ACM3_CHICK
ID ACM3_CHICK Reviewed; 639 AA.
AC P49578;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Muscarinic acetylcholine receptor M3;
GN Name=CHRM3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7929287; DOI=10.1016/s0021-9258(18)47321-8;
RA Gadbut A.P., Galper J.B.;
RT "A novel M3 muscarinic acetylcholine receptor is expressed in chick atrium
RT and ventricle.";
RL J. Biol. Chem. 269:25823-25829(1994).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20309};
CC Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane;
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Brain, heart atria, and ventricle.
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; L10617; AAA65961.1; -; mRNA.
DR PIR; A55019; A55019.
DR RefSeq; NP_990730.1; NM_205399.1.
DR AlphaFoldDB; P49578; -.
DR SMR; P49578; -.
DR STRING; 9031.ENSGALP00000017509; -.
DR PaxDb; P49578; -.
DR GeneID; 396364; -.
DR KEGG; gga:396364; -.
DR CTD; 1131; -.
DR VEuPathDB; HostDB:geneid_396364; -.
DR eggNOG; KOG4220; Eukaryota.
DR InParanoid; P49578; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P49578; -.
DR PRO; PR:P49578; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..639
FT /note="Muscarinic acetylcholine receptor M3"
FT /id="PRO_0000069035"
FT TOPO_DOM 1..115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..139
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 153..173
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..190
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 191..212
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 213..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 233..255
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 256..277
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 278..300
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 301..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 543..563
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 564..576
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 577..596
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 597..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 370..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 189..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 639 AA; 71977 MW; 7243F132B561B446 CRC64;
MLTHYQLCFQ KRSSQNYTVP DPTSCFDVPP WTILCQRATM IMHNNSSALP LFSNVSSFWK
RDSHGPGLLD EGASLIGSYD SPETTESFPF STVETTNSSL NATIKDPLGG HAVWQVVLIA
FLTGIIALVT IIGNILVIVS FKVNKQLKTV NNYFLLSLAC ADLIIGVISM NLFTTYIIMG
HWALGNLACD LWLSIDYVAS NASVMNLLVI SFDRYFSITR PLTYRAKRTT KRAGVMIGLA
WIISFVLWAP AILFWQYFVG KRTVPLDECF IQFLSEPIIT FGTAIAAFYL PVTIMSILYW
RIYKETEKRT KELAGLQASG SEAETARFVH QTGSSRSLSS YELQRQSTKR SSRRKYRRCH
FWLTMKSWEP NTDQGDQEHS SSDSWNNNDA AASLENSASS DEEDITAETR AIYSIVLKLP
GHSAILNSTK LPSSEDLNES ADELQKSDTD SQEKKPKKLQ PPKSIQDGGS FQKSFSKLPI
QPGSAETATA SDGISSVTKT SAALPLSFKE ATLAKKFALK TRSQITKRKR MSLIKEKKAA
QTLSAILFAF IITWTPYNIM VLVNTFCDCV PKTVWNLGYW LCYINSTVNP VCYALCNKMF
RNTFKMLLLC QCDKRKRRKQ QYQQRQSVIF HKRIPREAS
