ACM3_MOUSE
ID ACM3_MOUSE Reviewed; 589 AA.
AC Q9ERZ3; Q64055;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Muscarinic acetylcholine receptor M3;
DE AltName: Full=Mm3 mAChR;
GN Name=Chrm3; Synonyms=Chrm-3;
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].
RA Gomeza J., Wess J.;
RT "Isolation, sequence and functional expression of mouse muscarinic
RT acetylcholine receptor genes.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 314-439.
RC TISSUE=Brain;
RX PubMed=7874308; DOI=10.1111/j.1460-9568.1994.tb00561.x;
RA Andre C., Dos Santos G., Koulakoff A.;
RT "Cultured neurons from mouse brain reproduce the muscarinic receptor
RT profile of their tissue of origin.";
RL Eur. J. Neurosci. 6:1691-1701(1994).
RN [3]
RP INTERACTION WITH NALCN.
RX PubMed=19575010; DOI=10.1038/embor.2009.125;
RA Swayne L.A., Mezghrani A., Varrault A., Chemin J., Bertrand G., Dalle S.,
RA Bourinet E., Lory P., Miller R.J., Nargeot J., Monteil A.;
RT "The NALCN ion channel is activated by M3 muscarinic receptors in a
RT pancreatic beta-cell line.";
RL EMBO Rep. 10:873-880(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, 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).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=21056967; DOI=10.1124/mol.110.067363;
RA Rosemond E., Rossi M., McMillin S.M., Scarselli M., Donaldson J.G.,
RA Wess J.;
RT "Regulation of M(3) muscarinic receptor expression and function by
RT transmembrane protein 147.";
RL Mol. Pharmacol. 79:251-261(2011).
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: Homodimer; the dimers can form tetramers (By similarity).
CC Interacts with NALCN (PubMed:19575010). Interacts with TMEM147 (By
CC similarity). {ECO:0000250|UniProtKB:P20309,
CC ECO:0000269|PubMed:19575010}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20309};
CC Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000255}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:P20309}; Multi-pass membrane
CC protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P20309}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalizes with TMEM147 in the endoplasmic
CC reticulum (ER) membrane. TMEM147 impairs its trafficking to the cell
CC membrane leading to its retention in the ER membrane.
CC {ECO:0000250|UniProtKB:P20309}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebral cortex, submandibular gland,
CC hypothalamus, pancreas, liver, and ileum.
CC {ECO:0000269|PubMed:21056967}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Muscarinic acetylcholine receptor subfamily. CHRM3 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF264050; AAG14344.1; -; Genomic_DNA.
DR EMBL; S74908; AAB33576.2; -; mRNA.
DR CCDS; CCDS26238.1; -.
DR RefSeq; NP_150372.1; NM_033269.4.
DR RefSeq; XP_006516531.1; XM_006516468.3.
DR AlphaFoldDB; Q9ERZ3; -.
DR SMR; Q9ERZ3; -.
DR BioGRID; 198707; 1.
DR STRING; 10090.ENSMUSP00000140131; -.
DR BindingDB; Q9ERZ3; -.
DR ChEMBL; CHEMBL5105; -.
DR DrugCentral; Q9ERZ3; -.
DR GlyGen; Q9ERZ3; 5 sites.
DR iPTMnet; Q9ERZ3; -.
DR PhosphoSitePlus; Q9ERZ3; -.
DR SwissPalm; Q9ERZ3; -.
DR MaxQB; Q9ERZ3; -.
DR PaxDb; Q9ERZ3; -.
DR PRIDE; Q9ERZ3; -.
DR ProteomicsDB; 285644; -.
DR Antibodypedia; 4169; 376 antibodies from 37 providers.
DR DNASU; 12671; -.
DR Ensembl; ENSMUST00000063093; ENSMUSP00000055579; ENSMUSG00000046159.
DR Ensembl; ENSMUST00000187510; ENSMUSP00000140131; ENSMUSG00000046159.
DR GeneID; 12671; -.
DR KEGG; mmu:12671; -.
DR UCSC; uc007plb.1; mouse.
DR CTD; 1131; -.
DR MGI; MGI:88398; Chrm3.
DR VEuPathDB; HostDB:ENSMUSG00000046159; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000160084; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; Q9ERZ3; -.
DR OMA; ISASWIH; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; Q9ERZ3; -.
DR TreeFam; TF320495; -.
DR Reactome; R-MMU-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 12671; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Chrm3; mouse.
DR PRO; PR:Q9ERZ3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9ERZ3; protein.
DR Bgee; ENSMUSG00000046159; Expressed in granulocyte and 88 other tissues.
DR ExpressionAtlas; Q9ERZ3; baseline and differential.
DR Genevisible; Q9ERZ3; 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:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042166; F:acetylcholine binding; ISS:UniProtKB.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; ISS:UniProtKB.
DR GO; GO:0031789; F:G protein-coupled acetylcholine receptor binding; 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:0050997; F:quaternary ammonium group binding; ISO:MGI.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:MGI.
DR GO; GO:0007197; P:adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0003063; P:negative regulation of heart rate by acetylcholine; ISO:MGI.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:MGI.
DR GO; GO:1904695; P:positive regulation of vascular associated smooth muscle contraction; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0032412; P:regulation of ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; IBA:GO_Central.
DR GO; GO:1905144; P:response to acetylcholine; ISO:MGI.
DR GO; GO:0046541; P:saliva secretion; IMP:MGI.
DR GO; GO:0006939; P:smooth muscle contraction; IDA:MGI.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001183; Musac_Ach_M3_rcpt.
DR InterPro; IPR000995; Musac_Ach_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PRINTS; PR00540; MUSCRINICM3R.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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; Endoplasmic reticulum;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Synapse;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..589
FT /note="Muscarinic acetylcholine receptor M3"
FT /id="PRO_0000069030"
FT TOPO_DOM 1..66
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 67..90
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 91..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..129
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 130..141
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..163
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 164..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 184..205
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 206..228
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 229..251
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 252..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 491..513
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 514..525
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 526..545
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 546..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 275..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 274..280
FT /note="Basolateral sorting signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 516..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 589 AA; 66212 MW; AB782149EBEE7804 CRC64;
MTLHSNSTTS PLFPNISSSW VHSPSEAGLP LGTVSQLDSY NISQTSGNFS SNDTSSDPLG
GHTIWQVVFI AFLTGFLALV TIIGNILVIV AFKVNKQLKT VNNYFLLSLA CADLIIGVIS
MNLFTTYIIM NRWALGNLAC DLWLSIDYVA SNASVMNLLV ISFDRYFSIT RPLTYRAKRT
TKRAGVMIGL AWVISFVLWA PAILFWQYFV GKRTVPPGEC FIQFLSEPTI TFGTAIAAFY
MPVTIMTILY WRIYKETEKR TKELAGLQAS GTEAEAENFV HPTGSSRSCS SYELQQQGTK
RSSRRKYGGC HFWFTTKSWK PSAEQMDQDH SSSDSWNNND AAASLENSAS SDEEDIGSET
RAIYSIVLKL PGHSTILNST KLPSSDNLQV PDKDLGTMDV ERNAHKLQAQ KSMDDRDNCQ
KDFSKLPIQL ESAVDTAKTS DTNSSVDKTT AALPLSFKEA TLAKRFALKT RSQITKRKRM
SLIKEKKAAQ TLSAILLAFI ITWTPYNIMV LVNTFCDSCI PKTYWNLGYW LCYINSTVNP
VCYALCNKTF RTTFKMLLLC QCDKRKRRKQ QYQQRQSVIF HKRVPEQAL
