ACM2_MOUSE
ID ACM2_MOUSE Reviewed; 466 AA.
AC Q9ERZ4; E9Q9P0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Muscarinic acetylcholine receptor M2;
GN Name=Chrm2; Synonyms=Chrm-2;
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 (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Heart;
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).
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
CC adenylate cyclase inhibition. Signaling promotes phospholipase C
CC activity, leading to the release of inositol trisphosphate (IP3); this
CC then triggers calcium ion release into the cytosol (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARRB1 and ARRB2. Interacts with RACK1; the
CC interaction regulates CHRM2 internalization (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Note=Phosphorylation in response
CC to agonist binding promotes receptor internalization. {ECO:0000250}.
CC -!- PTM: Phosphorylated in response to agonist treatment. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Muscarinic acetylcholine receptor subfamily. CHRM2 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF264049; AAG14343.1; -; Genomic_DNA.
DR EMBL; AC113246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS20004.1; -.
DR RefSeq; NP_987076.2; NM_203491.3.
DR RefSeq; XP_006506199.1; XM_006506136.2.
DR AlphaFoldDB; Q9ERZ4; -.
DR SMR; Q9ERZ4; -.
DR STRING; 10090.ENSMUSP00000130874; -.
DR BindingDB; Q9ERZ4; -.
DR ChEMBL; CHEMBL3197; -.
DR DrugCentral; Q9ERZ4; -.
DR GuidetoPHARMACOLOGY; 14; -.
DR GlyGen; Q9ERZ4; 3 sites.
DR iPTMnet; Q9ERZ4; -.
DR PhosphoSitePlus; Q9ERZ4; -.
DR SwissPalm; Q9ERZ4; -.
DR PaxDb; Q9ERZ4; -.
DR PRIDE; Q9ERZ4; -.
DR ProteomicsDB; 285839; -.
DR Antibodypedia; 18171; 566 antibodies from 39 providers.
DR DNASU; 243764; -.
DR Ensembl; ENSMUST00000172278; ENSMUSP00000130874; ENSMUSG00000045613.
DR GeneID; 243764; -.
DR KEGG; mmu:243764; -.
DR UCSC; uc009biy.2; mouse.
DR CTD; 1129; -.
DR MGI; MGI:88397; Chrm2.
DR VEuPathDB; HostDB:ENSMUSG00000045613; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000158940; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; Q9ERZ4; -.
DR OMA; TSERQNH; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; Q9ERZ4; -.
DR TreeFam; TF320495; -.
DR Reactome; R-MMU-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 243764; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Chrm2; mouse.
DR PRO; PR:Q9ERZ4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9ERZ4; protein.
DR Bgee; ENSMUSG00000045613; Expressed in interventricular septum and 67 other tissues.
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:0098981; C:cholinergic synapse; IMP:SynGO.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic 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:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032280; C:symmetric synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:1990763; F:arrestin family protein binding; ISO:MGI.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IMP: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: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:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IMP:MGI.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001065; Musac_Ach_M2_rcpt.
DR InterPro; IPR000995; Musac_Ach_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PRINTS; PR00539; MUSCRINICM2R.
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; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..466
FT /note="Muscarinic acetylcholine receptor M2"
FT /id="PRO_0000069022"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 23..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 46..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 81..97
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 98..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 120..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 140..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 163..184
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 210..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 388..410
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 411..418
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 419..442
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 443..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 218..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..122
FT /note="Important for signaling"
FT MOTIF 436..440
FT /note="Important for signaling"
FT COMPBIAS 230..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 413..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 266
FT /note="P -> L (in Ref. 1; AAG14343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51499 MW; 93F90B639CB45AE3 CRC64;
MNNSTNSSNN GLAITSPYKT FEVVFIVLVA GSLSLVTIIG NILVMVSIKV NRHLQTVNNY
FLFSLACADL IIGVFSMNLY TLYTVIGYWP LGPVVCDLWL ALDYVVSNAS VMNLLIISFD
RYFCVTKPLT YPVKRTTKMA GMMIAAAWVL SFILWAPAIL FWQFIVGVRT VEDGECYIQF
FSNAAVTFGT AIAAFYLPVI IMTVLYWHIS RASKSRIKKE KKEPVANQDP VSPSLVQGRI
VKPNNNNMPG GDGGLEHNKI QNGKAPRDGG TENCVQGEEK ESSNDSTSVS AVASNMRDDE
ITQDENTVST SLGHSKDDNS RQTCIKIVTK TQKGDACTPT STTVELVGSS GQNGDEKQNI
VARKIVKMTK QPAKKKPPPS REKKVTRTIL AILLAFIITW APYNVMVLIN TFCAPCIPNT
VWTIGYWLCY INSTINPACY ALCNATFKKT FKHLLMCHYK NIGATR
