ACM3_CAEEL
ID ACM3_CAEEL Reviewed; 611 AA.
AC Q9U7D5; Q7JKV1; Q9XW31;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Muscarinic acetylcholine receptor gar-3;
DE AltName: Full=G-protein-linked acetylcholine receptor 3;
GN Name=gar-3; ORFNames=Y40H4A.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAD48771.1};
RN [1] {ECO:0000312|EMBL:AAD48771.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAD48771.1};
RX PubMed=10635059;
RA Hwang J.M., Chang D.-J., Kim U.S., Lee Y.-S., Park Y.-S., Kaang B.-K.,
RA Cho N.J.;
RT "Cloning and functional characterization of a Caenorhabditis elegans
RT muscarinic acetylcholine receptor.";
RL Recept. Channels 6:415-424(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12927813; DOI=10.1016/s0006-291x(03)01508-0;
RA Park Y.-S., Kim S., Shin Y., Choi B., Cho N.J.;
RT "Alternative splicing of the muscarinic acetylcholine receptor GAR-3 in
RT Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 308:961-965(2003).
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-28 AND ASN-33, AND
RP IDENTIFICATION BY MASS 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 [5]
RP FUNCTION.
RX PubMed=18614679; DOI=10.1523/jneurosci.0378-08.2008;
RA Dittman J.S., Kaplan J.M.;
RT "Behavioral impact of neurotransmitter-activated G-protein-coupled
RT receptors: muscarinic and GABAB receptors regulate Caenorhabditis elegans
RT locomotion.";
RL J. Neurosci. 28:7104-7112(2008).
CC -!- FUNCTION: The muscarinic acetylcholine receptor mediates various
CC cellular responses, including inhibition of adenylate cyclase,
CC breakdown of phosphoinositides and modulation of potassium channels
CC through the action of G proteins (PubMed:10635059, PubMed:12927813).
CC Primary transducing effect is Pi turnover (By similarity). Enhances the
CC release of the neurotransmitter acetlycholine in cholinergic motor
CC neurons, which in turn positively feeds back to depolarize body wall
CC muscles and allows for the maintenance of normal body posture and
CC locomotion (PubMed:18614679). {ECO:0000250|UniProtKB:P20309,
CC ECO:0000269|PubMed:10635059, ECO:0000269|PubMed:12927813,
CC ECO:0000269|PubMed:18614679}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b; Synonyms=GAR-3a;
CC IsoId=Q9U7D5-1; Sequence=Displayed;
CC Name=a; Synonyms=GAR-3b;
CC IsoId=Q9U7D5-2; Sequence=VSP_012003;
CC -!- DEVELOPMENTAL STAGE: Isoform a and isoform b are expressed at all
CC developmental stages examined, isoform a is more abundant at embryonic
CC and early larval stages and isoform b at first larval instar.
CC {ECO:0000269|PubMed:12927813}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Muscarinic acetylcholine receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
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DR EMBL; AF139093; AAD48771.1; -; mRNA.
DR EMBL; AY221631; AAP97492.1; -; mRNA.
DR EMBL; AL034391; CAA22301.2; -; Genomic_DNA.
DR EMBL; Z81486; CAA22301.2; JOINED; Genomic_DNA.
DR EMBL; AL034391; CAE47471.1; -; Genomic_DNA.
DR EMBL; Z81486; CAE47471.1; JOINED; Genomic_DNA.
DR PIR; T20171; T20171.
DR PIR; T26789; T26789.
DR RefSeq; NP_001024235.1; NM_001029064.3. [Q9U7D5-2]
DR RefSeq; NP_001024236.1; NM_001029065.2. [Q9U7D5-1]
DR AlphaFoldDB; Q9U7D5; -.
DR SMR; Q9U7D5; -.
DR BioGRID; 44964; 2.
DR STRING; 6239.Y40H4A.1b; -.
DR iPTMnet; Q9U7D5; -.
DR PaxDb; Q9U7D5; -.
DR EnsemblMetazoa; Y40H4A.1a.1; Y40H4A.1a.1; WBGene00001519. [Q9U7D5-2]
DR EnsemblMetazoa; Y40H4A.1a.2; Y40H4A.1a.2; WBGene00001519. [Q9U7D5-2]
DR EnsemblMetazoa; Y40H4A.1a.3; Y40H4A.1a.3; WBGene00001519. [Q9U7D5-2]
DR EnsemblMetazoa; Y40H4A.1b.1; Y40H4A.1b.1; WBGene00001519. [Q9U7D5-1]
DR GeneID; 179962; -.
DR KEGG; cel:CELE_Y40H4A.1; -.
DR UCSC; Y40H4A.1b.1; c. elegans. [Q9U7D5-1]
DR CTD; 179962; -.
DR WormBase; Y40H4A.1a; CE27783; WBGene00001519; gar-3. [Q9U7D5-2]
DR WormBase; Y40H4A.1b; CE35800; WBGene00001519; gar-3. [Q9U7D5-1]
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000166540; -.
DR InParanoid; Q9U7D5; -.
DR OMA; TWACDLW; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; Q9U7D5; -.
DR Reactome; R-CEL-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-CEL-390650; Histamine receptors.
DR Reactome; R-CEL-416476; G alpha (q) signalling events.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9U7D5; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001519; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IMP:UniProtKB.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0001508; P:action potential; IMP:WormBase.
DR GO; GO:0007197; P:adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IMP:WormBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IMP:UniProtKB.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000995; Musac_Ach_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..611
FT /note="Muscarinic acetylcholine receptor gar-3"
FT /id="PRO_0000069050"
FT TOPO_DOM 1..67
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..88
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 102..122
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 123..140
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 141..161
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 162..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 182..202
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 203..227
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 228..248
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 249..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 526..546
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 547..557
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 558..578
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 579..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 299..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 138..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 271..296
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:10635059,
FT ECO:0000303|PubMed:12927813"
FT /id="VSP_012003"
SQ SEQUENCE 611 AA; 69563 MW; F1DD615020CA3180 CRC64;
MQSSSLGNAD DPRFRQTHLF QMLVKVINTS AENATKTAIA TSSTSTPSFV DTYSTSSLLG
EEGRMVMIVV IGAMFALVTS LGNLMVMVSF KIDKQLQTIS NYFLFSLAVA DIAIGVISIP
MFTYYTAIQK WDLGYTMCQF WLCIDYLMSN ASVLNLLLIS FDRYFSVTRP LSYRPRRTTK
KALTMIACTY IISLILWPPW IISWPYIEGK FTAEPGTCVV QFLQTNPYVT VGTAVAAFYL
PVTIMCILYT RVYWETQKRQ KEFGKLQATQ TWASDVVDRP STQSFRNSKM WKKVKKFSRR
SMKRDVSSTS IIKSSGSMRK KNNQDGYVED SVTPCTSSRN SKRKSWLRNC TGKSNSSSED
SSEAVAMNLD DTSLSSSHFA LSGSRRRNIS PPCTPMPTNF EDEEQTDAGA SMRNGSARFR
SRPSDTGKNN NSDTYTVLIE LNDEGSRPSV RLSSCEPYLD EPISTRNRSK SDCNSEIDER
RHSLLNKQSP FKNGRILKNF SSQERKSEKE QRKNERKQES KAAKTLSAIL CAFIATWTPY
NLIVCWEAFF PNTVPNVLWT FSYFLCYINS TINPLCYALC NARFRHTYMR ILRCKFKAER
PTMNQGYVRR N
