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ACM3_PONPY
ID   ACM3_PONPY              Reviewed;         590 AA.
AC   Q9N2A2; Q5R9M0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Muscarinic acetylcholine receptor M3;
GN   Name=CHRM3;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate oran-Po13;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; the dimers can form tetramers (By similarity).
CC       Interacts with NALCN (By similarity). Interacts with TMEM147 (By
CC       similarity). {ECO:0000250|UniProtKB:P20309,
CC       ECO:0000250|UniProtKB:Q9ERZ3}.
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   -!- 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; AB041398; BAA94483.1; -; Genomic_DNA.
DR   EMBL; CR859367; CAH91540.1; -; mRNA.
DR   AlphaFoldDB; Q9N2A2; -.
DR   SMR; Q9N2A2; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:InterPro.
DR   GO; GO:0046541; P:saliva secretion; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Synapse; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..590
FT                   /note="Muscarinic acetylcholine receptor M3"
FT                   /id="PRO_0000069033"
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                   /evidence="ECO:0000250"
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        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   CONFLICT        31
FT                   /note="R -> P (in Ref. 2; CAH91540)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263
FT                   /note="K -> R (in Ref. 2; CAH91540)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="A -> T (in Ref. 2; CAH91540)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   590 AA;  66136 MW;  0FECCF6B6A8ECBAE CRC64;
     MTLHSNSTTS PLFPNISSSW IHSPSDAGLP RGTVTHFGSY NVSRAAGNFS SPNGPTDDPL
     GGHTVWQVVF IAFLTGILAL VTIIGNILVI VSFKVNKQLK TVNNYFLLSL ACADLIIGVI
     SMNLFTTYII MNRWALGNLA CDLWLAIDYV ASNASVMNLL VISFDRYFSI TRPLTYRAKR
     TTKRAGVMIG LAWVISFVLW APAILFWQYF VGKRTVPPGE CFIQFLSEPT ITFGTAIAAF
     YMPVTIMTIL YWRIYKETEK RTKELAGLQA SGTEAETENF VHPTGSSRSC SSYELQQQSM
     KRANRRKYGR CHFWFTTKSW KPSSEQMDQD HSSSDSWNNN DAAASLENSA SSDEEDIGSE
     TRAIYSIVLK LPGHSTILNS TKLPSSDNLQ VPEEELGMVD LERKANKLQA QKSVDDGGSF
     PKSFSKLPIQ LESAVDTAKT ADVNSSVGKT TATLPLSFKE ATLAKRFALK TRSQITKRKR
     MSLVKEKKAA QTLSAILLAF IITWTPYNIM VLVNTFCDSC IPKTFWNLGY WLCYINSTVN
     PVCYALCNKT FRTTFKMLLL CQCDKKKRRK QQYQQRQSVI FHKRAPEQAL
 
 
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