ACM2_BOVIN
ID ACM2_BOVIN Reviewed; 465 AA.
AC P41985; Q3Y686;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Muscarinic acetylcholine receptor M2;
GN Name=CHRM2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corneal endothelium;
RA Rae J.L.;
RT "Ion channels in ocular epithelia.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 247-373.
RC TISSUE=Adrenal gland;
RA Sui A.-L., Chou W.-Y., Kao L.-S.;
RT "Presence of multiple muscarinic receptor subtypes in bovine chromaffin
RT cells - analysis by polymerase chain reaction.";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARRB1 and ARRB2. Interacts with RACK1; the
CC interaction regulates CHRM2 internalization (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Note=Phosphorylation in response
CC to agonist binding promotes receptor internalization. {ECO:0000250}.
CC -!- PTM: Phosphorylated in response to agonist treatment. {ECO:0000250}.
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; DQ154113; AAZ81568.1; -; mRNA.
DR EMBL; L27102; AAA30652.1; -; mRNA.
DR RefSeq; NP_001074202.1; NM_001080733.1.
DR RefSeq; XP_005205909.1; XM_005205852.3.
DR AlphaFoldDB; P41985; -.
DR SMR; P41985; -.
DR STRING; 9913.ENSBTAP00000019534; -.
DR BindingDB; P41985; -.
DR PaxDb; P41985; -.
DR PRIDE; P41985; -.
DR Ensembl; ENSBTAT00000019534; ENSBTAP00000019534; ENSBTAG00000014674.
DR GeneID; 522170; -.
DR KEGG; bta:522170; -.
DR CTD; 1129; -.
DR VEuPathDB; HostDB:ENSBTAG00000014674; -.
DR VGNC; VGNC:27319; CHRM2.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000158940; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P41985; -.
DR OMA; TSERQNH; -.
DR OrthoDB; 1245472at2759; -.
DR TreeFam; TF320495; -.
DR Reactome; R-BTA-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000014674; Expressed in myometrium and 37 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 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..465
FT /note="Muscarinic acetylcholine receptor M2"
FT /id="PRO_0000069020"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 22..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 45..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 80..96
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 97..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 162..183
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 184..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 209..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 387..409
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 410..417
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 418..441
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 442..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 217..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 119..121
FT /note="Important for signaling"
FT MOTIF 435..439
FT /note="Important for signaling"
FT COMPBIAS 229..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ4"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 464
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 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 412..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 465 AA; 51613 MW; 6DDA56A83B04ACEB CRC64;
MNNSTNSSNN VALTSPYKTF EVVFIVLVAG SLSLVTIIGN ILVMVSIKVN RHLQTVNNYF
LFSLACADLI IGVFSMNLYT LYTVIGYWPL GPVVCDLWLA LDYVVSNASV MNLLIISFDR
YFCVTKPLTY PVKRTTKMAG MMIAAAWVLS FILWAPAILF WQFIVGVRTV EDGECYIQFF
SNAAVTFGTA IAAFYLPVII MTVLYWHISR ASKSRIKKDK KEPVANQDPV SPSLVQGRIV
KPNNNNMPGS DDGLEHNKIQ NGKTPRDAVT ENCVQGEEKE SSNDSTSVSA VASNMRDDEI
TQDENTVSTS VGHSKDENSK QTCIKIVTKT PKGDQCTPTN TTVELVGSSG QNGDEKQNIV
ARKIVKMTKQ PAKKKPPPSR EKKVTRTILA ILLAFIITWA PYNVMVLINT FCAPCIPNTV
WTIGYWLCYI NSTINPACYA LCNATFKKTF KHLLMCHYKN IGATR
