ACH3_CAEEL
ID ACH3_CAEEL Reviewed; 564 AA.
AC P54244;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Acetylcholine receptor subunit alpha-type deg-3;
DE Flags: Precursor;
GN Name=deg-3; ORFNames=K03B8.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND MUTAGENESIS OF ILE-314.
RC STRAIN=Bristol N2;
RX PubMed=7718248; DOI=10.1016/0896-6273(95)90231-7;
RA Treinin M., Chalfie M.;
RT "A mutated acetylcholine receptor subunit causes neuronal degeneration in
RT C. elegans.";
RL Neuron 14:871-877(1995).
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 INTERACTION WITH DES-2, AND FUNCTION.
RX PubMed=9860996; DOI=10.1073/pnas.95.26.15492;
RA Treinin M., Gillo B., Liebman L., Chalfie M.;
RT "Two functionally dependent acetylcholine subunits are encoded in a single
RT Caenorhabditis elegans operon.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15492-15495(1998).
RN [4]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11273652; DOI=10.1006/mcne.2000.0944;
RA Yassin L., Gillo B., Kahan T., Halevi S., Eshel M., Treinin M.;
RT "Characterization of the deg-3/des-2 receptor: a nicotinic acetylcholine
RT receptor that mutates to cause neuronal degeneration.";
RL Mol. Cell. Neurosci. 17:589-599(2001).
RN [5]
RP INTERACTION WITH DES-2 AND RIC-3.
RX PubMed=11867529; DOI=10.1093/emboj/21.5.1012;
RA Halevi S., McKay J., Palfreyman M., Yassin L., Eshel M., Jorgensen E.,
RA Treinin M.;
RT "The C. elegans ric-3 gene is required for maturation of nicotinic
RT acetylcholine receptors.";
RL EMBO J. 21:1012-1020(2002).
RN [6]
RP INTERACTION WITH DES-2 AND RIC-3.
RX PubMed=15932871; DOI=10.1074/jbc.m504369200;
RA Ben-Ami H.C., Yassin L., Farah H., Michaeli A., Eshel M., Treinin M.;
RT "RIC-3 affects properties and quantity of nicotinic acetylcholine receptors
RT via a mechanism that does not require the coiled-coil domains.";
RL J. Biol. Chem. 280:28053-28060(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37, 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 [8]
RP MUTAGENESIS OF ILE-314.
RX PubMed=17891142; DOI=10.1038/nn1981;
RA Van Buskirk C., Sternberg P.W.;
RT "Epidermal growth factor signaling induces behavioral quiescence in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 10:1300-1307(2007).
CC -!- FUNCTION: Subunit of the non-synaptic neuronal acetylcholine receptor,
CC which may play a role in chemotaxis towards choline. After binding
CC choline or acetylcholine, the AChR responds by an extensive change in
CC conformation that affects all subunits and leads to opening of an ion-
CC conducting channel across the plasma membrane (PubMed:9860996,
CC PubMed:11273652). {ECO:0000269|PubMed:11273652,
CC ECO:0000269|PubMed:9860996}.
CC -!- SUBUNIT: The functional receptor is a heteromer of deg-3 and des-2.
CC Interacts with ric-3; which is required for proper receptor folding.
CC {ECO:0000269|PubMed:11867529, ECO:0000269|PubMed:15932871,
CC ECO:0000269|PubMed:9860996}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:11273652}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11273652}. Cell membrane
CC {ECO:0000269|PubMed:11273652}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11273652}. Note=Enriched in the sensory endings of
CC sensory neurons.
CC -!- MISCELLANEOUS: This locus is redundant or nonessential as suppression
CC of deg-3 function results in wild-type revertants.
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; U19747; AAA92689.1; -; mRNA.
DR EMBL; U19746; AAA92688.1; -; Genomic_DNA.
DR EMBL; Z74039; CAA98507.1; -; Genomic_DNA.
DR PIR; T23269; T23269.
DR RefSeq; NP_505897.1; NM_073496.5.
DR AlphaFoldDB; P54244; -.
DR SMR; P54244; -.
DR BioGRID; 532518; 2.
DR STRING; 6239.K03B8.9.1; -.
DR TCDB; 1.A.9.1.14; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR iPTMnet; P54244; -.
DR PaxDb; P54244; -.
DR EnsemblMetazoa; K03B8.9.1; K03B8.9.1; WBGene00000951.
DR EnsemblMetazoa; K03B8.9.2; K03B8.9.2; WBGene00000951.
DR GeneID; 3565200; -.
DR KEGG; cel:CELE_K03B8.9; -.
DR UCSC; K03B8.9.2; c. elegans.
DR CTD; 3565200; -.
DR WormBase; K03B8.9; CE06083; WBGene00000951; deg-3.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_0_2_1; -.
DR InParanoid; P54244; -.
DR OMA; IPNEEWQ; -.
DR OrthoDB; 406640at2759; -.
DR PhylomeDB; P54244; -.
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:P54244; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000951; Expressed in larva and 2 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; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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: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:0043067; P:regulation of programmed cell death; 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 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; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..564
FT /note="Acetylcholine receptor subunit alpha-type deg-3"
FT /id="PRO_0000000397"
FT TOPO_DOM 21..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 185..199
FT /evidence="ECO:0000250"
FT DISULFID 248..249
FT /evidence="ECO:0000250"
FT MUTAGEN 314
FT /note="I->N: In u662; degeneration of a set of touch
FT receptor neurons, including ALA neurons, probably due to
FT channel hyperactivity (gain-of-function). Uncoordinated,
FT insensitive to both gentle and harsh stimuli, and display
FT vacuolated cell death. Restores normal pharyngeal pumping
FT rate in animals overexpressing lin-3."
FT /evidence="ECO:0000269|PubMed:17891142,
FT ECO:0000269|PubMed:7718248"
SQ SEQUENCE 564 AA; 64927 MW; BA38F7F05B987B9E CRC64;
MTLKIRTIII LFCVISVTTT SQSLNATLKT FDPRLLNSTA DRDIAMKNVP LVRLTRHLLS
PERYDVRVRP ILDHKKSLKV HISISLYQII EVDEPSQNIK LNVWMIQKWR DEYLDWNPNE
YGMINSTIIP FHHLWIPDTY LYNSVKMSRD ETERYMNIQA TSNYWKGEKG AELSFLYPAI
YTITCRLNIR FFPYDRQNCT LTISSWTNSK SALDYYADTE VSMQSFIPNE EWQVKSFKIH
RHEYKYACCA EPWVILQASL VIQRKPLYYL VNLIIPTSII TLVAITGFFT PASTDDDRTE
KINLGITTLL AMSILMLMVS DQMPTTSEFV PLIAWFYLSI IIIISIGTFL TSVVLSVQGR
RQYGRNPPQF IRYIFFVLLP QVLLLNVPPP LQTLWGELDD DPLNVRRRKK SHYLSRNVNN
GSTKMASPMS TLRVPQSAGS VSEKRQSFQM IDVTSPNSPN TARSRAPSLA PSTAKATMWE
GTMSALAGTN TQLRRTSNVF NKEVDEMRRK RQCSLEWEFL ATVLDRFLLI VFVGAVVIVT
AGLILVGRMA QYSYDHPDDR FFNV
