P30729
uniprot
P30729
canonical
amino_acid_sequence
MGNSSATGDGGLLAGRGPESLGTGTGLGGAGAAALVGGVLLIGMVLAGNSLVCVSVASERILQTPTNYFIVSLAAADLLLAVLVLPLFVYSEVQGGVWLLSPRLCDTLMAMDVMLCTASIFNLCAISVDRFVAVTVPLRYNQQGQCQLLLIAATWLLSAAVAAPVVCGLNDVPGRDPTVCCLEDRDYVVYSSICSFFLPCPLMLLLYWATFRGLRRWEAARHTKLHSRAPRRPSGPGPPVSDPTQGPLFSDCPPPSPSLRTSPTVSSRPESDLSQSPCSPGCLLPDAALAQPPAPSSRRKRGAKITGRERKAMRVLPVVVGAFLMCWTPFFVVHITRALCPACFVSPRLVSAVTWLGYVNSALNPIIYTIFNAEFRSVFRKTLRLRC
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for dopamine, a catecholamine neurotransmitter hormone that functions as the brain's 'reward chemical', driving motivation, reinforcement learning and pleasure (PubMed:10832611). In addition to dopamine, also activated by epinephrine and norepinephrine, and by numerous synthetic agonists and drugs (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:10832611). Dopamine receptors can be classified in two categories: (1) DRD4 (together with DRD2 and DRD3) is a D2-type receptor and is coupled to G(i)/G(o) G proteins, mediating inhibition of adenylate cyclase activity, while D1-type receptors (DRD1 and DRD5) are coupled to G(s) G proteins and promote activation of adenylate cyclase activity (PubMed:10832611). D1- and D2-type dopamine receptors have antagonistic effects, particularly in the brain's striatum, where they govern voluntary movement and reward: D1-type receptors generally stimulate neural activity and promotes action, while D2-type receptors tend to inhibit neural activity and suppress movement (By similarity). DRD4 is expressed in the mesolimbic system of the brain, an area of the brain that regulates emotion and complex behavior (By similarity). Modulates the circadian rhythm of contrast sensitivity by regulating the rhythmic expression of NPAS2 in the retinal ganglion cells (By similarity). {ECO:0000250|UniProtKB:P21917, ECO:0000250|UniProtKB:P51436, ECO:0000269|PubMed:10832611}.
uniprot
proteins
mass_dalton
41294
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated via both ester and isopeptide bonds; leading to its degradation. {ECO:0000250|UniProtKB:P21917}.; PTM: Palmitoylated. Palmitoylation of the C-terminal Cys is important for normal expression at the cell membrane. {ECO:0000250|UniProtKB:P21917}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10832611
uniprot
proteins
pubmed
14499480
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
1554689
uniprot
proteins
pubmed
8078498
uniprot
proteins
sequence_length
387
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10832611}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 35..57; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P21917"; TRANSMEM 68..90; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P21917"; TRANSMEM 107..128; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P21917"; TRANSMEM 147..170; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P21917"; TRANSMEM 187..208; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P21917"; TRANSMEM 315..337; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P21917"; TRANSMEM 347..369; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P21917
uniprot
proteins