ACM3_GORGO
ID ACM3_GORGO Reviewed; 590 AA.
AC Q9N2A3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Muscarinic acetylcholine receptor M3;
GN Name=CHRM3;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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; AB041397; BAA94482.1; -; Genomic_DNA.
DR RefSeq; XP_018887642.1; XM_019032097.1.
DR RefSeq; XP_018887649.1; XM_019032104.1.
DR RefSeq; XP_018887651.1; XM_019032106.1.
DR RefSeq; XP_018887653.1; XM_019032108.1.
DR AlphaFoldDB; Q9N2A3; -.
DR SMR; Q9N2A3; -.
DR STRING; 9593.ENSGGOP00000007281; -.
DR GeneID; 101123925; -.
DR KEGG; ggo:101123925; -.
DR CTD; 1131; -.
DR eggNOG; KOG4220; Eukaryota.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; Q9N2A3; -.
DR OrthoDB; 1245472at2759; -.
DR Proteomes; UP000001519; 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; 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: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: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 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_0000069028"
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 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 590 AA; 66086 MW; 2D8F90F54E774782 CRC64;
MTLHNNSTTS PLFPNISSSW IHSPSDAGLP PGTDTHFGSY NVSRAAGNFS SPDGTTDDPL
GGHTVWQVVF IAFLTGILAL VTIIGNILVI VSFKVNKQLK TVNNYFLLSL ACADLIIGVI
SMNLFTTYII MNRWALGNLA CDLWLAIDYV ASNASVMNLL VISFDRYFSI TRPLTYRAKR
TTKRAGVMIG LAWVISFVLW APAILFWQYF VGKRTVPPGE CFIQFLSEPT ITFGTAIAAF
YMPVTIMTIL YWRIYKETEK RTKELAGLQA SGTEAETENF VHPTGSSRSC SSYELQQQSM
KRSNRRKYGR CHFWFTTKSW KPSSEQMDQD HSSSDSWNNN DAAASLENSA SSDEEDIGSE
TRAIYSIVLK LPGHSTILNS TKLPSSDNLQ VPEEELGMVD LERKADKLQA QKSVDDGGSF
PKSFSKLPIQ LESAVDTAKT SDVNSSVGKS TATLPLSFKE ATLAKRFALK TRSQITKRKR
MSLVKEKKAA QTLSAILLAF IITWTPYNIM VLVNTFCDSC IPKTFWNLGY WLCYINSTVN
PVCYALCNKT FRTTFKMLLL CQCGKKKRRK QQYQQRQSVI FHKRAPEQAL
