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   02-SEP-2026, entry version 202.
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   CORUM; P12657; -.
DR   FunCoup; P12657; 1046.
DR   STRING; 10090.ENSMUSP00000126103; -.
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   GlyCosmos; P12657; 2 sites, No reported glycans.
DR   GlyGen; P12657; 2 sites.
DR   iPTMnet; P12657; -.
DR   PhosphoSitePlus; P12657; -.
DR   SwissPalm; P12657; -.
DR   PaxDb; 10090-ENSMUSP00000126103; -.
DR   ProteomicsDB; 285586; -.
DR   Antibodypedia; 2948; 326 antibodies from 38 providers.
DR   DNASU; 12669; -.
DR   Ensembl; ENSMUST00000035444.10; ENSMUSP00000042632.4; ENSMUSG00000032773.10.
DR   Ensembl; ENSMUST00000163785.2; ENSMUSP00000126103.2; ENSMUSG00000032773.10.
DR   GeneID; 12669; -.
DR   KEGG; mmu:12669; -.
DR   UCSC; uc008gmf.2; mouse.
DR   AGR; MGI:88396; -.
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; CCCWGPR; -.
DR   OrthoDB; 10071887at2759; -.
DR   PhylomeDB; P12657; -.
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 76 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
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 cell types or tissues.
DR   ExpressionAtlas; P12657; baseline and differential.
DR   GO; GO:0032279; C:asymmetric synapse; ISO:GO_Central.
DR   GO; GO:0043679; C:axon terminus; ISO:GO_Central.
DR   GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR   GO; GO:0030425; C:dendrite; ISO:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:GO_Central.
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: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:0050890; P:cognition; IEA:InterPro.
DR   GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:GO_Central.
DR   GO; GO:0043270; P:positive regulation of monoatomic ion transport; ISO:MGI.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0040012; P:regulation of locomotion; IMP:MGI.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0046541; P:saliva secretion; IEA:InterPro.
DR   CDD; cd17790; 7tmA_mAChR_M1; 1.
DR   FunFam; 1.20.1070.10:FF:000103; Muscarinic acetylcholine receptor; 1.
DR   FunFam; 1.20.1070.10:FF:000162; Muscarinic acetylcholine receptor; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1.
DR   PANTHER; PTHR24247:SF182; MUSCARINIC ACETYLCHOLINE RECEPTOR M1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   PRINTS; PR00538; MUSCRINICM1R.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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        238..257
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..343
FT                   /note="Basic 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
//