ACH5_CAEEL
ID ACH5_CAEEL Reviewed; 511 AA.
AC Q23022; O02559; P91265; Q17408;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Acetylcholine receptor subunit alpha-type unc-38;
DE AltName: Full=Uncoordinated protein 38;
DE Flags: Precursor;
GN Name=unc-38; ORFNames=F21F3.5;
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], AND FUNCTION.
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 NICOTINIC ACETYLCHOLINE RECEPTOR, SUBCELLULAR
RP LOCATION, AND DISRUPTION 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 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).
CC -!- FUNCTION: Alpha subunit of nicotinic acetylcholine receptor (nAChR)
CC (PubMed:9221782, 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 (PubMed:9221782, PubMed:15990870).
CC {ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:20027209,
CC ECO:0000269|PubMed:9221782}.
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). {ECO:0000269|PubMed:15990870,
CC ECO:0000269|PubMed:20027209}.
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 lev-1
CC and partially with acr-12 and acr-8 at nerve cord synapses.
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X98599; CAA67196.1; -; Genomic_DNA.
DR EMBL; X98600; CAA67197.1; -; mRNA.
DR EMBL; FO081197; CCD69819.1; -; Genomic_DNA.
DR PIR; T25720; T25720.
DR PIR; T43634; T43634.
DR RefSeq; NP_491472.1; NM_059071.5.
DR AlphaFoldDB; Q23022; -.
DR SMR; Q23022; -.
DR BioGRID; 37567; 3.
DR IntAct; Q23022; 4.
DR MINT; Q23022; -.
DR STRING; 6239.F21F3.5; -.
DR DrugBank; DB00848; Levamisole.
DR TCDB; 1.A.9.1.2; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR iPTMnet; Q23022; -.
DR EPD; Q23022; -.
DR PaxDb; Q23022; -.
DR EnsemblMetazoa; F21F3.5.1; F21F3.5.1; WBGene00006774.
DR GeneID; 172105; -.
DR KEGG; cel:CELE_F21F3.5; -.
DR UCSC; F21F3.5; c. elegans.
DR CTD; 172105; -.
DR WormBase; F21F3.5; CE24908; WBGene00006774; unc-38.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000171907; -.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; Q23022; -.
DR OMA; AYIDIMY; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; Q23022; -.
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:Q23022; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006774; Expressed in larva 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:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
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; IDA:WormBase.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IDA:WormBase.
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:0098662; P:inorganic cation transmembrane transport; IDA:WormBase.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IDA:WormBase.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
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 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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..511
FT /note="Acetylcholine receptor subunit alpha-type unc-38"
FT /id="PRO_0000000399"
FT TOPO_DOM 17..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..165
FT /evidence="ECO:0000250"
FT DISULFID 238..239
FT /evidence="ECO:0000250"
SQ SEQUENCE 511 AA; 59454 MW; 19F690731B23E1A6 CRC64;
MRSFWLFLLL LLFCISFIKL TEGNEDAKRL YDDLMVNYNR HRRPSTSPNK PLTIKLKLRL
SQIIDVHEID QIMTCSVWLK QTWIDRKLSW DPVNYGGVNV LYVPYEMIWV PDIVLYNNAD
SNYNITISTK ATLHYTGEVT WEPPAIFKSM CQIDVRWFPF DEQQCHLKFG SWTFSENLLS
VELNEPSLRY EEEIDEKGII DNVTVAEDGI DLSDYYPSVE WDIMSRVAKR RAKNYPSCCP
QSAYIDVTYY LQLRRKPLFY TVNLVFPCVG ISFLTILVFY LPSDSGEKVT LCISILVALT
IFFLLLTEII PATSITLPLI GKYLLFTMVM VTLSVVVTVI SLNLHFRTPT THLMPNWVKK
VFLKWLPKLL FMRRPIDDYE EKFDDKKKPK DGKIALSVHA HRVSNVGNNI RNATIDDTIQ
KMYYSPPVVK AFENICFIAE LLKKKDRDDK IDEDWKYVAM VLDRLFLLIF SIACFVGTVI
ILLRAPTLYD TRQPIDLQYR PANLSANPIS F
