ACM1_DROME
ID ACM1_DROME Reviewed; 805 AA.
AC P16395; G4LU59; M9NHK8; M9NKN3; Q1ECB8; Q8MLP2; Q9W180;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Muscarinic acetylcholine receptor DM1;
GN Name=mAChR-A; Synonyms=AcrC, mAcR-60C; ORFNames=CG4356;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=2507354; DOI=10.1016/0014-5793(89)81095-6;
RA Onai T., Fitzgerald M.G., Arakawa S., Gocayne J.D., Urquhart D.A.,
RA Hall L.M., Fraser C.M., McCombie W.R., Venter J.C.;
RT "Cloning, sequence analysis and chromosome localization of a Drosophila
RT muscarinic acetylcholine receptor.";
RL FEBS Lett. 255:219-225(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX PubMed=23604020; DOI=10.1007/s00018-013-1334-0;
RA Collin C., Hauser F., de Valdivia E.G., Li S., Reisenberger J.,
RA Carlsen E.M., Khan Z., Hansen N.O., Puhm F., Sondergaard L., Niemiec J.,
RA Heninger M., Ren G.R., Grimmelikhuijzen C.J.;
RT "Two types of muscarinic acetylcholine receptors in Drosophila and other
RT arthropods.";
RL Cell. Mol. Life Sci. 70:3231-3242(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RA Carlson J., Stapleton M., Booth B., Chavez C., Frise E., George R.,
RA Pacleb J., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-805 (ISOFORM B), AND FUNCTION.
RC STRAIN=Oregon-R;
RX PubMed=2510174; DOI=10.1073/pnas.86.22.9039;
RA Shapiro R.A., Wakimoto B.T., Subers E.M., Nathanson N.M.;
RT "Characterization and functional expression in mammalian cells of genomic
RT and cDNA clones encoding a Drosophila muscarinic acetylcholine receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9039-9043(1989).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7550280; DOI=10.1111/j.1365-2826.1995.tb00768.x;
RA Harrison J.B., Chen H.H., Blake A.D., Huskisson N.S., Barker P.,
RA Sattelle D.B.;
RT "Localization in the nervous system of Drosophila melanogaster of a C-
RT terminus anti-peptide antibody to a cloned Drosophila muscarinic
RT acetylcholine receptor.";
RL J. Neuroendocrinol. 7:347-352(1995).
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. Primary transducing effect is Pi
CC turnover. May have a role in the processing of olfactory and
CC mechanosensory signals; regulation of neurosecretion.
CC {ECO:0000269|PubMed:2510174, ECO:0000269|PubMed:7550280}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P16395-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P16395-2; Sequence=VSP_012002;
CC -!- TISSUE SPECIFICITY: Intense staining in the glomeruli of the antennal
CC lobes, the region of the nervous system containing terminals of
CC antennal olfactory sensory neurons and mechanosensory neurons. Also a
CC discrete group of neurosecretory cells in the pars intercerebralis of
CC the brain. {ECO:0000269|PubMed:7550280}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Muscarinic acetylcholine receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85449.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ABF85716.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. E.coli genomic contaminant.; Evidence={ECO:0000305};
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DR EMBL; M23412; AAA28676.1; -; mRNA.
DR EMBL; JQ922420; AFJ23964.1; -; mRNA.
DR EMBL; JQ922421; AFJ23965.1; -; mRNA.
DR EMBL; AE013599; AAF47197.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68310.1; -; Genomic_DNA.
DR EMBL; BT025816; ABF85716.1; ALT_SEQ; mRNA.
DR EMBL; BT132689; AEQ62993.1; -; mRNA.
DR EMBL; M27495; AAA85449.1; ALT_FRAME; mRNA.
DR PIR; S05661; S05661.
DR RefSeq; NP_523844.2; NM_079120.3. [P16395-1]
DR RefSeq; NP_726440.1; NM_166668.2. [P16395-2]
DR AlphaFoldDB; P16395; -.
DR SMR; P16395; -.
DR STRING; 7227.FBpp0072275; -.
DR BindingDB; P16395; -.
DR ChEMBL; CHEMBL2366467; -.
DR DrugCentral; P16395; -.
DR GlyGen; P16395; 3 sites.
DR PaxDb; P16395; -.
DR PRIDE; P16395; -.
DR EnsemblMetazoa; FBtr0072367; FBpp0072274; FBgn0000037. [P16395-2]
DR EnsemblMetazoa; FBtr0072368; FBpp0072275; FBgn0000037. [P16395-1]
DR GeneID; 37892; -.
DR KEGG; dme:Dmel_CG4356; -.
DR CTD; 37892; -.
DR FlyBase; FBgn0000037; mAChR-A.
DR VEuPathDB; VectorBase:FBgn0000037; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000166540; -.
DR InParanoid; P16395; -.
DR OMA; TWACDLW; -.
DR PhylomeDB; P16395; -.
DR Reactome; R-DME-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-DME-390650; Histamine receptors.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 37892; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37892; -.
DR PRO; PR:P16395; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000037; Expressed in brain and 7 other tissues.
DR Genevisible; P16395; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IDA:FlyBase.
DR GO; GO:0008227; F:G protein-coupled amine receptor activity; ISS:FlyBase.
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: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; IDA:FlyBase.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:FlyBase.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Receptor; Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..805
FT /note="Muscarinic acetylcholine receptor DM1"
FT /id="PRO_0000069051"
FT TOPO_DOM 1..100
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..121
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 122..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..162
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 163..177
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 178..198
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 199..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 221..241
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 242..266
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 267..287
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 288..718
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 719..739
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 740..752
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 753..773
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 774..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 427..443
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:23604020,
FT ECO:0000303|PubMed:2507354"
FT /id="VSP_012002"
FT CONFLICT 23
FT /note="K -> R (in Ref. 1; AAA28676, 2; AFJ23964/AFJ23965
FT and 5; AEQ62993)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="I -> M (in Ref. 2; AFJ23965)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="A -> T (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="S -> N (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="R -> G (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="Missing (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="Q -> H (in Ref. 2; AFJ23965)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="G -> P (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="P -> A (in Ref. 1; AAA28676, 2; AFJ23964/AFJ23965
FT and 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="G -> A (in Ref. 1; AAA28676)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="A -> T (in Ref. 2; AFJ23964/AFJ23965 and 6;
FT AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 687..688
FT /note="VG -> C (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 696..697
FT /note="AR -> P (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 737..739
FT /note="VLI -> CLS (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="C -> S (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
FT CONFLICT 797..805
FT /note="EGMVRGVYN -> DFMYAASTIR (in Ref. 6; AAA85449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 86623 MW; 97A9229CAA5BBED8 CRC64;
MEPVMSLALA AHGPPSILEP LFKTVTTSTT TTTTTTTSTT TTTASPAGYS PGYPGTTLLT
ALFENLTSTA ASGLYDPYSG MYGNQTNGTI GFETKGPRYS LASMVVMGFV AAILSTVTVA
GNVMVMISFK IDKQLQTISN YFLFSLAIAD FAIGAISMPL FAVTTILGYW PLGPIVCDTW
LALDYLASNA SVLNLLIISF DRYFSVTRPL TYRAKRTTNR AAVMIGAAWG ISLLLWPPWI
YSWPYIEGKR TVPKDECYIQ FIETNQYITF GTALAAFYFP VTIMCFLYWR IWRETKKRQK
DLPNLQAGKK DSSKRSNSSD ENTVVNHASG GLLAFAQVGG NDHDTWRRPR SESSPDAESV
YMTNMVIDSG YHGMHSRKSS IKSTNTIKKS YTCFGSIKEW CIAWWHSGRE DSDDFAYEQE
EPSDLGYATP VTIETPLQSS VSRCTSMNVM RDNYSMGGSV SGVRPPSILL SDVSPTPLPR
PPLASISQLQ EMSAVTASTT ANVNTSGNGN GAINNNNNAS HNGNGAVNGN GAGNGSGIGL
GTTGNATHRD SRTLPVINRI NSRSVSQDSV YTILIRLPSD GASSNAANGG GGGPGAGAAA
SASLSMQGDC APSIKMIHED GPTTTAAAAP LASAAATRRP LPSRDSEFSL PLGRRMSHAQ
HDARLLNAKV IPKQLGKAGG GAAGGGVGGA HALMNARNAA KKKKKSQEKR QESKAAKTLS
AILLSFIITW TPYNILVLIK PLTTCSDCIP TELWDFFYAL CYINSTINPM CYALCNATFR
RTYVRILTCK WHTRNREGMV RGVYN
