ACM5_RAT
ID ACM5_RAT Reviewed; 531 AA.
AC P08911;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Muscarinic acetylcholine receptor M5;
GN Name=Chrm5; Synonyms=Chrm-5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3272174; DOI=10.1016/0896-6273(88)90190-0;
RA Bonner T.I., Young A.C., Brann M.R., Buckley N.J.;
RT "Cloning and expression of the human and rat m5 muscarinic acetylcholine
RT receptor genes.";
RL Neuron 1:403-410(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2540186; DOI=10.1016/s0021-9258(18)83237-9;
RA Liao C.-F., Themmen A.P.N., Joho R., Barberis C., Birnbaumer M.,
RA Birnbaumer L.;
RT "Molecular cloning and expression of a fifth muscarinic acetylcholine
RT receptor.";
RL J. Biol. Chem. 264:7328-7337(1989).
RN [3]
RP PROTEIN SEQUENCE OF 66-128.
RX PubMed=2380182; DOI=10.1016/s0021-9258(18)77406-1;
RA Kurtenbach E., Curtis C.A.M., Pedder E.K., Aitken A., Harris A.C.M.,
RA Hulme E.C.;
RT "Muscarinic acetylcholine receptors. Peptide sequencing identifies residues
RT involved in antagonist binding and disulfide bond formation.";
RL J. Biol. Chem. 265:13702-13708(1990).
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; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Muscarinic acetylcholine receptor subfamily. CHRM5 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M22926; AAA40658.1; -; mRNA.
DR EMBL; M22925; AAA41572.1; -; Genomic_DNA.
DR PIR; JT0531; JT0531.
DR RefSeq; NP_059058.1; NM_017362.4.
DR AlphaFoldDB; P08911; -.
DR SMR; P08911; -.
DR IntAct; P08911; 3.
DR MINT; P08911; -.
DR STRING; 10116.ENSRNOP00000008387; -.
DR BindingDB; P08911; -.
DR ChEMBL; CHEMBL277; -.
DR DrugCentral; P08911; -.
DR GuidetoPHARMACOLOGY; 17; -.
DR GlyGen; P08911; 1 site.
DR iPTMnet; P08911; -.
DR PhosphoSitePlus; P08911; -.
DR PaxDb; P08911; -.
DR Ensembl; ENSRNOT00000008387; ENSRNOP00000008387; ENSRNOG00000006397.
DR GeneID; 53949; -.
DR KEGG; rno:53949; -.
DR UCSC; RGD:620027; rat.
DR CTD; 1133; -.
DR RGD; 620027; Chrm5.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000158450; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P08911; -.
DR OMA; RHGLWEV; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P08911; -.
DR TreeFam; TF320495; -.
DR Reactome; R-RNO-390648; Muscarinic acetylcholine receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P08911; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006397; Expressed in brain.
DR Genevisible; P08911; RN.
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; IBA:GO_Central.
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; IDA:RGD.
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:0015872; P:dopamine transport; ISO:RGD.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0001696; P:gastric acid secretion; IEA:InterPro.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IMP:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000502; Musac_Ach_M5_rcpt.
DR InterPro; IPR000995; Musac_Ach_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PRINTS; PR00542; MUSCRINICM5R.
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..531
FT /note="Muscarinic acetylcholine receptor M5"
FT /id="PRO_0000069046"
FT TOPO_DOM 1..28
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 29..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 53..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 87..103
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 126..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 146..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 169..190
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 191..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 214..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 443..463
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 464..477
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 478..497
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 498..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 259..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 531 AA; 60137 MW; 647CE0D5D75A2BB1 CRC64;
MEGESYNEST VNGTPVNHQA LERHGLWEVI TIAVVTAVVS LMTIVGNVLV MISFKVNSQL
KTVNNYYLLS LACADLIIGI FSMNLYTTYI LMGRWVLGSL ACDLWLALDY VASNASVMNL
LVISFDRYFS ITRPLTYRAK RTPKRAGIMI GLAWLVSFIL WAPAILCWQY LVGKRTVPPD
ECQIQFLSEP TITFGTAIAA FYIPVSVMTI LYCRIYRETE KRTKDLADLQ GSDSVAEAKK
REPAQRTLLR SFFSCPRPSL AQRERNQASW SSSRRSTSTT GKTTQATDLS ADWEKAEQVT
TCSSYPSSED EAKPTTDPVF QMVYKSEAKE SPGKESNTQE TKETVVNTRT ENSDYDTPKY
FLSPAAAHRL KSQKCVAYKF RLVVKADGTQ ETNNGCRKVK IMPCSFPVSK DPSTKGPDPN
LSHQMTKRKR MVLVKERKAA QTLSAILLAF IITWTPYNIM VLVSTFCDKC VPVTLWHLGY
WLCYVNSTIN PICYALCNRT FRKTFKLLLL CRWKKKKVEE KLYWQGNSKL P
