ACM3_PIG
ID ACM3_PIG Reviewed; 590 AA.
AC P11483;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Muscarinic acetylcholine receptor M3;
GN Name=CHRM3;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3402600; DOI=10.1016/0014-5793(88)81274-2;
RA Akiba I., Kubo T., Maeda A., Bujo H., Nakai J., Mishina M., Numa S.;
RT "Primary structure of porcine muscarinic acetylcholine receptor III and
RT antagonist binding studies.";
RL FEBS Lett. 235:257-261(1988).
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; X12712; CAA31215.1; -; Genomic_DNA.
DR PIR; S01114; S01114.
DR RefSeq; NP_001116570.1; NM_001123098.1.
DR AlphaFoldDB; P11483; -.
DR SMR; P11483; -.
DR BindingDB; P11483; -.
DR PRIDE; P11483; -.
DR Ensembl; ENSSSCT00005039521; ENSSSCP00005024229; ENSSSCG00005024941.
DR Ensembl; ENSSSCT00015060537; ENSSSCP00015024322; ENSSSCG00015045363.
DR Ensembl; ENSSSCT00025005455; ENSSSCP00025002116; ENSSSCG00025004125.
DR Ensembl; ENSSSCT00030012542; ENSSSCP00030005632; ENSSSCG00030009177.
DR Ensembl; ENSSSCT00035027967; ENSSSCP00035010746; ENSSSCG00035021445.
DR Ensembl; ENSSSCT00040076397; ENSSSCP00040032836; ENSSSCG00040056396.
DR Ensembl; ENSSSCT00045021992; ENSSSCP00045015144; ENSSSCG00045012920.
DR Ensembl; ENSSSCT00050068737; ENSSSCP00050029507; ENSSSCG00050050504.
DR Ensembl; ENSSSCT00060013899; ENSSSCP00060005322; ENSSSCG00060010699.
DR Ensembl; ENSSSCT00065056498; ENSSSCP00065024575; ENSSSCG00065041295.
DR Ensembl; ENSSSCT00070036599; ENSSSCP00070030604; ENSSSCG00070018556.
DR GeneID; 100144478; -.
DR KEGG; ssc:100144478; -.
DR CTD; 1131; -.
DR InParanoid; P11483; -.
DR OrthoDB; 1245472at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 14.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
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:0045202; C:synapse; IBA:GO_Central.
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: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; ISS:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:InterPro.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; IBA:GO_Central.
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 3: Inferred from homology;
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_0000069032"
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 324..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 324..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 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 DISULFID 517..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 590 AA; 66078 MW; 9998D2A4802FD32A CRC64;
MTLHNNNTTS PLFPNISSSW IHGPSDAGLP PGTVTHFGSY NISQAAGNFS SPNGTTSDPL
GGHTIWQVVF IAFLTGILAL VTIIGNILVI VAFKVNKQLK TVNNYFLLSL ACADLIIGVI
SMNLFTTYII MNRWALGNLA CDLWLSIDYV ASNASVMNLL VISFDRYFSI TRPLTYRAKR
TTKRAGVMIG LAWVISFILW APAILFWQYF VGKRTVPPGE CFIQFLSEPT ITFGTAIAAF
YMPVTIMTIL YWRIYKETEK RTKELAGLQA SGTEAEAENF VHPTGSSRSC SSYELQQQSL
KRSARRKYGR CHFWFTTKSW KPSAEQMDQD HSSSDSWNNN DAAASLENSA SSDEEDIGSE
TRAIYSIVLK LPGHSTILNS TKLPSSDNLQ VPEEELGTVD LERKASKLQA QKSMDDGGSF
QKSFSKLPIQ LESAVDTAKA SDVNSSVGKT TATLPLSFKE ATLAKRFALK TRSQITKRKR
MSLIKEKKAA QTLSAILLAF IITWTPYNIM VLVNTFCDSC IPKTYWNLGY WLCYINSTVN
PVCYALCNKT FRTTFKMLLL CQCDKRKRRK QQYQQRQSVI FHKRVPEQAL
