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Database: UniProt
Entry: ACM1_HUMAN
LinkDB: ACM1_HUMAN
Original site: ACM1_HUMAN 
ID   ACM1_HUMAN              Reviewed;         460 AA.
AC   P11229; Q96RH1;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   24-JAN-2024, entry version 223.
DE   RecName: Full=Muscarinic acetylcholine receptor M1;
GN   Name=CHRM1;
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=3697105; DOI=10.1093/nar/15.24.10604;
RA   Allard W.J., Sigal I.S., Dixon R.A.F.;
RT   "Sequence of the gene encoding the human M1 muscarinic acetylcholine
RT   receptor.";
RL   Nucleic Acids Res. 15:10604-10604(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2336407; DOI=10.1093/nar/18.8.2191;
RA   Chapman C.G., Browne M.J.;
RT   "Isolation of the human ml (Hml) muscarinic acetylcholine receptor gene by
RT   PCR amplification.";
RL   Nucleic Acids Res. 18:2191-2191(1990).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Arredondo J., Grando S.A.;
RT   "Cloning Cholinergic Receptors in Human Keratinocytes.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   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   [8]
RP   MUTAGENESIS.
RX   PubMed=1445347; DOI=10.1016/0006-291x(92)91346-r;
RA   Arden J.R., Nagata O., Shockley M.S., Philip M., Lameh J., Sadee W.;
RT   "Mutational analysis of third cytoplasmic loop domains in G-protein
RT   coupling of the HM1 muscarinic receptor.";
RL   Biochem. Biophys. Res. Commun. 188:1111-1115(1992).
RN   [9]
RP   INTERACTION WITH GPRASP2.
RX   PubMed=15086532; DOI=10.1111/j.1471-4159.2004.02411.x;
RA   Simonin F., Karcher P., Boeuf J.J.-M., Matifas A., Kieffer B.L.;
RT   "Identification of a novel family of G protein-coupled receptor associated
RT   sorting proteins.";
RL   J. Neurochem. 89:766-775(2004).
RN   [10]
RP   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] {ECO:0000312|PDB:6WJC}
RP   X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-218 AND 355-460 IN COMPLEX WITH
RP   SNAKE VENOM MUSCARINIC TOXIN 7, TOPOLOGY, AND DISULFIDE BONDS.
RX   PubMed=32646996; DOI=10.1126/science.aax2517;
RA   Maeda S., Xu J., Kadji F.M.N., Clark M.J., Zhao J., Tsutsumi N., Aoki J.,
RA   Sunahara R.K., Inoue A., Garcia K.C., Kobilka B.K.;
RT   "Structure and selectivity engineering of the M1 muscarinic receptor toxin
RT   complex.";
RL   Science 369:161-167(2020).
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 (PubMed:15086532). Interacts with
CC       TMEM147 (PubMed:21056967). {ECO:0000269|PubMed:15086532,
CC       ECO:0000269|PubMed:21056967}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Postsynaptic cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P11229-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P11229-2; Sequence=VSP_056651;
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; Y00508; CAA68560.1; -; Genomic_DNA.
DR   EMBL; X52068; CAA36291.1; -; Genomic_DNA.
DR   EMBL; X15263; CAA33334.1; -; Genomic_DNA.
DR   EMBL; AF385587; AAK68112.1; -; mRNA.
DR   EMBL; AF498915; AAM18938.1; -; mRNA.
DR   EMBL; AP000438; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007740; AAH07740.1; -; mRNA.
DR   EMBL; BC022984; AAH22984.1; -; mRNA.
DR   CCDS; CCDS8040.1; -. [P11229-1]
DR   PIR; S09508; S09508.
DR   RefSeq; NP_000729.2; NM_000738.2. [P11229-1]
DR   RefSeq; XP_011543044.1; XM_011544742.2. [P11229-1]
DR   PDB; 5CXV; X-ray; 2.70 A; A=2-218, A=355-460.
DR   PDB; 6OIJ; EM; 3.30 A; R=2-460.
DR   PDB; 6WJC; X-ray; 2.55 A; A=2-218, A=355-460.
DR   PDB; 6ZFZ; X-ray; 2.17 A; A=27-219, A=355-438.
DR   PDB; 6ZG4; X-ray; 2.33 A; A=27-219, A=355-438.
DR   PDB; 6ZG9; X-ray; 2.50 A; A=27-219, A=355-438.
DR   PDBsum; 5CXV; -.
DR   PDBsum; 6OIJ; -.
DR   PDBsum; 6WJC; -.
DR   PDBsum; 6ZFZ; -.
DR   PDBsum; 6ZG4; -.
DR   PDBsum; 6ZG9; -.
DR   AlphaFoldDB; P11229; -.
DR   EMDB; EMD-20078; -.
DR   SMR; P11229; -.
DR   BioGRID; 107550; 4.
DR   IntAct; P11229; 5.
DR   MINT; P11229; -.
DR   STRING; 9606.ENSP00000306490; -.
DR   BindingDB; P11229; -.
DR   ChEMBL; CHEMBL216; -.
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; DB00245; Benzatropine.
DR   DrugBank; DB00767; Benzquinamide.
DR   DrugBank; DB01019; Bethanechol.
DR   DrugBank; DB00810; Biperiden.
DR   DrugBank; DB00835; Brompheniramine.
DR   DrugBank; DB00354; Buclizine.
DR   DrugBank; DB00411; Carbamoylcholine.
DR   DrugBank; DB00185; Cevimeline.
DR   DrugBank; DB00477; Chlorpromazine.
DR   DrugBank; DB01239; Chlorprothixene.
DR   DrugBank; DB00568; Cinnarizine.
DR   DrugBank; DB00771; Clidinium.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB00907; Cocaine.
DR   DrugBank; DB00979; Cyclopentolate.
DR   DrugBank; DB00942; Cycrimine.
DR   DrugBank; DB00434; Cyproheptadine.
DR   DrugBank; DB00496; Darifenacin.
DR   DrugBank; DB01151; Desipramine.
DR   DrugBank; DB00804; Dicyclomine.
DR   DrugBank; DB01231; Diphenidol.
DR   DrugBank; DB00280; Disopyramide.
DR   DrugBank; DB09167; Dosulepin.
DR   DrugBank; DB01142; Doxepin.
DR   DrugBank; DB00366; Doxylamine.
DR   DrugBank; DB01175; Escitalopram.
DR   DrugBank; DB09194; Etoperidone.
DR   DrugBank; DB06702; Fesoterodine.
DR   DrugBank; DB01148; Flavoxate.
DR   DrugBank; DB00875; Flupentixol.
DR   DrugBank; DB00483; Gallamine triethiodide.
DR   DrugBank; DB00986; Glycopyrronium.
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; 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; DB01233; Metoclopramide.
DR   DrugBank; DB00805; Minaprine.
DR   DrugBank; DB01618; Molindone.
DR   DrugBank; DB05152; NGX267.
DR   DrugBank; DB00622; Nicardipine.
DR   DrugBank; DB05766; Norclozapine.
DR   DrugBank; DB00540; Nortriptyline.
DR   DrugBank; DB00334; Olanzapine.
DR   DrugBank; DB01062; Oxybutynin.
DR   DrugBank; DB00383; Oxyphencyclimine.
DR   DrugBank; DB00219; Oxyphenonium.
DR   DrugBank; DB00715; Paroxetine.
DR   DrugBank; DB01085; Pilocarpine.
DR   DrugBank; DB00670; Pirenzepine.
DR   DrugBank; DB06153; Pizotifen.
DR   DrugBank; DB00387; Procyclidine.
DR   DrugBank; DB00392; Profenamine.
DR   DrugBank; DB00420; Promazine.
DR   DrugBank; DB01069; Promethazine.
DR   DrugBank; DB00782; Propantheline.
DR   DrugBank; DB00777; Propiomazine.
DR   DrugBank; DB12278; Propiverine.
DR   DrugBank; DB11156; Pyrantel.
DR   DrugBank; DB01224; Quetiapine.
DR   DrugBank; DB11855; Revefenacin.
DR   DrugBank; DB13581; Rociverine.
DR   DrugBank; DB00747; Scopolamine.
DR   DrugBank; DB01591; Solifenacin.
DR   DrugBank; DB02010; Staurosporine.
DR   DrugBank; DB00342; Terfenadine.
DR   DrugBank; DB11235; Thonzylamine.
DR   DrugBank; DB01409; Tiotropium.
DR   DrugBank; DB01036; Tolterodine.
DR   DrugBank; DB00193; Tramadol.
DR   DrugBank; DB00505; Tridihexethyl.
DR   DrugBank; DB00508; Triflupromazine.
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; DB09185; Viloxazine.
DR   DrugBank; DB00246; Ziprasidone.
DR   DrugCentral; P11229; -.
DR   GuidetoPHARMACOLOGY; 13; -.
DR   GlyCosmos; P11229; 2 sites, No reported glycans.
DR   GlyGen; P11229; 2 sites.
DR   iPTMnet; P11229; -.
DR   PhosphoSitePlus; P11229; -.
DR   BioMuta; CHRM1; -.
DR   DMDM; 113118; -.
DR   MassIVE; P11229; -.
DR   PaxDb; 9606-ENSP00000306490; -.
DR   PeptideAtlas; P11229; -.
DR   ProteomicsDB; 52724; -. [P11229-1]
DR   ProteomicsDB; 77961; -.
DR   ABCD; P11229; 12 sequenced antibodies.
DR   Antibodypedia; 2948; 365 antibodies from 37 providers.
DR   DNASU; 1128; -.
DR   Ensembl; ENST00000306960.4; ENSP00000306490.3; ENSG00000168539.4. [P11229-1]
DR   Ensembl; ENST00000543973.1; ENSP00000441188.1; ENSG00000168539.4. [P11229-2]
DR   GeneID; 1128; -.
DR   KEGG; hsa:1128; -.
DR   MANE-Select; ENST00000306960.4; ENSP00000306490.3; NM_000738.3; NP_000729.2.
DR   UCSC; uc058cqg.1; human. [P11229-1]
DR   AGR; HGNC:1950; -.
DR   CTD; 1128; -.
DR   DisGeNET; 1128; -.
DR   GeneCards; CHRM1; -.
DR   HGNC; HGNC:1950; CHRM1.
DR   HPA; ENSG00000168539; Group enriched (brain, prostate, salivary gland).
DR   MIM; 118510; gene.
DR   neXtProt; NX_P11229; -.
DR   OpenTargets; ENSG00000168539; -.
DR   PharmGKB; PA26484; -.
DR   VEuPathDB; HostDB:ENSG00000168539; -.
DR   eggNOG; KOG4220; Eukaryota.
DR   GeneTree; ENSGT00940000162301; -.
DR   HOGENOM; CLU_009579_11_2_1; -.
DR   InParanoid; P11229; -.
DR   OMA; ETPPGHC; -.
DR   OrthoDB; 4136179at2759; -.
DR   PhylomeDB; P11229; -.
DR   TreeFam; TF320495; -.
DR   PathwayCommons; P11229; -.
DR   Reactome; R-HSA-390648; Muscarinic acetylcholine receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   SignaLink; P11229; -.
DR   SIGNOR; P11229; -.
DR   BioGRID-ORCS; 1128; 16 hits in 1157 CRISPR screens.
DR   ChiTaRS; CHRM1; human.
DR   GeneWiki; Muscarinic_acetylcholine_receptor_M1; -.
DR   GenomeRNAi; 1128; -.
DR   Pharos; P11229; Tclin.
DR   PRO; PR:P11229; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P11229; Protein.
DR   Bgee; ENSG00000168539; Expressed in prefrontal cortex and 92 other cell types or tissues.
DR   ExpressionAtlas; P11229; baseline and differential.
DR   Genevisible; P11229; HS.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IBA:GO_Central.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; TAS:ProtInc.
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; TAS:ProtInc.
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:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR   GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; IEA:Ensembl.
DR   GO; GO:0043270; P:positive regulation of monoatomic ion transport; IGI:MGI.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0060251; P:regulation of glial cell proliferation; TAS:GO_Central.
DR   GO; GO:0040012; P:regulation of locomotion; IEA:Ensembl.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; IEA:Ensembl.
DR   GO; GO:0046541; P:saliva secretion; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:GO_Central.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; 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_0000069015"
FT   TOPO_DOM        1..22
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TRANSMEM        23..48
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TOPO_DOM        49..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TRANSMEM        63..84
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TOPO_DOM        85..95
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TRANSMEM        96..121
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TOPO_DOM        122..142
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TRANSMEM        143..164
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TOPO_DOM        165..185
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TRANSMEM        186..209
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TOPO_DOM        210..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TRANSMEM        367..390
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TOPO_DOM        391..397
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TRANSMEM        398..420
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   TOPO_DOM        421..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:32646996,
FT                   ECO:0007744|PDB:6WJC"
FT   REGION          225..256
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   SITE            170
FT                   /note="Subtype-specific residue that binds to snake venom
FT                   muscarinic toxin 7"
FT                   /evidence="ECO:0000269|PubMed:32646996"
FT   SITE            172
FT                   /note="Binds to snake venom muscarinic toxin 7"
FT                   /evidence="ECO:0000269|PubMed:32646996"
FT   SITE            174
FT                   /note="Subtype-specific residue that binds to snake venom
FT                   muscarinic toxin 7"
FT                   /evidence="ECO:0000269|PubMed:32646996"
FT   SITE            397
FT                   /note="Subtype-specific residue that binds to snake venom
FT                   muscarinic toxin 7"
FT                   /evidence="ECO:0000269|PubMed:32646996"
FT   SITE            401
FT                   /note="Subtype-specific residue that binds to snake venom
FT                   muscarinic toxin 7"
FT                   /evidence="ECO:0000269|PubMed:32646996"
FT   MOD_RES         230
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P12657"
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:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         455..460
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_056651"
FT   CONFLICT        173
FT                   /note="V -> M (in Ref. 3; CAA33334)"
FT                   /evidence="ECO:0000305"
FT   HELIX           27..52
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           59..76
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           78..88
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           95..128
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   TURN            130..132
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           133..135
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           139..168
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:6ZG4"
FT   HELIX           186..196
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           198..219
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           362..390
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   STRAND          391..393
FT                   /evidence="ECO:0007829|PDB:6WJC"
FT   HELIX           397..408
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           410..421
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           423..437
FT                   /evidence="ECO:0007829|PDB:6ZFZ"
FT   HELIX           439..441
FT                   /evidence="ECO:0007829|PDB:6OIJ"
SQ   SEQUENCE   460 AA;  51421 MW;  567C20F63541C8D0 CRC64;
     MNTSAPPAVS PNITVLAPGK GPWQVAFIGI TTGLLSLATV TGNLLVLISF KVNTELKTVN
     NYFLLSLACA DLIIGTFSMN LYTTYLLMGH WALGTLACDL WLALDYVASN ASVMNLLLIS
     FDRYFSVTRP LSYRAKRTPR RAALMIGLAW LVSFVLWAPA ILFWQYLVGE RTVLAGQCYI
     QFLSQPIITF GTAMAAFYLP VTVMCTLYWR IYRETENRAR ELAALQGSET PGKGGGSSSS
     SERSQPGAEG SPETPPGRCC RCCRAPRLLQ AYSWKEEEEE DEGSMESLTS SEGEEPGSEV
     VIKMPMVDPE AQAPTKQPPR SSPNTVKRPT KKGRDRAGKG QKPRGKEQLA KRKTFSLVKE
     KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW ELGYWLCYVN STINPMCYAL
     CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC
//
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