ACH2_CAEEL
ID ACH2_CAEEL Reviewed; 493 AA.
AC P48181; O02520; O02600; Q94014;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Acetylcholine receptor subunit beta-type unc-29;
DE AltName: Full=Uncoordinated protein 29;
DE Flags: Precursor;
GN Name=unc-29 {ECO:0000312|WormBase:T08G11.5};
GN ORFNames=T08G11.5 {ECO:0000312|WormBase:T08G11.5};
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 [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=8627624; DOI=10.1006/jmbi.1996.0248;
RA Ballivet M., Alliod C., Bertrand S., Bertrand D.;
RT "Nicotinic acetylcholine receptors in the nematode Caenorhabditis
RT elegans.";
RL J. Mol. Biol. 258:261-269(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
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 [4]
RP FUNCTION, INTERACTION WITH LEV-1, 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 [5]
RP INTERACTION WITH OIG-4.
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).
RN [6]
RP INTERACTION WITH CRLD-1.
RX PubMed=30407909; DOI=10.7554/elife.39649;
RA D'Alessandro M., Richard M., Stigloher C., Gache V., Boulin T.,
RA Richmond J.E., Bessereau J.L.;
RT "CRELD1 is an evolutionarily-conserved maturational enhancer of ionotropic
RT acetylcholine receptors.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Non-alpha subunit of nicotinic acetylcholine receptor
CC (nAChR). Involved in nAChR sensitivity to nicotine and levasimole.
CC {ECO:0000269|PubMed:15990870}.
CC -!- SUBUNIT: Interacts with lev-1 (PubMed:15990870). Component of nicotinic
CC acetylcholine receptor composed of 2 non-alpha subunits lev-1 and unc-
CC 29, and 3 alpha subunits unc-38, unc-63 and lev-8 (PubMed:15990870).
CC Interacts with oig-4 (PubMed:21252855). Interacts with crld-1
CC (PubMed:30407909). {ECO:0000269|PubMed:15990870,
CC ECO:0000269|PubMed:21252855, ECO:0000269|PubMed:30407909}.
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-38 and lev-1
CC at nerve cord synapses. {ECO:0000269|PubMed:15990870}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a resistance to
CC nicotine-mediated paralysis and small impairment in mobility.
CC {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; X83888; CAA58765.1; -; mRNA.
DR EMBL; U81144; AAB39358.1; -; Genomic_DNA.
DR EMBL; BX284601; CAB02308.1; -; Genomic_DNA.
DR PIR; S68587; S68587.
DR PIR; T24695; T24695.
DR RefSeq; NP_492399.1; NM_059998.4.
DR AlphaFoldDB; P48181; -.
DR SMR; P48181; -.
DR BioGRID; 38136; 159.
DR IntAct; P48181; 139.
DR MINT; P48181; -.
DR STRING; 6239.T08G11.5.2; -.
DR DrugBank; DB00848; Levamisole.
DR TCDB; 1.A.9.1.16; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR EPD; P48181; -.
DR PaxDb; P48181; -.
DR EnsemblMetazoa; T08G11.5.1; T08G11.5.1; WBGene00006765.
DR GeneID; 172703; -.
DR KEGG; cel:CELE_T08G11.5; -.
DR UCSC; T08G11.5; c. elegans.
DR CTD; 172703; -.
DR WormBase; T08G11.5; CE13451; WBGene00006765; unc-29.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_1_0_1; -.
DR InParanoid; P48181; -.
DR OMA; RWMMEIP; -.
DR OrthoDB; 381858at2759; -.
DR PhylomeDB; P48181; -.
DR Reactome; R-CEL-629594; Highly calcium permeable postsynaptic nicotinic acetylcholine receptors.
DR Reactome; R-CEL-629597; Highly calcium permeable nicotinic acetylcholine receptors.
DR SignaLink; P48181; -.
DR PRO; PR:P48181; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006765; 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:0043025; C:neuronal cell body; 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; 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: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:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IMP:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IGI: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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..493
FT /note="Acetylcholine receptor subunit beta-type unc-29"
FT /id="PRO_0000000396"
FT TOPO_DOM 27..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 155..169
FT /evidence="ECO:0000250"
FT CONFLICT 355
FT /note="S -> T (in Ref. 1; CAA58765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 56497 MW; EBE1D5CC40D25EB6 CRC64;
MRTNRLSWIL VLSVVIFLVI INTINASDDE ERLMVDVFRG YNSLIQPVRN SSELPLIVKM
ALQLVLLINV DEKDQVMHTN VWLTLQWHDF QMKWNPVNYG EIKQIRVSPD KVWLPDIVLF
NNADGNYEVS FMCNVVINHK GDMLWVPPAI YKSSCIIDVE FFPFDEQVCT LVFGSWTYNE
NEIKLEFVQA ELVDVSEYSA SSIWDVIDVP ASLVNKRSRI EFQVRIRRKT LFYTVVLIIP
TVLMAFLSMA VFFLPTDSGE KITLTISVLL SIVVFLLLVS KILPPTSSTI PLMAKYLLLT
FVLNVITILV TVIIINVYFR GPRTHRMPQW VRVVFLQFLP KLVCMKRPKS ASERSAVRSG
MAQLPGVGQF TLSPSAHHPL CPSADDRTTT IRNTASNETS AYYPLSTDAL RAIDAIEYIT
EHLKRDEQHK SFRDDWKYVA MIIDRLLLYV FFGITVGGTC GILFSAPHVF QRIDQQEMLD
RLKEKYDTAS NIP
