ACM2_CAEEL
ID ACM2_CAEEL Reviewed; 627 AA.
AC Q09388; Q09561; Q95WX7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Muscarinic acetylcholine receptor gar-2 {ECO:0000303|PubMed:11032868};
DE AltName: Full=G-protein-linked acetylcholine receptor 2;
GN Name=gar-2 {ECO:0000312|WormBase:F47D12.1a};
GN ORFNames=F47D12.1 {ECO:0000312|WormBase:F47D12.1a};
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] (ISOFORM B), AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=11032868; DOI=10.1046/j.1471-4159.2000.0751800.x;
RA Lee Y.-S., Park Y.-S., Nam S., Suh S.J., Lee J., Kaang B.-K., Cho N.J.;
RT "Characterization of GAR-2, a novel G protein-linked acetylcholine receptor
RT from Caenorhabditis elegans.";
RL J. Neurochem. 75:1800-1809(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11700045; DOI=10.1006/bbrc.2001.5909;
RA Suh S.J., Park Y.-S., Lee Y.-S., Cho T.J., Kaang B.-K., Cho N.J.;
RT "Three functional isoforms of GAR-2, a Caenorhabditis elegans G-protein-
RT linked acetylcholine receptor, are produced by alternative splicing.";
RL Biochem. Biophys. Res. Commun. 288:1238-1243(2001).
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, AND DISRUPTION PHENOTYPE.
RX PubMed=12954868; DOI=10.1523/jneurosci.23-22-08060.2003;
RA Bany I.A., Dong M.Q., Koelle M.R.;
RT "Genetic and cellular basis for acetylcholine inhibition of Caenorhabditis
RT elegans egg-laying behavior.";
RL J. Neurosci. 23:8060-8069(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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:11032868, PubMed:11700045).
CC Primary transducing effect is Pi turnover (By similarity). Regulates
CC the activity of ventral cord motor neurons (PubMed:18614679). Couples
CC to the G(o)-alpha G-protein subunit goa-1 to negatively regulate
CC cholinergic receptor activity in the presence of high levels of the
CC neurotransmitter acetylcholine in ventral cord motor neurons
CC (PubMed:18614679). As acetylcholine depolarizes body wall muscles,
CC modulation of acetylcholine levels most likely results in the control
CC locomotory behavior and egg-laying (PubMed:12954868, PubMed:18614679).
CC {ECO:0000250|UniProtKB:P20309, ECO:0000269|PubMed:11032868,
CC ECO:0000269|PubMed:11700045, ECO:0000269|PubMed:12954868,
CC ECO:0000269|PubMed:18614679}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11700045};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P08172}. Cell
CC projection, axon {ECO:0000269|PubMed:18614679}. Note=Diffusely
CC localized in axons. {ECO:0000269|PubMed:18614679}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F47D12.1a};
CC IsoId=Q09388-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F47D12.1b}; Synonyms=c
CC {ECO:0000303|PubMed:11700045};
CC IsoId=Q09388-2; Sequence=VSP_001862;
CC -!- TISSUE SPECIFICITY: Expressed in putative sensory neurons, many cells
CC of the ventral cord and in the HSN motor neurons (PubMed:11032868).
CC Expressed in some cholinergic motor neurons and GABAergic motor
CC neurons, which are the two major types of ventral cord motor neurons
CC (PubMed:18614679). {ECO:0000269|PubMed:11032868,
CC ECO:0000269|PubMed:18614679}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from the embryo
CC to the adult (PubMed:11032868, PubMed:11700045). Expressed in the head
CC region of larva (PubMed:11032868). {ECO:0000269|PubMed:11032868,
CC ECO:0000269|PubMed:11700045}.
CC -!- DISRUPTION PHENOTYPE: Egg-laying defect whereby 30% of eggs are laid at
CC an early developmental stage (PubMed:12954868). Increased sensitivity
CC to the acetylcholine esterase inhibitor Aldicarb, which results in
CC accelerated paralysis likely due to enhanced acetylcholine release by
CC ventral cord neurons and enhanced depolarization of muscles on one side
CC of the body (PubMed:18614679). Exploratory behavior is similar to wild-
CC type, but in contrast to wild-type, there is irregular locomotory
CC behavior characterized by a 9.2% increase in speed of locomotion over a
CC 1-minute interval, decreased turning frequency, reduced rate of
CC reversals, and a 25% increase in the maximal distance covered over a 40
CC second interval (PubMed:18614679). Double knockout with the G-protein
CC coupled receptor for GABA subunit gbb-2 results in a slight increase in
CC sensitivity to Aldicarb and accelerated paralysis 50 minutes following
CC exposure to Aldicarb as compared to the gar-2 and gbb-2 single mutants
CC (PubMed:18614679). {ECO:0000269|PubMed:12954868,
CC ECO:0000269|PubMed:18614679}.
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; AF272738; AAK94896.1; -; mRNA.
DR EMBL; AY053365; AAL15153.1; -; mRNA.
DR EMBL; FO080618; CCD83363.1; -; Genomic_DNA.
DR EMBL; FO080618; CCD83364.1; -; Genomic_DNA.
DR RefSeq; NP_001022593.1; NM_001027422.3. [Q09388-1]
DR RefSeq; NP_001022594.1; NM_001027423.4. [Q09388-2]
DR AlphaFoldDB; Q09388; -.
DR SMR; Q09388; -.
DR STRING; 6239.F47D12.1c; -.
DR EnsemblMetazoa; F47D12.1a.1; F47D12.1a.1; WBGene00001518. [Q09388-1]
DR EnsemblMetazoa; F47D12.1b.1; F47D12.1b.1; WBGene00001518. [Q09388-2]
DR GeneID; 175893; -.
DR UCSC; F47D12.1d; c. elegans. [Q09388-1]
DR CTD; 175893; -.
DR WormBase; F47D12.1a; CE30134; WBGene00001518; gar-2. [Q09388-1]
DR WormBase; F47D12.1b; CE30135; WBGene00001518; gar-2. [Q09388-2]
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q09388; -.
DR PRO; PR:Q09388; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001518; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q09388; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IDA:WormBase.
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:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:WormBase.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0032223; P:negative regulation of synaptic transmission, cholinergic; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IBA:GO_Central.
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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW G-protein coupled receptor; Membrane; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..627
FT /note="Muscarinic acetylcholine receptor gar-2"
FT /id="PRO_0000069049"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 31..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 63..81
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 82..102
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 103..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..143
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 144..172
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 173..193
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 194..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 550..570
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 571..586
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 587..609
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 610..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 222..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 79..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 520..532
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:11032868"
FT /id="VSP_001862"
SQ SEQUENCE 627 AA; 71483 MW; CB319E3BA8230AE5 CRC64;
MAVASVLLAL FMLFLSIVTV IGNLAVLLSY YLDKNIRQPT NYFIFSLAIS DLLIGLEGIP
VYTAFYLNNN EWIWGDVLCD LWLSIDYIVC LASIYTVLGI TVDRYYSVKK PATYRNWRTP
GRVVLIIIFI WLVPSILFSV SIFGYGTFTG TGRILKETEC YVQFMTNPYL NMGMYISYYW
TTLFVMLYLY WGIYRAAKKL ALKSDQKTKR LALLTEMRRP EVSVRTSDAG NSSSDSPNDT
SNSSKCFRTA PPTTTVQTTQ TNVGTPPPVF RNHMTLHNNN MDFTKDNEIV RPPTPPDDNT
YSNPNFSMIS EQLTNGFSRQ EPSSVIERES TAPCVSPEPS HASLENEFNE NHHAHFKPEL
SLPFIDADSV SSMVGHDDLR RAMSIRISRS VSMQGTARAT PVIEIVENLE EALKICENLE
ELREDENKNE EEKQKNGLEN GGMNHVIIAN DEQQPSTSKE SEQKEEMTPE NHDPNEVKVP
LIAVSRVESV KSTAGGKVRR LITQMRSHSI RSKRKANKNK SVLSALNFFQ RKKEYKSRSE
NRARKALRTI TFILGSFIIL WTPFYVLATI YGFCETCKAS PSFNTLYTIS YYLCYMNSPL
NPFCYAMANQ QFKKTLTRIF KGDFRRV
