DRD4_MUSPF
ID DRD4_MUSPF Reviewed; 357 AA.
AC Q6TLJ0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=D(4) dopamine receptor;
DE AltName: Full=Dopamine D4 receptor;
GN Name=DRD4;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gubbins E.J., Masters J., Moreland R.B.;
RT "Cloning and functional expression of ferret dopamine D2 and D4
RT receptors.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dopamine receptor responsible for neuronal signaling in the
CC mesolimbic system of the brain, an area of the brain that regulates
CC emotion and complex behavior. Activated by dopamine, but also by
CC epinephrine and norepinephrine, and by numerous synthetic agonists and
CC drugs. Agonist binding triggers signaling via G proteins that inhibit
CC adenylyl cyclase. Modulates the circadian rhythm of contrast
CC sensitivity by regulating the rhythmic expression of NPAS2 in the
CC retinal ganglion cells. {ECO:0000250|UniProtKB:P21917,
CC ECO:0000250|UniProtKB:P51436}.
CC -!- SUBUNIT: Forms homo- and heterooligomers with DRD2. D4.7 allele
CC exhibits higher affinity for homodimers compared to DRD2 heterodimers,
CC while alleles D42. and 4.4 have similar affinities for both. The
CC interaction with DRD2 may modulate agonist-induced downstream signaling
CC (By similarity). Interacts with CLIC6 (By similarity). Interacts with
CC GPRASP1. May interact with ADORA2A. Interacts with KLHL12 (By
CC similarity). {ECO:0000250|UniProtKB:P21917,
CC ECO:0000250|UniProtKB:P30729}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21917};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P21917}.
CC -!- PTM: Polyubiquitinated by the BCR(KLHL12) E3 ubiquitin ligase complex:
CC polyubiquitination does not lead to degradation of DRD4 protein.
CC {ECO:0000250|UniProtKB:P21917}.
CC -!- PTM: Palmitoylated. Palmitoylation of the C-terminal Cys is important
CC for normal expression at the cell membrane.
CC {ECO:0000250|UniProtKB:P21917}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY394848; AAQ95734.1; -; mRNA.
DR RefSeq; NP_001297096.1; NM_001310167.1.
DR AlphaFoldDB; Q6TLJ0; -.
DR SMR; Q6TLJ0; -.
DR GeneID; 106004514; -.
DR CTD; 1815; -.
DR InParanoid; Q6TLJ0; -.
DR Proteomes; UP000000715; Unassembled WGS sequence.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0035240; F:dopamine binding; ISS:UniProtKB.
DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR002185; Dopamine_D4_rcpt.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248:SF143; PTHR24248:SF143; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00569; DOPAMINED4R.
DR PRINTS; PR00242; DOPAMINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Biological rhythms; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Receptor; Reference proteome; Sodium; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..357
FT /note="D(4) dopamine receptor"
FT /id="PRO_0000232451"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 33..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 56..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 66..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 89..104
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 127..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 147..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 171..186
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 187..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 209..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 285..307
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 308..316
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 317..339
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 340..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT REGION 225..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT BINDING 117
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT LIPID 357
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 310..313
FT /evidence="ECO:0000250|UniProtKB:P21917"
SQ SEQUENCE 357 AA; 37701 MW; 4B06C705F02CF998 CRC64;
MGNRSAADAD GLLAGRGPGT GGGAGSPGAA AALVGGVLLI GAVLAGNALV CVSVAAERAL
QTPTNYFIVS LAAADLLLAL LVLPLFVYSE VQGGVWQFSP GLCDALMAMD VMLCTASIFN
LCAISADRFV AVAVPLSYNR QSGGGRQLLL IGATWLLSAA VAAPVLCGLN DARGRDPAVC
RLEDRDYVVY SSVCSFFLPC PVMLLLYWAT FRGLRRWEAA RRTKLHGRRP RRPSGPGPPP
PEAVETPEAP EAIPTPDATL AEPALPASEE RRAKITGRER KAMRVLPVVV GAFLVCWTPF
FVVHITGALC PACAVPPRLV SAVTWLGYVN SALNPLIYTV FNAEFRAVFR KALRLCC
