ID   ACM1_RAT                Reviewed;         460 AA.
AC   P08482;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=Muscarinic acetylcholine receptor M1;
GN   Name=Chrm1; Synonyms=Chrm-1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3037705; DOI=10.1126/science.3037705;
RA   Bonner T.I., Buckley N.J., Young A.C., Brann M.R.;
RT   "Identification of a family of muscarinic acetylcholine receptor genes.";
RL   Science 237:527-532(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1759615; DOI=10.1007/978-1-4684-5907-4_26;
RA   Lai J., Smith T.L., Mei L., Ikeda M., Fujiwara Y., Gomez J., Halonen M.,
RA   Roeske W.R., Yamamura H.I.;
RT   "The molecular properties of the M1 muscarinic receptor and its regulation
RT   of cytosolic calcium in a eukaryotic gene expression system.";
RL   Adv. Exp. Med. Biol. 287:313-330(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 63-124, AND BINDING TO ANTAGONIST PROPYLBENZILYLCHOLINE
RP   MUSTARD.
RX   PubMed=2380182; DOI=10.1016/s0021-9258(18)77406-1;
RA   Kurtenbach E., Curtis C.A.M., Pedder E.K., Aitken A., Harris A.C.M.,
RA   Hulme E.C.;
RT   "Muscarinic acetylcholine receptors. Peptide sequencing identifies residues
RT   involved in antagonist binding and disulfide bond formation.";
RL   J. Biol. Chem. 265:13702-13708(1990).
RN   [4]
RP   MUTAGENESIS OF CYSTEINE RESIDUES.
RX   PubMed=1317867; DOI=10.1016/s0021-9258(19)49929-8;
RA   Savarese T.M., Wang C.-D., Fraser C.M.;
RT   "Site-directed mutagenesis of the rat m1 muscarinic acetylcholine receptor.
RT   Role of conserved cysteines in receptor function.";
RL   J. Biol. Chem. 267:11439-11448(1992).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; M16406; AAA40660.1; -; Genomic_DNA.
DR   EMBL; S73971; AAB20705.1; -; Genomic_DNA.
DR   PIR; A94518; A29514.
DR   RefSeq; NP_542951.1; NM_080773.1.
DR   RefSeq; XP_006231036.1; XM_006230974.3.
DR   RefSeq; XP_008758437.1; XM_008760215.2.
DR   AlphaFoldDB; P08482; -.
DR   SMR; P08482; -.
DR   BioGRID; 247270; 1.
DR   CORUM; P08482; -.
DR   STRING; 10116.ENSRNOP00000024785; -.
DR   BindingDB; P08482; -.
DR   ChEMBL; CHEMBL276; -.
DR   DrugCentral; P08482; -.
DR   GuidetoPHARMACOLOGY; 13; -.
DR   GlyCosmos; P08482; 2 sites, No reported glycans.
DR   GlyGen; P08482; 2 sites.
DR   iPTMnet; P08482; -.
DR   PhosphoSitePlus; P08482; -.
DR   PaxDb; 10116-ENSRNOP00000024785; -.
DR   Ensembl; ENSRNOT00000024785.5; ENSRNOP00000024785.2; ENSRNOG00000018385.5.
DR   Ensembl; ENSRNOT00055040486; ENSRNOP00055032888; ENSRNOG00055023559.
DR   Ensembl; ENSRNOT00060057380; ENSRNOP00060047398; ENSRNOG00060033086.
DR   Ensembl; ENSRNOT00065056701; ENSRNOP00065046680; ENSRNOG00065032960.
DR   GeneID; 25229; -.
DR   KEGG; rno:25229; -.
DR   UCSC; RGD:2342; rat.
DR   AGR; RGD:2342; -.
DR   CTD; 1128; -.
DR   RGD; 2342; Chrm1.
DR   eggNOG; KOG4220; Eukaryota.
DR   GeneTree; ENSGT00940000162301; -.
DR   HOGENOM; CLU_009579_11_2_1; -.
DR   InParanoid; P08482; -.
DR   OMA; ETPPGHC; -.
DR   OrthoDB; 4136179at2759; -.
DR   PhylomeDB; P08482; -.
DR   TreeFam; TF320495; -.
DR   Reactome; R-RNO-390648; Muscarinic acetylcholine receptors.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   PRO; PR:P08482; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018385; Expressed in frontal cortex and 6 other cell types or tissues.
DR   GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR   GO; GO:0043679; C:axon terminus; IDA:RGD.
DR   GO; GO:0098981; C:cholinergic synapse; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IDA:RGD.
DR   GO; GO:0004993; F:G protein-coupled serotonin 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:0050890; P:cognition; IEA:InterPro.
DR   GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IDA:RGD.
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; IDA:RGD.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:RGD.
DR   GO; GO:0043270; P:positive regulation of monoatomic ion transport; ISO:RGD.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0040012; P:regulation of locomotion; ISO:RGD.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
DR   GO; GO:0046541; P:saliva secretion; IEA:InterPro.
DR   CDD; cd17790; 7tmA_mAChR_M1; 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.
DR   Genevisible; P08482; RN.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Synapse;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..460
FT                   /note="Muscarinic acetylcholine receptor M1"
FT                   /id="PRO_0000069019"
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:0000250|UniProtKB:P12657"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         428
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
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:0000305"
SQ   SEQUENCE   460 AA;  51369 MW;  527573ED8FF7C317 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
     VIKMPMVDSE AQAPTKQPPK SSPNTVKRPT KKGRDRGGKG QKPRGKEQLA KRKTFSLVKE
     KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW ELGYWLCYVN STVNPMCYAL
     CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC
//