ACM1_RAT
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 03-AUG-2022, entry version 174.
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 GlyGen; P08482; 2 sites.
DR iPTMnet; P08482; -.
DR PhosphoSitePlus; P08482; -.
DR PaxDb; P08482; -.
DR PRIDE; P08482; -.
DR Ensembl; ENSRNOT00000024785; ENSRNOP00000024785; ENSRNOG00000018385.
DR GeneID; 25229; -.
DR KEGG; rno:25229; -.
DR UCSC; RGD:2342; rat.
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; RCCRTPR; -.
DR OrthoDB; 1245472at2759; -.
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 tissues.
DR Genevisible; P08482; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
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:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0099529; F:neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
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 ion transport; ISO:RGD.
DR GO; GO:0040012; P:regulation of locomotion; ISO:RGD.
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; 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
