ACM2_PIG
ID ACM2_PIG Reviewed; 466 AA.
AC P06199;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Muscarinic acetylcholine receptor M2;
GN Name=CHRM2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=3792556; DOI=10.1016/0014-5793(86)81144-9;
RA Kubo T., Maeda A., Sugimoto K., Akiba I., Mikami A., Takahashi H., Haga T.,
RA Haga K., Ichiyama A., Kangawa K., Matsuo H., Hirose T., Numa S.;
RT "Primary structure of porcine cardiac muscarinic acetylcholine receptor
RT deduced from the cDNA sequence.";
RL FEBS Lett. 209:367-372(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=3107123; DOI=10.1126/science.3107123;
RA Peralta E.G., Winslow J.W., Peterson G.L., Smith D.H., Ashkenazi A.,
RA Ramachandran J., Schimerlik M.I., Capon D.J.;
RT "Primary structure and biochemical properties of an M2 muscarinic
RT receptor.";
RL Science 236:600-606(1987).
RN [3]
RP PHOSPHORYLATION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9228066; DOI=10.1074/jbc.272.30.18882;
RA Schlador M.L., Nathanson N.M.;
RT "Synergistic regulation of m2 muscarinic acetylcholine receptor
RT desensitization and sequestration by G protein-coupled receptor kinase-2
RT and beta-arrestin-1.";
RL J. Biol. Chem. 272:18882-18890(1997).
RN [4]
RP INTERACTION WITH RACK1, AND SUBCELLULAR LOCATION.
RX PubMed=20976005; DOI=10.1371/journal.pone.0013517;
RA Reiner C.L., McCullar J.S., Kow R.L., Le J.H., Goodlett D.R.,
RA Nathanson N.M.;
RT "RACK1 associates with muscarinic receptors and regulates M(2) receptor
RT trafficking.";
RL PLoS ONE 5:E13517-E13517(2010).
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. {ECO:0000269|PubMed:9228066}.
CC -!- SUBUNIT: Interacts with ARRB1 and ARRB2 (By similarity). Interacts with
CC RACK1; the interaction regulates CHRM2 internalization. {ECO:0000250,
CC ECO:0000269|PubMed:20976005}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:20976005,
CC ECO:0000305|PubMed:3107123, ECO:0000305|PubMed:9228066}; Multi-pass
CC membrane protein {ECO:0000305}. Postsynaptic cell membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC Note=Phosphorylation in response to agonist binding promotes receptor
CC internalization. {ECO:0000269|PubMed:9228066}.
CC -!- PTM: Phosphorylated in response to agonist treatment.
CC {ECO:0000269|PubMed:9228066}.
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; X04708; CAA28413.1; -; mRNA.
DR EMBL; M16331; AAA30986.1; -; Genomic_DNA.
DR PIR; A27386; A27386.
DR RefSeq; NP_999426.1; NM_214261.1.
DR AlphaFoldDB; P06199; -.
DR SMR; P06199; -.
DR IntAct; P06199; 1.
DR BindingDB; P06199; -.
DR ChEMBL; CHEMBL4781; -.
DR DrugCentral; P06199; -.
DR PRIDE; P06199; -.
DR Ensembl; ENSSSCT00005029987; ENSSSCP00005018264; ENSSSCG00005019043.
DR Ensembl; ENSSSCT00005030016; ENSSSCP00005018285; ENSSSCG00005019043.
DR Ensembl; ENSSSCT00015049354; ENSSSCP00015019670; ENSSSCG00015037045.
DR Ensembl; ENSSSCT00015049468; ENSSSCP00015019722; ENSSSCG00015037045.
DR Ensembl; ENSSSCT00025012609; ENSSSCP00025004979; ENSSSCG00025009535.
DR Ensembl; ENSSSCT00030091367; ENSSSCP00030042034; ENSSSCG00030065386.
DR Ensembl; ENSSSCT00035017089; ENSSSCP00035005909; ENSSSCG00035013538.
DR Ensembl; ENSSSCT00045039850; ENSSSCP00045027745; ENSSSCG00045023330.
DR Ensembl; ENSSSCT00050056187; ENSSSCP00050023878; ENSSSCG00050041436.
DR Ensembl; ENSSSCT00055053377; ENSSSCP00055042595; ENSSSCG00055027008.
DR Ensembl; ENSSSCT00055053400; ENSSSCP00055042610; ENSSSCG00055027008.
DR Ensembl; ENSSSCT00060086672; ENSSSCP00060037487; ENSSSCG00060063522.
DR Ensembl; ENSSSCT00065006367; ENSSSCP00065002839; ENSSSCG00065004639.
DR Ensembl; ENSSSCT00070051184; ENSSSCP00070043296; ENSSSCG00070025599.
DR GeneID; 397498; -.
DR KEGG; ssc:397498; -.
DR CTD; 1129; -.
DR InParanoid; P06199; -.
DR PRO; PR:P06199; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 18.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0016907; F:G protein-coupled acetylcholine receptor activity; ISS:UniProtKB.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Synapse;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..466
FT /note="Muscarinic acetylcholine receptor M2"
FT /id="PRO_0000069024"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 23..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 46..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 81..97
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 98..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 120..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 140..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 163..184
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 210..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 218..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..122
FT /note="Important for signaling"
FT MOTIF 436..440
FT /note="Important for signaling"
FT COMPBIAS 230..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ4"
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 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 413..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 330
FT /note="K -> N (in Ref. 2; AAA30986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51673 MW; 53D089F179789CD9 CRC64;
MNNSTNSSNS GLALTSPYKT FEVVFIVLVA GSLSLVTIIG NILVMVSIKV NRHLQTVNNY
FLFSLACADL IIGVFSMNLY TLYTVIGYWP LGPVVCDLWL ALDYVVSNAS VMNLLIISFD
RYFCVTKPLT YPVKRTTKMA GMMIAAAWVL SFILWAPAIL FWQFIVGVRT VEDGECYIQF
FSNAAVTFGT AIAAFYLPVI IMTVLYWHIS RASKSRIKKD KKEPVANQEP VSPSLVQGRI
VKPNNNNMPG SDEALEHNKI QNGKAPRDAV TENCVQGEEK ESSNDSTSVS AVASNMRDDE
ITQDENTVST SLGHSKDENS KQTCIKIVTK TQKSDSCTPA NTTVELVGSS GQNGDEKQNI
VARKIVKMTK QPAKKKPPPS REKKVTRTIL AILLAFIITW APYNVMVLIN TFCAPCIPNT
VWTIGYWLCY INSTINPACY ALCNATFKKT FKHLLMCHYK NIGATR
