ACM1_MOUSE
ID ACM1_MOUSE Reviewed; 460 AA.
AC P12657; Q52KQ0; Q8BJN3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Muscarinic acetylcholine receptor M1;
GN Name=Chrm1; Synonyms=Chrm-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2848036; DOI=10.1016/s0021-9258(19)81372-8;
RA Shapiro R.A., Scherer N.M., Habecker B.A., Subers E.M., Nathanson N.M.;
RT "Isolation, sequence, and functional expression of the mouse M1 muscarinic
RT acetylcholine receptor gene.";
RL J. Biol. Chem. 263:18397-18403(1988).
RN [2]
RP ERRATUM OF PUBMED:2848036.
RA Shapiro R.A., Scherer N.M., Habecker B.A., Subers E.M., Nathanson N.M.;
RL J. Biol. Chem. 264:6596-6596(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- SUBUNIT: Interacts with GPRASP2 (By similarity). Interacts with TMEM147
CC (By similarity). {ECO:0000250|UniProtKB:P11229}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Muscarinic acetylcholine receptor subfamily. CHRM1 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; J04192; AAA37158.1; -; Genomic_DNA.
DR EMBL; AK081248; BAC38175.1; -; mRNA.
DR EMBL; AK138282; BAE23612.1; -; mRNA.
DR EMBL; AC025794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466612; EDL33348.1; -; Genomic_DNA.
DR EMBL; CH466612; EDL33349.1; -; Genomic_DNA.
DR EMBL; BC094242; AAH94242.1; -; mRNA.
DR CCDS; CCDS29539.1; -.
DR PIR; A31897; A31897.
DR RefSeq; NP_001106167.1; NM_001112697.1.
DR RefSeq; NP_031724.2; NM_007698.3.
DR AlphaFoldDB; P12657; -.
DR SMR; P12657; -.
DR STRING; 10090.ENSMUSP00000042632; -.
DR BindingDB; P12657; -.
DR ChEMBL; CHEMBL3733; -.
DR DrugCentral; P12657; -.
DR GuidetoPHARMACOLOGY; 13; -.
DR TCDB; 9.A.14.3.2; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P12657; 2 sites.
DR iPTMnet; P12657; -.
DR PhosphoSitePlus; P12657; -.
DR PaxDb; P12657; -.
DR PRIDE; P12657; -.
DR ProteomicsDB; 285586; -.
DR Antibodypedia; 2948; 326 antibodies from 37 providers.
DR DNASU; 12669; -.
DR Ensembl; ENSMUST00000035444; ENSMUSP00000042632; ENSMUSG00000032773.
DR Ensembl; ENSMUST00000163785; ENSMUSP00000126103; ENSMUSG00000032773.
DR GeneID; 12669; -.
DR KEGG; mmu:12669; -.
DR UCSC; uc008gmf.2; mouse.
DR CTD; 1128; -.
DR MGI; MGI:88396; Chrm1.
DR VEuPathDB; HostDB:ENSMUSG00000032773; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000162301; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P12657; -.
DR OMA; RCCRTPR; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P12657; -.
DR TreeFam; TF320495; -.
DR Reactome; R-MMU-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 12669; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Chrm1; mouse.
DR PRO; PR:P12657; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P12657; protein.
DR Bgee; ENSMUSG00000032773; Expressed in dentate gyrus of hippocampal formation granule cell and 88 other tissues.
DR ExpressionAtlas; P12657; baseline and differential.
DR Genevisible; P12657; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; ISO:MGI.
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:0099529; F:neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
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:0050890; P:cognition; IEA:InterPro.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISO:MGI.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:MGI.
DR GO; GO:0043270; P:positive regulation of ion transport; ISO:MGI.
DR GO; GO:0040012; P:regulation of locomotion; IMP:MGI.
DR GO; GO:0046541; P:saliva secretion; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002228; Musac_Ach_M1_rcpt.
DR InterPro; IPR000995; Musac_Ach_rcpt.
DR PANTHER; PTHR24248:SF155; PTHR24248:SF155; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PRINTS; PR00538; MUSCRINICM1R.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..460
FT /note="Muscarinic acetylcholine receptor M1"
FT /id="PRO_0000069017"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 23..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 49..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 63..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 85..95
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 96..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 122..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 143..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 165..185
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 186..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 210..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 367..390
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 391..397
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 398..420
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 421..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT REGION 225..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08482"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 98..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 30
FT /note="I -> S (in Ref. 1; AAA37158)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="F -> I (in Ref. 1; AAA37158)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="L -> S (in Ref. 1; AAA37158)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="T -> H (in Ref. 1; AAA37158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 51379 MW; 2F6A93DE8FF4F325 CRC64;
MNTSVPPAVS PNITVLAPGK GPWQVAFIGI TTGLLSLATV TGNLLVLISF KVNTELKTVN
NYFLLSLACA DLIIGTFSMN LYTTYLLMGH WALGTLACDL WLALDYVASN ASVMNLLLIS
FDRYFSVTRP LSYRAKRTPR RAALMIGLAW LVSFVLWAPA ILFWQYLVGE RTVLAGQCYI
QFLSQPIITF GTAMAAFYLP VTVMCTLYWR IYRETENRAR ELAALQGSET PGKGGGSSSS
SERSQPGAEG SPESPPGRCC RCCRAPRLLQ AYSWKEEEEE DEGSMESLTS SEGEEPGSEV
VIKMPMVDPE AQAPTKQPPK SSPNTVKRPT KKGRDRGGKG QKPRGKEQLA KRKTFSLVKE
KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW ELGYWLCYVN STVNPMCYAL
CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC
