ACH7_CAEEL
ID ACH7_CAEEL Reviewed; 507 AA.
AC Q27218; O02278; Q19273;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Acetylcholine receptor subunit beta-type lev-1;
DE AltName: Full=Levamisole-resistant protein 1;
DE Flags: Precursor;
GN Name=lev-1; ORFNames=F09E8.7;
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 [GENOMIC DNA / MRNA].
RC STRAIN=Bristol N2;
RX PubMed=9221782; DOI=10.1523/jneurosci.17-15-05843.1997;
RA Fleming J.T., Squire M.D., Barnes T.M., Tornoe C., Matsuda K., Ahnn J.,
RA Fire A., Sulston J.E., Barnard E.A., Sattelle D.B., Lewis J.A.;
RT "Caenorhabditis elegans levamisole resistance genes lev-1, unc-29, and unc-
RT 38 encode functional nicotinic acetylcholine receptor subunits.";
RL J. Neurosci. 17:5843-5857(1997).
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 UNC-29, SUBCELLULAR LOCATION, 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-109, 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).
CC -!- FUNCTION: Non-alpha subunit of nicotinic acetylcholine receptor
CC (nAChR). Involved in nAChR sensitivity to nicotine.
CC {ECO:0000269|PubMed:15990870}.
CC -!- SUBUNIT: Interacts with unc-29. Component of nicotinic acetylcholine
CC receptor composed of 2 non-alpha subunits lev-1 and unc-29, and 3 alpha
CC subunits unc-38, unc-63 and lev-8. {ECO:0000269|PubMed:15990870}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:15990870}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:15990870}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Co-localizes with unc-29 and unc-
CC 38 at nerve cord synapses. {ECO:0000269|PubMed:15990870}.
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; X98601; CAA67198.1; -; mRNA.
DR EMBL; X98246; CAA66902.1; -; Genomic_DNA.
DR EMBL; Z81093; CAB03148.2; -; Genomic_DNA.
DR PIR; T22910; T22910.
DR RefSeq; NP_001255705.1; NM_001268776.1.
DR AlphaFoldDB; Q27218; -.
DR SMR; Q27218; -.
DR BioGRID; 43360; 2.
DR IntAct; Q27218; 3.
DR MINT; Q27218; -.
DR STRING; 6239.F09E8.7a; -.
DR DrugBank; DB00848; Levamisole.
DR iPTMnet; Q27218; -.
DR PaxDb; Q27218; -.
DR PRIDE; Q27218; -.
DR EnsemblMetazoa; F09E8.7a.1; F09E8.7a.1; WBGene00002974.
DR GeneID; 178269; -.
DR UCSC; F09E8.7; c. elegans.
DR CTD; 178269; -.
DR WormBase; F09E8.7a; CE24888; WBGene00002974; lev-1.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; Q27218; -.
DR OMA; NPNEFAG; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; Q27218; -.
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:Q27218; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002974; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q27218; baseline and differential.
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:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; 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; IMP: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:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IMP:WormBase.
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:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..507
FT /note="Acetylcholine receptor subunit beta-type lev-1"
FT /id="PRO_0000000403"
FT TOPO_DOM 32..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 373..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 163..177
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 58026 MW; 6111C3BC3984111E CRC64;
MMLGGGGGCG AGGTWLGFLV FLAVSLRNHS TCEDIDAEDR LMVDLFRGYN SLVQPVRNRS
ELPMIVKIGM QLVLLINVDE KEQVMHTNVW LTMKWDDFQL KWDPRDYANI TQIRVAPEKV
WLPDIVLFNN ADGNYEVSFM CNVLILSTGT VLWVPPAIYK SSCIIDVEFF PFDDQLCSLT
FGSWTYNRDE IKLDFLTSDR VDFSEYSTSS IWDMMDGPAV LTSDRSRIEF QIRIRRKTLF
YTVVLILPTV LMAFLNVTVF YLPTASGEKM GLTMNVLLSI VVFLLLVSKI LPPTSSSIPL
VAKYLLLTFV LNIITIMVTT IICNIYFRSP ITHRLPPWVR KVFLDILPLL MCMQRPHRKN
VIQRSHRRLL ETGPSVEENP MRSGEHHPLC RHTHNQDSCR RVRIQSDELD DELSPEAQRA
IDAIEFITEN RRDEEITKQF RDDWKFIASV VDRFLLYGFF GATVGGTIGI IFTAPSVFET
FDENATLVKL KQLYDMGLAN DTVLGIF
