ACM1_MACMU
ID ACM1_MACMU Reviewed; 460 AA.
AC P56489;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Muscarinic acetylcholine receptor M1;
GN Name=CHRM1;
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 -!- SUBUNIT: Interacts with GPRASP2 (By similarity). Interacts with TMEM147
CC (By similarity). {ECO:0000250|UniProtKB:P11229}.
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. CHRM1 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF026262; AAB95157.1; -; mRNA.
DR RefSeq; NP_001028117.1; NM_001032945.1.
DR AlphaFoldDB; P56489; -.
DR SMR; P56489; -.
DR STRING; 9544.ENSMMUP00000022746; -.
DR ChEMBL; CHEMBL1795124; -.
DR GeneID; 574362; -.
DR KEGG; mcc:574362; -.
DR CTD; 1128; -.
DR eggNOG; KOG4220; Eukaryota.
DR InParanoid; P56489; -.
DR OrthoDB; 1245472at2759; -.
DR PRO; PR:P56489; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016907; F:G protein-coupled acetylcholine receptor activity; IEA:InterPro.
DR GO; GO:0050890; P:cognition; IEA:InterPro.
DR GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
DR GO; GO:0046541; P:saliva secretion; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002228; Musac_Ach_M1_rcpt.
DR InterPro; IPR000995; Musac_Ach_rcpt.
DR PANTHER; PTHR24248:SF155; PTHR24248:SF155; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PRINTS; PR00538; MUSCRINICM1R.
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..460
FT /note="Muscarinic acetylcholine receptor M1"
FT /id="PRO_0000069016"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 23..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 49..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 63..84
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 85..95
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 96..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 122..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 143..164
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 165..185
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 186..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 210..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 367..390
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 391..401
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TRANSMEM 402..420
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT TOPO_DOM 421..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11229"
FT REGION 225..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12657"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 98..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 460 AA; 51433 MW; 1B19845C3BFE79CA CRC64;
MNTSAPPAVS PNITVLAPGK GPWQVAFIGI TTGLLSLATV TGNLLVLISF KVNTELKTVN
NYFLLSLACA DLIIGTFSMN LYTTYLLMGH WALGTLACDL WLALDYVASN ASVMNLLLIS
FDRYFSVTRP LSYRAKRTPR RAALMIGLAW LVSFVLWAPA ILFWQYLVGE RTVLAGQCYI
QFLSQPIITF GTAMAAFYLP VTVMCTLYWR IYRETENRAR ELAALQGSET PGKGGGSSSS
SERSQPGAEG SPETPPGRCC RCCRPPRLLQ AYSWKEDEEE DEGSMESLTS SEGEEPGSEV
VIKMPMVDPE AQAPTKQPPR SSPNTVKRPT KKGRDRAGKG QKPRGKEQLA KRKTFSLVKE
KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW ELGYWLCYVN STINPMCYAL
CNKAFRDTFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC
