ACM3_HUMAN
ID ACM3_HUMAN Reviewed; 590 AA.
AC P20309; Q0VAJ8; Q4QRI3; Q5VXY2; Q9HB60;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Muscarinic acetylcholine receptor M3;
GN Name=CHRM3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3443095; DOI=10.1002/j.1460-2075.1987.tb02733.x;
RA Peralta E.G., Ashkenazi A., Winslow J.W., Smith D.H., Ramachandran J.,
RA Capon D.J.;
RT "Distinct primary structures, ligand-binding properties and tissue-specific
RT expression of four human muscarinic acetylcholine receptors.";
RL EMBO J. 6:3923-3929(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3272174; DOI=10.1016/0896-6273(88)90190-0;
RA Bonner T.I., Young A.C., Brann M.R., Buckley N.J.;
RT "Cloning and expression of the human and rat m5 muscarinic acetylcholine
RT receptor genes.";
RL Neuron 1:403-410(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-384.
RC TISSUE=Teratocarcinoma;
RX PubMed=11238933; DOI=10.1128/mcb.21.6.1973-1985.2001;
RA Speek M.;
RT "Antisense promoter of human L1 retrotransposon drives transcription of
RT adjacent cellular genes.";
RL Mol. Cell. Biol. 21:1973-1985(2001).
RN [8]
RP FUNCTION.
RX PubMed=7565628;
RA Yang J., Williams J.A., Yule D.I., Logsdon C.D.;
RT "Mutation of carboxyl-terminal threonine residues in human M3 muscarinic
RT acetylcholine receptor modulates the extent of sequestration and
RT desensitization.";
RL Mol. Pharmacol. 48:477-485(1995).
RN [9]
RP INVOLVEMENT IN PBS.
RX PubMed=22077972; DOI=10.1016/j.ajhg.2011.10.007;
RA Weber S., Thiele H., Mir S., Toliat M.R., Sozeri B., Reutter H.,
RA Draaken M., Ludwig M., Altmuller J., Frommolt P., Stuart H.M., Ranjzad P.,
RA Hanley N.A., Jennings R., Newman W.G., Wilcox D.T., Thiel U.,
RA Schlingmann K.P., Beetz R., Hoyer P.F., Konrad M., Schaefer F.,
RA Nurnberg P., Woolf A.S.;
RT "Muscarinic acetylcholine receptor M3 mutation causes urinary bladder
RT disease and a prune-belly-like syndrome.";
RL Am. J. Hum. Genet. 89:668-674(2011).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMEM147.
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).
RN [11]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23521066; DOI=10.1042/bj20121902;
RA Patowary S., Alvarez-Curto E., Xu T.R., Holz J.D., Oliver J.A.,
RA Milligan G., Raicu V.;
RT "The muscarinic M3 acetylcholine receptor exists as two differently sized
RT complexes at the plasma membrane.";
RL Biochem. J. 452:303-312(2013).
RN [12]
RP STRUCTURE BY NMR OF 271-289, MUTAGENESIS OF GLU-276; PHE-280 AND VAL-281,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15870063; DOI=10.1074/jbc.m501264200;
RA Iverson H.A., Fox D. III, Nadler L.S., Klevit R.E., Nathanson N.M.;
RT "Identification and structural determination of the M(3) muscarinic
RT acetylcholine receptor basolateral sorting signal.";
RL J. Biol. Chem. 280:24568-24575(2005).
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. {ECO:0000269|PubMed:7565628}.
CC -!- SUBUNIT: Homodimer; the dimers can form tetramers (PubMed:23521066).
CC Interacts with NALCN (By similarity). Interacts with TMEM147
CC (PubMed:21056967). {ECO:0000250|UniProtKB:Q9ERZ3,
CC ECO:0000269|PubMed:21056967, ECO:0000269|PubMed:23521066}.
CC -!- INTERACTION:
CC P20309; P08912: CHRM5; NbExp=7; IntAct=EBI-2687785, EBI-6655256;
CC P20309; Q8IZF0: NALCN; NbExp=3; IntAct=EBI-2687785, EBI-7085333;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21056967};
CC Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane;
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000269|PubMed:15870063}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21056967}; 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:0000269|PubMed:21056967}.
CC -!- DISEASE: Prune belly syndrome (PBS) [MIM:100100]: A syndrome
CC characterized by thin abdominal musculature with overlying lax skin,
CC cryptorchism, megacystis with disorganized detrusor muscle, and urinary
CC tract abnormalities. {ECO:0000269|PubMed:22077972}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
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; X15266; CAA33337.1; -; Genomic_DNA.
DR EMBL; U29589; AAA70337.1; -; Genomic_DNA.
DR EMBL; AB041395; BAA94480.1; -; Genomic_DNA.
DR EMBL; AF498917; AAM18940.1; -; mRNA.
DR EMBL; AL356361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096844; AAH96844.1; -; mRNA.
DR EMBL; BC121026; AAI21027.1; -; mRNA.
DR EMBL; AF279779; AAG30036.1; -; mRNA.
DR CCDS; CCDS1616.1; -.
DR PIR; S10128; S10128.
DR RefSeq; NP_000731.1; NM_000740.3.
DR RefSeq; NP_001334645.1; NM_001347716.1.
DR RefSeq; XP_005273089.1; XM_005273032.3.
DR RefSeq; XP_011542343.1; XM_011544041.2.
DR RefSeq; XP_011542345.1; XM_011544043.2.
DR RefSeq; XP_011542346.1; XM_011544044.2.
DR RefSeq; XP_011542348.1; XM_011544046.2.
DR RefSeq; XP_011542349.1; XM_011544047.2.
DR RefSeq; XP_016855641.1; XM_017000152.1.
DR RefSeq; XP_016855642.1; XM_017000153.1.
DR RefSeq; XP_016855643.1; XM_017000154.1.
DR RefSeq; XP_016855644.1; XM_017000155.1.
DR RefSeq; XP_016855645.1; XM_017000156.1.
DR RefSeq; XP_016855646.1; XM_017000157.1.
DR RefSeq; XP_016855647.1; XM_017000158.1.
DR RefSeq; XP_016855648.1; XM_017000159.1.
DR RefSeq; XP_016855649.1; XM_017000160.1.
DR RefSeq; XP_016855650.1; XM_017000161.1.
DR RefSeq; XP_016855651.1; XM_017000162.1.
DR RefSeq; XP_016855652.1; XM_017000163.1.
DR PDB; 2CSA; NMR; -; A=271-289.
DR PDBsum; 2CSA; -.
DR AlphaFoldDB; P20309; -.
DR SMR; P20309; -.
DR BioGRID; 107553; 80.
DR DIP; DIP-44291N; -.
DR IntAct; P20309; 65.
DR MINT; P20309; -.
DR STRING; 9606.ENSP00000255380; -.
DR BindingDB; P20309; -.
DR ChEMBL; CHEMBL245; -.
DR DrugBank; DB03128; Acetylcholine.
DR DrugBank; DB08897; Aclidinium.
DR DrugBank; DB05752; ALKS 27.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB00517; Anisotropine methylbromide.
DR DrugBank; DB04365; Arecoline.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB00572; Atropine.
DR DrugBank; DB00767; Benzquinamide.
DR DrugBank; DB01019; Bethanechol.
DR DrugBank; DB00835; Brompheniramine.
DR DrugBank; DB09300; Butylscopolamine.
DR DrugBank; DB00411; Carbamoylcholine.
DR DrugBank; DB00185; Cevimeline.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB00568; Cinnarizine.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB00434; Cyproheptadine.
DR DrugBank; DB00496; Darifenacin.
DR DrugBank; DB01151; Desipramine.
DR DrugBank; DB00804; Dicyclomine.
DR DrugBank; DB13720; Diphemanil.
DR DrugBank; DB01231; Diphenidol.
DR DrugBank; DB00280; Disopyramide.
DR DrugBank; DB09167; Dosulepin.
DR DrugBank; DB01142; Doxepin.
DR DrugBank; DB00366; Doxylamine.
DR DrugBank; DB09194; Etoperidone.
DR DrugBank; DB06702; Fesoterodine.
DR DrugBank; DB00986; Glycopyrronium.
DR DrugBank; DB00502; Haloperidol.
DR DrugBank; DB06787; Hexocyclium.
DR DrugBank; DB11181; Homatropine.
DR DrugBank; DB00725; Homatropine methylbromide.
DR DrugBank; DB00424; Hyoscyamine.
DR DrugBank; DB09262; Imidafenacin.
DR DrugBank; DB00458; Imipramine.
DR DrugBank; DB00332; Ipratropium.
DR DrugBank; DB01625; Isopropamide.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB00934; Maprotiline.
DR DrugBank; DB04843; Mepenzolate.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB06709; Methacholine.
DR DrugBank; DB00940; Methantheline.
DR DrugBank; DB01403; Methotrimeprazine.
DR DrugBank; DB00462; Methscopolamine bromide.
DR DrugBank; DB00340; Metixene.
DR DrugBank; DB01226; Mivacurium.
DR DrugBank; DB00622; Nicardipine.
DR DrugBank; DB00540; Nortriptyline.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB01062; Oxybutynin.
DR DrugBank; DB00383; Oxyphencyclimine.
DR DrugBank; DB01337; Pancuronium.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB01085; Pilocarpine.
DR DrugBank; DB01338; Pipecuronium.
DR DrugBank; DB06153; Pizotifen.
DR DrugBank; DB00387; Procyclidine.
DR DrugBank; DB01069; Promethazine.
DR DrugBank; DB00777; Propiomazine.
DR DrugBank; DB12278; Propiverine.
DR DrugBank; DB01224; Quetiapine.
DR DrugBank; DB11855; Revefenacin.
DR DrugBank; DB13581; Rociverine.
DR DrugBank; DB00747; Scopolamine.
DR DrugBank; DB01591; Solifenacin.
DR DrugBank; DB00202; Succinylcholine.
DR DrugBank; DB00342; Terfenadine.
DR DrugBank; DB00599; Thiopental.
DR DrugBank; DB11235; Thonzylamine.
DR DrugBank; DB01409; Tiotropium.
DR DrugBank; DB01036; Tolterodine.
DR DrugBank; DB00193; Tramadol.
DR DrugBank; DB00505; Tridihexethyl.
DR DrugBank; DB00376; Trihexyphenidyl.
DR DrugBank; DB09089; Trimebutine.
DR DrugBank; DB00726; Trimipramine.
DR DrugBank; DB00809; Tropicamide.
DR DrugBank; DB00209; Trospium.
DR DrugBank; DB09076; Umeclidinium.
DR DrugBank; DB00246; Ziprasidone.
DR DrugCentral; P20309; -.
DR GuidetoPHARMACOLOGY; 15; -.
DR GlyGen; P20309; 5 sites.
DR iPTMnet; P20309; -.
DR PhosphoSitePlus; P20309; -.
DR BioMuta; CHRM3; -.
DR DMDM; 113125; -.
DR jPOST; P20309; -.
DR MassIVE; P20309; -.
DR MaxQB; P20309; -.
DR PaxDb; P20309; -.
DR PeptideAtlas; P20309; -.
DR PRIDE; P20309; -.
DR ProteomicsDB; 53745; -.
DR Antibodypedia; 4169; 376 antibodies from 37 providers.
DR DNASU; 1131; -.
DR Ensembl; ENST00000255380.8; ENSP00000255380.4; ENSG00000133019.12.
DR Ensembl; ENST00000615928.5; ENSP00000482377.1; ENSG00000133019.12.
DR Ensembl; ENST00000675184.1; ENSP00000502349.1; ENSG00000133019.12.
DR Ensembl; ENST00000676153.1; ENSP00000502667.1; ENSG00000133019.12.
DR Ensembl; ENST00000676433.1; ENSP00000502013.1; ENSG00000133019.12.
DR GeneID; 1131; -.
DR KEGG; hsa:1131; -.
DR MANE-Select; ENST00000676153.1; ENSP00000502667.1; NM_001375978.1; NP_001362907.1.
DR UCSC; uc001hyp.4; human.
DR CTD; 1131; -.
DR DisGeNET; 1131; -.
DR GeneCards; CHRM3; -.
DR HGNC; HGNC:1952; CHRM3.
DR HPA; ENSG00000133019; Tissue enhanced (brain, salivary gland).
DR MalaCards; CHRM3; -.
DR MIM; 100100; phenotype.
DR MIM; 118494; gene.
DR neXtProt; NX_P20309; -.
DR OpenTargets; ENSG00000133019; -.
DR Orphanet; 2970; Prune belly syndrome.
DR PharmGKB; PA112; -.
DR VEuPathDB; HostDB:ENSG00000133019; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000160084; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P20309; -.
DR OMA; ISASWIH; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P20309; -.
DR TreeFam; TF320495; -.
DR PathwayCommons; P20309; -.
DR Reactome; R-HSA-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P20309; -.
DR SIGNOR; P20309; -.
DR BioGRID-ORCS; 1131; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; CHRM3; human.
DR EvolutionaryTrace; P20309; -.
DR GeneWiki; Muscarinic_acetylcholine_receptor_M3; -.
DR GenomeRNAi; 1131; -.
DR Pharos; P20309; Tclin.
DR PRO; PR:P20309; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P20309; protein.
DR Bgee; ENSG00000133019; Expressed in endothelial cell and 154 other tissues.
DR ExpressionAtlas; P20309; baseline and differential.
DR Genevisible; P20309; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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: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:0004435; F:phosphatidylinositol phospholipase C activity; TAS:ProtInc.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:ARUK-UCL.
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; IDA:ARUK-UCL.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0032412; P:regulation of ion transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; IBA:GO_Central.
DR GO; GO:0046541; P:saliva secretion; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
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 3D-structure; 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..590
FT /note="Muscarinic acetylcholine receptor M3"
FT /id="PRO_0000069029"
FT TOPO_DOM 1..67
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..91
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 92..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..130
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 131..142
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 165..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..206
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 207..229
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 230..252
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 253..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 492..514
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 515..526
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 527..546
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 547..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 323..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 275..281
FT /note="Basolateral sorting signal"
FT COMPBIAS 323..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ3"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 DISULFID 141..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 517..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 65
FT /note="V -> I (in dbSNP:rs2067481)"
FT /id="VAR_033461"
FT VARIANT 431
FT /note="L -> P (in dbSNP:rs16839102)"
FT /id="VAR_049368"
FT MUTAGEN 276
FT /note="E->A: Loss of basolateral sorting."
FT /evidence="ECO:0000269|PubMed:15870063"
FT MUTAGEN 276
FT /note="E->D: Loss of basolateral sorting. No effect on
FT basolateral sorting; when associated with L-280 and L-281."
FT /evidence="ECO:0000269|PubMed:15870063"
FT MUTAGEN 280
FT /note="F->A: Loss of basolateral sorting."
FT /evidence="ECO:0000269|PubMed:15870063"
FT MUTAGEN 280
FT /note="F->L: No effect on basolateral sorting."
FT /evidence="ECO:0000269|PubMed:15870063"
FT MUTAGEN 281
FT /note="V->A: Loss of basolateral sorting."
FT /evidence="ECO:0000269|PubMed:15870063"
FT MUTAGEN 281
FT /note="V->L: No effect on basolateral sorting."
FT /evidence="ECO:0000269|PubMed:15870063"
FT CONFLICT 382..384
FT /note="KLP -> RLS (in Ref. 7; AAG30036)"
FT /evidence="ECO:0000305"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:2CSA"
SQ SEQUENCE 590 AA; 66128 MW; 5CB473C57B9526E9 CRC64;
MTLHNNSTTS PLFPNISSSW IHSPSDAGLP PGTVTHFGSY NVSRAAGNFS SPDGTTDDPL
GGHTVWQVVF IAFLTGILAL VTIIGNILVI VSFKVNKQLK TVNNYFLLSL ACADLIIGVI
SMNLFTTYII MNRWALGNLA CDLWLAIDYV ASNASVMNLL VISFDRYFSI TRPLTYRAKR
TTKRAGVMIG LAWVISFVLW APAILFWQYF VGKRTVPPGE CFIQFLSEPT ITFGTAIAAF
YMPVTIMTIL YWRIYKETEK RTKELAGLQA SGTEAETENF VHPTGSSRSC SSYELQQQSM
KRSNRRKYGR CHFWFTTKSW KPSSEQMDQD HSSSDSWNNN DAAASLENSA SSDEEDIGSE
TRAIYSIVLK LPGHSTILNS TKLPSSDNLQ VPEEELGMVD LERKADKLQA QKSVDDGGSF
PKSFSKLPIQ LESAVDTAKT SDVNSSVGKS TATLPLSFKE ATLAKRFALK TRSQITKRKR
MSLVKEKKAA QTLSAILLAF IITWTPYNIM VLVNTFCDSC IPKTFWNLGY WLCYINSTVN
PVCYALCNKT FRTTFKMLLL CQCDKKKRRK QQYQQRQSVI FHKRAPEQAL
