG88; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000062; Expressed in larva.
DR ExpressionAtlas; G5EG88; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 1.
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 PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 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; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..545
FT /note="Betaine receptor acr-23"
FT /evidence="ECO:0000255"
FT /id="PRO_0000425863"
FT TOPO_DOM 20..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..171
FT /evidence="ECO:0000250|UniProtKB:P02708"
FT DISULFID 224..225
FT /note="Associated with receptor activation"
FT /evidence="ECO:0000250|UniProtKB:P02708"
FT MUTAGEN 112
FT /note="D->N: In cb101; highly resistant to monepantel."
FT /evidence="ECO:0000269|PubMed:23950710"
FT MUTAGEN 301
FT /note="I->N: Increases sensitivity to betaine. Leads to
FT death during larval development in most cases, with
FT escapees reaching to adulthood but being hypercontracted
FT and uncoordinated."
FT /evidence="ECO:0000269|PubMed:24212673"
FT MUTAGEN 311
FT /note="P->L: In ox429; mild swimming defects and lethargic
FT movement when crawling on a food-free environment."
FT /evidence="ECO:0000269|PubMed:24212673"
FT MUTAGEN 321
FT /note="A->T: In cb103; highly resistant to monepantel."
FT /evidence="ECO:0000269|PubMed:23950710"
SQ SEQUENCE 545 AA; 62549 MW; E23060B59A170221 CRC64;
MHRIYTFLIF ISQLALGLSN NPDIPIQYEL ANNIMENYQK GLIPKVRKGS PINVTLSLQL
YQIIQVNEPQ QYLLLNAWAV ERWVDQMLGW DPSEFDNETE IMARHDDIWL PDTTLYNSLE
MDDSASKKLT HVKLTTLGKN QGAMVELLYP TIYKISCLLN LKYFPFDTQT CRMTFGSWSF
DNSLIDYFPR TFTNGPIGLA NFLENDAWSV LGTKVNREEK KYTCCPVNYT LLHYDVVIQR
KPLYYVLNLI APTAVITFIS IIGFFTSVNP FTNFCNVSSS VHDLRQEKIT LGITTLLSMS
IMIFMVSDKM PSTSTCVPLI ALFYTLMITI ISVGTLAASS VIFVQKLGSI GNPPASKTMK
WTHRIAPFVL IQMPLVMKQA YAKRAKEEKH RKRMSRKNSM WTKVYHLARD HSKLMETVPD
GAVKFNQISD FKNNDIGNME SPRMAESQTS ETFAAPMDTS FTESLHIPEL NRVASSNSIQ
SVLKPTEIQL TPYCTRNIVE LEWDWVAAVL ERVFLIFFTI CFLFSAIGIN LYGWYIWYTE
NHFLF
