ACM2_PANTR
ID ACM2_PANTR Reviewed; 440 AA.
AC Q9N2A7;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Muscarinic acetylcholine receptor M2;
DE Flags: Fragment;
GN Name=CHRM2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 220;
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
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; AB041392; BAA94477.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9N2A7; -.
DR SMR; Q9N2A7; -.
DR STRING; 9598.ENSPTRP00000054285; -.
DR PaxDb; Q9N2A7; -.
DR eggNOG; KOG4220; Eukaryota.
DR InParanoid; Q9N2A7; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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 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; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Synapse; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN <1..440
FT /note="Muscarinic acetylcholine receptor M2"
FT /id="PRO_0000069023"
FT TRANSMEM <1..19
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 20..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..54
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 55..71
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 72..93
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 94..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 114..136
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 137..158
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 159..183
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 184..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 362..384
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 385..392
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 393..416
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 417..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 192..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 94..96
FT /note="Important for signaling"
FT MOTIF 410..414
FT /note="Important for signaling"
FT COMPBIAS 204..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERZ4"
FT MOD_RES 420
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT DISULFID 70..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 387..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
SQ SEQUENCE 440 AA; 48854 MW; 12B0324E13D37DDF CRC64;
VLVAGSLSLV TIIGNILVMV SIKVNRHLQT VNNYFLFSLA CADLIIGVFS MNLYTLYTVI
GYWPLGPVVC DLWLALDYVV SNASVMNLLI ISFDRYFCVT KPLTYPVKRT TKMAGMMIAA
AWVLSFILWA PAILFWQFIV GVRTVEDGEC YIQFFSNAAV TFGTAIAAFY LPVIIMTVLY
WHISRASKSR IKKDKKEPVA NQDPVSPSLV QGRIVKPNNN NMPSSDDGLE HNKIQNGKAP
RDPVTENCVQ GEEKESSNDS TSVSAVASNM RDDEITQDEN TVSTSLGHSK DENSKQTCIR
IGTKTPKSDS CTPTNTTVEV VGSSGQNGDE KQNIVARKIV KMTKQPAKKK PPPSREKKVT
RTILAILLAF IITWAPYNVM VLINTFCAPC IPNTVWTIGY WLCYINSTIN PACYALCNAT
FKKTFKHLLM CHYKNIGATR
