Drd3
entrez
29238
canonical
uniprot
P19020
canonical
ensembl
ENSRNOG00000060806
resolver
ensp
ENSRNOP00000073117
resolver
genesymbol
Drd3
resolver
uniprot
P70647
resolver
uniprot_entry
DRD3_RAT
resolver
uniprot_sec
P70647
resolver
amino_acid_sequence
MAPLSQISTHLNSTCGAENSTGVNRARPHAYYALSYCALILAIIFGNGLVCAAVLRERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPSICSISNPDFVIYSSVVSFYVPFGVTVLVYARIYIVLRQRQRKRILTRQNSQCISIRPGFPQQSSCLRLHPIRQFSIRARFLSDATGQMEHIEDKQYPQKCQDPLLSHLQPPSPGQTHGGLKRYYSICQDTALRHPSLEGGAGMSPVERTRNSLSPTMAPKLSLEVRKLSNGRLSTSLRLGPLQPRGVPLREKKATQMVVIVLGAFIVCWLPFFLTHVLNTHCQACHVSPELYRATTWLGYVNSALNPVIYTTFNVEFRKAFLKILSC
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:1975644). Dopamine 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:1975644). Dopamine receptors can be classified in two categories: (1) DRD3 (together with DRD2 and DRD4) 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:1975644). 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). DRD3 is primarily expressed in limbic areas of the brain and is involved in the modulation of cognitive, emotional and motor functions: plays a key role in regulating neuronal signaling pathways associated with motivation, reward and behavior (By similarity). Involved in the incentive salience of drugs: controls responses to drug-related stimuli, making it a key target for reducing addiction to substances like cocaine, morphine, and alcohol (By similarity). Forms heterotetramers with DRD1 to potentiate beta-arrestin recruitment and mediate locomotor activity (By similarity). Also involved in autophagy regulation: receptor activation stimulates AMPK, which phosphorylates RPTOR and enhances its interaction with MTOR, thereby inhibiting mTORC1 signaling and its downstream target RPS6KB1 (By similarity). This leads to activation of ULK1 and initiation of the autophagy cascade (By similarity). {ECO:0000250|UniProtKB:P30728, ECO:0000250|UniProtKB:P35462, ECO:0000269|PubMed:1975644}.
uniprot
proteins
mass_dalton
49516
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by GRK4 (GRK4-alpha and GRK4-gamma). {ECO:0000250|UniProtKB:P35462}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P35462}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
1358063
uniprot
proteins
pubmed
14499480
uniprot
proteins
pubmed
1975644
uniprot
proteins
pubmed
2039532
uniprot
proteins
pubmed
8333859
uniprot
proteins
sequence_length
446
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35462}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35462}. Note=Both membrane-bound and scattered in the cytoplasm during basal conditions. Receptor stimulation results in the rapid internalization and sequestration of the receptors at the perinuclear area (5 and 15 minutes), followed by the dispersal of the receptors to the membrane (30 minutes). DRD3 and GRK4 co-localize in lipid rafts of renal proximal tubule cells. {ECO:0000250|UniProtKB:P35462}.
uniprot
proteins
transmembrane_region
TRANSMEM 33..55; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P35462"; TRANSMEM 66..88; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P35462"; TRANSMEM 105..126; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P35462"; TRANSMEM 150..170; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P35462"; TRANSMEM 188..209; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P35462"; TRANSMEM 376..397; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P35462"; TRANSMEM 413..432; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P35462
uniprot
proteins