ACM3_BOVIN
ID ACM3_BOVIN Reviewed; 590 AA.
AC P41984;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Muscarinic acetylcholine receptor M3;
GN Name=CHRM3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8061048; DOI=10.1016/0167-4889(94)90085-x;
RA Lee P.H., Hodges P.K., Glickman F., Chang K.J.;
RT "Cloning and expression of a cDNA encoding bovine muscarinic acetylcholine
RT m3 receptor.";
RL Biochim. Biophys. Acta 1223:151-154(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 327-467.
RC TISSUE=Adrenal gland;
RA Sui A.-L., Chou W.-Y., Kao L.-S.;
RT "Presence of multiple muscarinic receptor subtypes in bovine chromaffin
RT cells - analysis by polymerase chain reaction.";
RL Submitted (JAN-1994) 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.
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; U08286; AAA51866.1; -; mRNA.
DR EMBL; L27103; AAA30653.1; -; mRNA.
DR PIR; S47572; S47572.
DR RefSeq; NP_776695.1; NM_174270.2.
DR AlphaFoldDB; P41984; -.
DR SMR; P41984; -.
DR STRING; 9913.ENSBTAP00000010601; -.
DR iPTMnet; P41984; -.
DR PaxDb; P41984; -.
DR GeneID; 281685; -.
DR KEGG; bta:281685; -.
DR CTD; 1131; -.
DR eggNOG; KOG4220; Eukaryota.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P41984; -.
DR OrthoDB; 1245472at2759; -.
DR TreeFam; TF320495; -.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
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; Reference proteome; Synapse;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..590
FT /note="Muscarinic acetylcholine receptor M3"
FT /id="PRO_0000069027"
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..125
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 126..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..207
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 208..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..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 493..513
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 514..527
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 528..547
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 548..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 324..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..419
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 324..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..419
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 7
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 CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 424
FT /note="F -> S (in Ref. 2; AAA30653)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="A -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="A -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="A -> G (in Ref. 2; AAA30653)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="A -> G (in Ref. 2; AAA30653)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="F -> L (in Ref. 2; AAA30653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 66103 MW; 4DE04EDE33CCA8D6 CRC64;
MTLHNNNTTS PLFPNISSSW IHGPSDTGLP PGTVTHFGSY NISRAAGNLS SPNGTTSDPL
GGHTIWQVVF IAFLTGVLAL VTIIGNILVI VAFKVNKQLK TVNNYFLLSL ACADLIIGVI
SMNLFTTYII MNRWALGNLA CDLWLSIDYV ASNASVMNLL VISFDRYFSI TRPLTYRAKR
TTKRAGVMIG LAWVISFILW APAILFWQYF VGKRTVPPGE CFIQFLSEPT ITFGTAIAAF
YMPVTIMTIL YWRIYKETEK RTKELAGLQA SGTEAEAENF VHPTGSSRSC SSYELQQQSM
KRSARRKYGR CHFWFTTKSW KPSAEQMDQD HSSSDSWNNN DAAASLENSA SSDEEDIGSE
TRAIYSIVLK LPGHSTILNS TKLPSSDNLQ VPEEELGSVG LERKPSKLQT QQSMDDGGSF
QKSFSKLPIQ LESAVDTAKA SDVNSSVGKT TATLPLSFKE ATLAKRFALK TRSQITKRKR
MSLIKEKKAA QTLSAILLAF IITWTPYNIM VLVNTFCDSC IPKTYWNLGY WLCYINSTVN
PVCYALCNKT FRNTFKMLLL CQCDKRKRRK QQYQQRQSVI FHKRVPEQAL
