ACM5_MACMU
ID ACM5_MACMU Reviewed; 532 AA.
AC P56490;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Muscarinic acetylcholine receptor M5;
GN Name=CHRM5;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RL Submitted (SEP-1997) 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 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; AF026264; AAB95159.1; -; mRNA.
DR RefSeq; NP_001028103.1; NM_001032931.1.
DR AlphaFoldDB; P56490; -.
DR SMR; P56490; -.
DR STRING; 9544.ENSMMUP00000018686; -.
DR Ensembl; ENSMMUT00000019965; ENSMMUP00000018686; ENSMMUG00000014227.
DR GeneID; 574330; -.
DR KEGG; mcc:574330; -.
DR CTD; 1133; -.
DR VEuPathDB; HostDB:ENSMMUG00000014227; -.
DR VGNC; VGNC:71044; CHRM5.
DR eggNOG; KOG4220; Eukaryota.
DR GeneTree; ENSGT00940000158450; -.
DR HOGENOM; CLU_009579_11_2_1; -.
DR InParanoid; P56490; -.
DR OMA; RHGLWEV; -.
DR OrthoDB; 1245472at2759; -.
DR TreeFam; TF320495; -.
DR Proteomes; UP000006718; Chromosome 7.
DR Bgee; ENSMMUG00000014227; Expressed in spermatid and 4 other tissues.
DR ExpressionAtlas; P56490; baseline.
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; IBA:GO_Central.
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; IEA:Ensembl.
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:0019226; P:transmission of nerve impulse; IEA:Ensembl.
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 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..532
FT /note="Muscarinic acetylcholine receptor M5"
FT /id="PRO_0000069043"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 30..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 54..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 67..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 88..104
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 127..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 147..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 170..191
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 215..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 444..464
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 465..478
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 479..498
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 499..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 262..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 532 AA; 60141 MW; 33BCF6D67E600D79 CRC64;
MEGDSYHNAT TVNGTPVYHQ PLERHRLWEV ISIAAVTAVV SLITIVGNVL VMISFKVNSQ
LKTVNNYYLL SLACADLIIG IFSMNLYTTY ILMGRWALGS LACDLWLALD YVASNASVMN
LLVISFDRYF SITRPLTYRA KRTPKRAGVM IGLAWLISFI LWAPAILCWQ YLVGKRTVPL
DECQIQFLSE PTITFGTAIA AFYIPVSVMT ILYCRIYRET EKRTKDLADL QGSDSVTEAE
KRKPAHRALF RSCLRCPRPT LAQRERNQTS WSSSRRSAST SGKPSQATDP STNQAKAEQL
TTCSSYPSSE DEDKPATDPV LQVVYKSRGK ESPGEEFSSE DAEETFVKAQ TEKHDSDTPN
YFLSPAAAHR PKSQKCVAYK FRLVVKADGT QENNNGCHKV KIMPCSFPVA KEPSTKGLNP
NPSHQMTKRK RMVLVKERKA AQTLSAILLA FIITWTPYNI MVLVSTFCDK CVPVTLWHLG
YWLCYVNSTV NPICYALCNR TFRKTFKMLL LCRWKKKKVE EKLYWQGNSK LP
