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ACM4_MOUSE
ID   ACM4_MOUSE              Reviewed;         479 AA.
AC   P32211; Q64056;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Muscarinic acetylcholine receptor M4;
DE   AltName: Full=Mm4 mAChR;
GN   Name=Chrm4; Synonyms=Chrm-4;
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].
RX   PubMed=7916637; DOI=10.1016/0167-4781(93)90135-z;
RA   van Koppen C.J., Lenz W., Nathanson N.M.;
RT   "Isolation, sequence and functional expression of the mouse m4 muscarinic
RT   acetylcholine receptor gene.";
RL   Biochim. Biophys. Acta 1173:342-344(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 235-355.
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).
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       inhibition of adenylate cyclase.
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. CHRM4 sub-subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X63473; CAA45071.1; -; Genomic_DNA.
DR   EMBL; S74916; AAB33577.1; -; mRNA.
DR   CCDS; CCDS16439.1; -.
DR   PIR; S33776; S33776.
DR   RefSeq; NP_031725.1; NM_007699.2.
DR   AlphaFoldDB; P32211; -.
DR   SMR; P32211; -.
DR   IntAct; P32211; 1.
DR   MINT; P32211; -.
DR   STRING; 10090.ENSMUSP00000040808; -.
DR   BindingDB; P32211; -.
DR   ChEMBL; CHEMBL4572; -.
DR   DrugCentral; P32211; -.
DR   GlyGen; P32211; 2 sites.
DR   iPTMnet; P32211; -.
DR   PhosphoSitePlus; P32211; -.
DR   SwissPalm; P32211; -.
DR   PaxDb; P32211; -.
DR   PRIDE; P32211; -.
DR   ProteomicsDB; 285645; -.
DR   Antibodypedia; 26327; 208 antibodies from 30 providers.
DR   DNASU; 12672; -.
DR   Ensembl; ENSMUST00000045537; ENSMUSP00000040808; ENSMUSG00000040495.
DR   GeneID; 12672; -.
DR   KEGG; mmu:12672; -.
DR   UCSC; uc008kwv.2; mouse.
DR   CTD; 1132; -.
DR   MGI; MGI:88399; Chrm4.
DR   VEuPathDB; HostDB:ENSMUSG00000040495; -.
DR   eggNOG; KOG4220; Eukaryota.
DR   GeneTree; ENSGT00940000160394; -.
DR   HOGENOM; CLU_009579_11_2_1; -.
DR   InParanoid; P32211; -.
DR   OMA; YKTVEMV; -.
DR   OrthoDB; 1245472at2759; -.
DR   PhylomeDB; P32211; -.
DR   TreeFam; TF320495; -.
DR   Reactome; R-MMU-390648; Muscarinic acetylcholine receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 12672; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Chrm4; mouse.
DR   PRO; PR:P32211; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P32211; protein.
DR   Bgee; ENSMUSG00000040495; Expressed in superior frontal gyrus and 59 other tissues.
DR   ExpressionAtlas; P32211; baseline and differential.
DR   Genevisible; P32211; 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:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IDA:MGI.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
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; IDA:MGI.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR   GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001432; Musac_Ach_M4_rcpt.
DR   InterPro; IPR000995; Musac_Ach_rcpt.
DR   PANTHER; PTHR24248:SF142; PTHR24248:SF142; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   PRINTS; PR00541; MUSCRINICM4R.
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   2: Evidence at transcript 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..479
FT                   /note="Muscarinic acetylcholine receptor M4"
FT                   /id="PRO_0000069038"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        31..53
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        54..67
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        68..88
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        89..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        106..127
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        128..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        148..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        171..192
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        193..215
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        216..401
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        402..422
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        423..436
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        437..456
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        457..479
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          271..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         459
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         463
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         477
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        322..323
FT                   /note="AL -> V (in Ref. 2; AAB33577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="S -> N (in Ref. 2; AAB33577)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   479 AA;  52973 MW;  04F301E78814CD70 CRC64;
     MANFTPVNGS SANQSVRLVT TAHNHLETVE MVFIATVTGS LSLVTVVGNI LVMLSIKVNR
     QLQTVNNYFL FSLACADLII GAFSMNLYTL YIIKGYWPLG AVVCDLWLAL DYVVSNASVM
     NLLIISFDRY FCVTKPLTYP ARRTTKMAGL MIAAAWVLSF VLWAPAILFW QFVVGKRTVP
     DNQCFIQFLS NPAVTFGTAI AAFYLPVVIM TVLYIHISLA SRSRVHKHRP EGPKEKKAKT
     LAFLKSPLMK PSIKKPPPGG ASREELRNGK LEEAPPPALP PPPRPVADKD TSNESSSGSA
     TQNTKERPPT ELSTTEAATT PALPAPTLQP RTLNPASKWS KIQIVTKQTG SECVTAIEIV
     PATPAGMRPA ANVARKFASI ARNQVRKKRQ MAARERKVTR TIFAILLAFI LTWTPYNVMV
     LVNTFCQSCI PERVWSIGYW LCYVNSTINP ACYALCNATF KKTFRHLLLC QYRNIGTAR
 
 
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