ACM4_CHICK
ID ACM4_CHICK Reviewed; 490 AA.
AC P17200;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Muscarinic acetylcholine receptor M4;
GN Name=CHRM4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2154460; DOI=10.1016/s0021-9258(19)39876-x;
RA Tietje K.M., Goldman P.S., Nathanson N.M.;
RT "Cloning and functional analysis of a gene encoding a novel muscarinic
RT acetylcholine receptor expressed in chick heart and brain.";
RL J. Biol. Chem. 265:2828-2834(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
CC inhibition of adenylate cyclase. May couple to multiple functional
CC responses in cell lines.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in heart and brain.
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; J05218; AAA48563.1; -; Genomic_DNA.
DR PIR; A35546; A35546.
DR RefSeq; NP_001026362.1; NM_001031191.1.
DR AlphaFoldDB; P17200; -.
DR SMR; P17200; -.
DR STRING; 9031.ENSGALP00000013605; -.
DR BindingDB; P17200; -.
DR PaxDb; P17200; -.
DR GeneID; 423195; -.
DR KEGG; gga:423195; -.
DR CTD; 1132; -.
DR VEuPathDB; HostDB:geneid_423195; -.
DR eggNOG; KOG4220; Eukaryota.
DR InParanoid; P17200; -.
DR OrthoDB; 1245472at2759; -.
DR PhylomeDB; P17200; -.
DR PRO; PR:P17200; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0016907; F:G protein-coupled acetylcholine receptor activity; NAS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; NAS:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; NAS:UniProtKB.
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 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 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..490
FT /note="Muscarinic acetylcholine receptor M4"
FT /id="PRO_0000069040"
FT TOPO_DOM 1..42
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 43..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 65..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 100..116
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 139..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 159..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 182..203
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 204..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 227..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 413..433
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 434..447
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 448..467
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 468..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 236..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..343
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 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 490 AA; 54937 MW; 2CDFDB5FA7D2298E CRC64;
MHNLSAQPWQ AKMANLTYDN VTLSNRSEVA IQPPTNYKTV ELVFIATVTG SLSLVTVVGN
ILVMLSIKVN RQLQTVNNYF LFSLACADLI IGVFSMNLYT VYIIKGYWPL GAVVCDLWLA
LDYVVSNASV MNLLIISFDR YFCVTKPLTY PARRTTKMAG LMIAAAWILS FILWAPAILF
WQFIVGKRTV HERECYIQFL SNPAVTFGTA IAAFYLPVVI MTVLYIHISL ASRSRVRRHK
PESRKERKGK SLSFFKAPPV KQNNNNSPKR AVEVKEEVRN GKVDDQPSAQ TEATGQQEEK
ETSNESSTVS MTQTTKDKPT TEILPAGQGQ SPAHPRVNPT SKWSKIKIVT KQTGTESVTA
IEIVPAKAGA SDHNSLSNSR PANVARKFAS IARSQVRKKR QMAAREKKVT RTIFAILLAF
ILTWTPYNVM VLINTFCETC VPETVWSIGY WLCYVNSTIN PACYALCNAT FKKTFKHLLM
CQYRNIGTAR
