ID G3I2C8_CRIGR Unreviewed; 589 AA.
AC G3I2C8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Muscarinic acetylcholine receptor {ECO:0000256|RuleBase:RU361191};
GN Name=Chrm3 {ECO:0000313|Ensembl:ENSCGRP00001008816.1,
GN ECO:0000313|RefSeq:XP_027260852.1};
GN ORFNames=I79_017557 {ECO:0000313|EMBL:EGV95582.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV95582.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2] {ECO:0000313|EMBL:EGV95582.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCGRP00001008816.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:XP_027260852.1}
RP IDENTIFICATION.
RC STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027260852.1};
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_027260852.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00003336}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU361191};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU361191}.
CC Postsynaptic cell membrane {ECO:0000256|RuleBase:RU361191}; Multi-pass
CC membrane protein {ECO:0000256|RuleBase:RU361191}. Lateral cell membrane
CC {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034693}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034099}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Muscarinic acetylcholine receptor subfamily.
CC {ECO:0000256|RuleBase:RU361191}.
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DR EMBL; JH001127; EGV95582.1; -; Genomic_DNA.
DR RefSeq; XP_003509454.1; XM_003509406.3.
DR RefSeq; XP_007631833.1; XM_007633643.2.
DR RefSeq; XP_027260852.1; XM_027405051.2.
DR STRING; 10029.G3I2C8; -.
DR PaxDb; 10029-XP_007631833-1; -.
DR Ensembl; ENSCGRT00001012964.1; ENSCGRP00001008816.1; ENSCGRG00001011017.1.
DR GeneID; 100753955; -.
DR KEGG; cge:100753955; -.
DR CTD; 1131; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000160084; -.
DR OMA; ISASWIH; -.
DR OrthoDB; 4136179at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR Proteomes; UP000694386; Unplaced.
DR Proteomes; UP001108280; Chromosome 3.
DR GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IEA:Ensembl.
DR GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0046541; P:saliva secretion; IEA:Ensembl.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
DR CDD; cd15299; 7tmA_mAChR_M3; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
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 PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1.
DR PANTHER; PTHR24247:SF183; MUSCARINIC ACETYLCHOLINE RECEPTOR M3; 1.
DR Pfam; PF00001; 7tm_1; 2.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PRINTS; PR00540; MUSCRINICM3R.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU361191};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU000688};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361191};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257,
KW ECO:0000256|RuleBase:RU361191};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Synapse {ECO:0000256|RuleBase:RU361191};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361191}.
FT TRANSMEM 64..92
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361191"
FT TRANSMEM 104..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361191"
FT TRANSMEM 142..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361191"
FT TRANSMEM 184..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361191"
FT TRANSMEM 229..251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361191"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361191"
FT TRANSMEM 528..546
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361191"
FT DOMAIN 84..543
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 323..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 66140 MW; F5FAD2BBF567BA1E CRC64;
MTLHSNSTTS PLFPNISSSW VHSSSEAGLP LGTVTHLGSY NISQAAGNFS SNDTSSDPLG
GHTVWQVVFI AFLTGFLALV TIIGNILVIV AFKVNKQLKT VNNYFLLSLA CADLIIGVIS
MNLFTTYIIM NRWALGNLAC DLWLSIDYVA SNASVMNLLV ISFDRYFSIT RPLTYRAKRT
TKRAGVMIGL AWVISIVLWA PAILFWQYFV GKRTVPPGEC FIQFLSEPTI TFGTAIAAFY
MPVTIMTILY WRIYKETEKR TKELAGLQAS GTEAEAENFV HPTGSSRSCS SYELQQQSMK
RSSRRKYGRC HFWFTTKSWK PSVEQMDQDH SSSDSWNNND AAASLENSAS SDEEDIGSET
RAIYSIVLKL PGHSTILNAT KLPSSDNLQV PDEDLGTVDV ERNANKLQAQ KSMDDGDSCQ
KDFSKLPIQL ESAVDTTKTS DTNSSVDKTT STLPLSFKEA TLAKRFALKT RSQITKRKRM
SLIKEKKAAQ TLSAILLAFI ITWTPYNIMV LVNTFCDSCI PKTYWNLGYW LCYINSTVNP
VCYALCNKTF RTTFKMLLLC QCDKRKRRKQ QYQQRQSVIF HKRVPEQAL
//