ACM4_XENLA
ID ACM4_XENLA Reviewed; 484 AA.
AC P30544;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Muscarinic acetylcholine receptor M4;
GN Name=chrm4;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Ovary;
RX PubMed=7925970; DOI=10.1016/0014-5793(94)00957-0;
RA Herrera L., Carvallo P., Antonelli M., Olate J.;
RT "Cloning of a Xenopus laevis muscarinic receptor encoded by an intronless
RT gene.";
RL FEBS Lett. 352:175-179(1994).
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 inhibition of adenylate cyclase.
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. CHRM4 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X65865; CAA46694.1; -; Genomic_DNA.
DR PIR; S48657; S48657.
DR Proteomes; UP000186698; Genome assembly.
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:0040012; P:regulation of locomotion; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001432; Musac_Ach_M4_rcpt.
DR InterPro; IPR000995; Musac_Ach_rcpt.
DR PANTHER; PTHR24248:SF142; PTHR24248:SF142; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00243; MUSCARINICR.
DR PRINTS; PR00541; MUSCRINICM4R.
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; Glycoprotein;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..484
FT /note="Muscarinic acetylcholine receptor M4"
FT /id="PRO_0000069041"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 33..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 56..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 91..107
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 108..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 130..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 173..194
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 218..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 407..427
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 428..441
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 442..461
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 462..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 259..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 484 AA; 54137 MW; D83BD856DE302BE8 CRC64;
MENDTWENES SASNHSIDET IVEIPGKYQT MEMIFIATVT GSLSLVTVVG NILVMLSIKV
NRQLQTVNNY FLFSLACADL IIGVFSMNLY SLYIIKGYWP LGPIVCDLWL ALDYVVSNAS
VMNLLIISLE RXFCVTKPLT YPARRTTKMA GLMIAAAWLL SFELWAPAIL FWQFIVGQRT
VPSGECYIQF LSNPAVTFGT AIAAFYLPVV IMTILYIHIS LASRSRVRRH CPETRQEKKK
PISSMKSLLI KQTKNIPKQD AGDKVVEKKN GVSNGKIEKS MTNLQTAEEK ETSNESSSAS
LSHNPPEKQP LSEASSGVVL APTQSMPPLP AKANTASKWS KIKIVTKQTG NECVTAIEIV
PECAIPLPEQ ANNRPVNVAR KFASIARNQV RKKRQMAARE KKVTRTIFAI LLAFIITWTP
YNVMVLINTF CQTCIPETIW YIGYWLCYVN STINPACYAL CNATFKKTFK HLLMCQYKSI
GTAR
