ACH4_CAEEL
ID ACH4_CAEEL Reviewed; 548 AA.
AC O76554;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Acetylcholine receptor subunit alpha-type des-2;
DE Flags: Precursor;
GN Name=des-2; Synonyms=acr-4; ORFNames=T26H10.1;
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], INTERACTION WITH DEG-3, 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 [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 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 [4]
RP INTERACTION WITH DEG-3 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 [5]
RP INTERACTION WITH DEG-3 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).
CC -!- FUNCTION: Subunit of the non-synaptic neuronal acetylcholine receptor
CC (AChR), which may play a role in chemotaxis towards choline. After
CC binding choline or acetylcholine, the AChR responds by an extensive
CC change in conformation that affects all subunits and leads to opening
CC of an ion-conducting channel across the plasma membrane.
CC {ECO:0000269|PubMed:11273652, 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: Cell membrane {ECO:0000269|PubMed:11273652};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11273652}.
CC Note=Enriched in the sensory endings of sensory neurons.
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; AF077307; AAC98095.1; -; mRNA.
DR EMBL; Z74044; CAA98550.1; -; Genomic_DNA.
DR EMBL; Z74039; CAA98550.1; JOINED; Genomic_DNA.
DR PIR; T23270; T23270.
DR RefSeq; NP_001256320.1; NM_001269391.1.
DR AlphaFoldDB; O76554; -.
DR SMR; O76554; -.
DR BioGRID; 44600; 2.
DR IntAct; O76554; 1.
DR STRING; 6239.T26H10.1b; -.
DR iPTMnet; O76554; -.
DR EPD; O76554; -.
DR PaxDb; O76554; -.
DR EnsemblMetazoa; T26H10.1a.1; T26H10.1a.1; WBGene00000955.
DR EnsemblMetazoa; T26H10.1a.2; T26H10.1a.2; WBGene00000955.
DR GeneID; 179574; -.
DR KEGG; cel:CELE_T26H10.1; -.
DR UCSC; T26H10.1; c. elegans.
DR CTD; 179574; -.
DR WormBase; T26H10.1a; CE21208; WBGene00000955; des-2.
DR eggNOG; KOG3645; Eukaryota.
DR HOGENOM; CLU_018074_2_5_1; -.
DR InParanoid; O76554; -.
DR PhylomeDB; O76554; -.
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:O76554; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000955; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; O76554; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
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; 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..548
FT /note="Acetylcholine receptor subunit alpha-type des-2"
FT /id="PRO_0000302736"
FT TOPO_DOM 21..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 422..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 548 AA; 62096 MW; A7495B31CFF5ACE5 CRC64;
MLIIIQSLLL ATTASLCIAD TPVPTQIRLV HDLLDNYDKK AKPMWDNSKP INVSFSMDLY
QILELNEPQQ YILLNAWIIE RWFDEFLYWN PDDYENITEL RLPYDSIWLP DTTLYNSLVM
KDDDTRRLLN SKLTTDTHRR AALIELLYPT IYKFSCLLDL RFFPFDVQVC TMTFSSWTYD
QKGIDYFPYS DKIGTSNYLE NEGWYILQTK IKRQEVKYAC CPNNYTLLQL TLYLRRKPLF
YLVNLIIPTS IITLIAIVGF FTTSSASGMR EEKVSLGITT LLSMSILMLM VSDQMPTTST
FIPLIGWFIL AMIIVISLGT VVSSVIIAIQ KRGSLGERMS KRALKFAKVL AWFTCTSLPP
HVEKEHMMEA FDAPTPLVEV RPLQLASVKE SVRNKWVSGA RRATQRGNSG LALISDKSTD
PLIHLSPTAH QPDESISPSA PPVPSSSPLP PPLTPGPADD VVSVASELSS KFLTSRMRPK
SQKDNTFAAM QSSIKANRQL AVAEFEWFAT VVERTCFVIF VVAFLIITFG INFIGFIHWH
QAGVEYGG
