ACM2_CHICK
ID ACM2_CHICK Reviewed; 466 AA.
AC P30372;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Muscarinic acetylcholine receptor M2;
GN Name=CHRM2; Synonyms=CM2;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1840593; DOI=10.1016/s0021-9258(19)47384-5;
RA Tietje K.M., Nathanson N.M.;
RT "Embryonic chick heart expresses multiple muscarinic acetylcholine receptor
RT subtypes. Isolation and characterization of a gene encoding a novel m2
RT muscarinic acetylcholine receptor with high affinity for pirenzepine.";
RL J. Biol. Chem. 266:17382-17387(1991).
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
CC adenylate cyclase inhibition. Signaling promotes phospholipase C
CC activity, leading to the release of inositol trisphosphate (IP3); this
CC then triggers calcium ion release into the cytosol.
CC {ECO:0000269|PubMed:1840593}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1840593};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1840593}. Postsynaptic
CC cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: This receptor has a high affinity for pirenzepine.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Muscarinic acetylcholine receptor subfamily. CHRM2 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M73217; AAB04106.1; -; Genomic_DNA.
DR PIR; A40972; A40972.
DR RefSeq; NP_001025936.1; NM_001030765.1.
DR RefSeq; XP_015141117.1; XM_015285631.1.
DR RefSeq; XP_015141126.1; XM_015285640.1.
DR RefSeq; XP_015141131.1; XM_015285645.1.
DR AlphaFoldDB; P30372; -.
DR SMR; P30372; -.
DR STRING; 9031.ENSGALP00000020999; -.
DR PaxDb; P30372; -.
DR Ensembl; ENSGALT00000021029; ENSGALP00000020999; ENSGALG00000012894.
DR GeneID; 418126; -.
DR KEGG; gga:418126; -.
DR CTD; 1129; -.
DR VEuPathDB; HostDB:geneid_418126; -.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000158940; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P30372; -.
DR OMA; TSERQNH; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P30372; -.
DR TreeFam; TF320495; -.
DR Reactome; R-GGA-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-GGA-418594; G alpha (i) signalling events.
DR PRO; PR:P30372; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000012894; Expressed in heart and 6 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of 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:1990763; F:arrestin family protein binding; IEA:Ensembl.
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:0008016; P:regulation of heart contraction; IEA:InterPro.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001065; Musac_Ach_M2_rcpt.
DR InterPro; IPR000995; Musac_Ach_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PRINTS; PR00539; MUSCRINICM2R.
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; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..466
FT /note="Muscarinic acetylcholine receptor M2"
FT /id="PRO_0000069026"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 26..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 49..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 84..100
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 123..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 166..187
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 188..212
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 213..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 388..410
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 411..418
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 419..442
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 443..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 223..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 123..125
FT /note="Important for signaling"
FT MOTIF 436..440
FT /note="Important for signaling"
FT COMPBIAS 230..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 413..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 466 AA; 51565 MW; 2E3D8241D6168995 CRC64;
MNNSTYINSS SENVIALESP YKTIEVVFIV LVAGSLSLVT IIGNILVMVS IKVNRHLQTV
NNYFLFSLAC ADLIIGIFSM NLYTLYTVIG YWPLGPVVCD LWLALDYVVS NASVMNLLII
SFDRYFCVTK PLTYPVKRTT KMAGMMIAAA WVLSFILWAP AILFWQFIVG GRTVPDKDCY
IQFFSNPAVT FGTAIAAFYL PVIIMTVLYW QISRASKSRI KKGKKEAAQN QDPVSPSLVQ
GKIVKPNNNN IPTSSDGLEH NKVQNGKTTG ESVMENCVQG EEKDSSNDST SVSVVPSNTK
EDEAAKDASQ ISASQDHLKV ENSKLTCIRI VTKSQKGDCC APTNTTVEIV GTNGDEKQNS
VARKIVKMTK QPAKKKPPPS REKKVTRTIL AILLAFIITW TPYNVMVLIN SFCASCIPGT
VWTIGYWLCY INSTINPACY ALCNATFKKT FKHLLMCHYK NIGATR
