Drd3
entrez
13490
canonical
uniprot
P30728
canonical
ensembl
ENSMUSG00000022705
resolver
ensp
ENSMUSP00000023390
resolver
ensp
ENSMUSP00000155033
resolver
enst
ENSMUST00000229953
resolver
genesymbol
Drd3
resolver
uniprot
A0A2R8VHF0
resolver
uniprot
Q0VEC4
resolver
uniprot_entry
A0A2R8VHF0_MOUSE
resolver
uniprot_entry
DRD3_MOUSE
resolver
uniprot_entry
Q0VEC4_MOUSE
resolver
amino_acid_sequence
MAPLSQISSHINSTCGAENSTGVNRARPHAYYALSYCALILAIIFGNGLVCAAVLRERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPSICSISNPDFVIYSSVVSFYVPFGVTVLVYARIYMVLRQRRRKRILTRQNSQCISIRPGFPQQSSCLRLHPIRQFSIRARFLSDATGQMEHIEDKPYPQKCQDPLLSHLQPLSPGQTHGELKRYYSICQDTALRHPNFEGGGGMSQVERTRNSLSPTMAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVVIVLGAFIVCWLPFFLTHVLNTHCQACHVSPELYRATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC
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:10432116, PubMed:31626970, PubMed:8700864, PubMed:9402626, PubMed:9691085). 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 (By similarity). 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:8700864). 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 (PubMed:10432116). Forms heterotetramers with DRD1 to potentiate beta-arrestin recruitment and mediate locomotor activity (PubMed:40523512). 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:P35462, ECO:0000269|PubMed:10432116, ECO:0000269|PubMed:31626970, ECO:0000269|PubMed:40523512, ECO:0000269|PubMed:8700864, ECO:0000269|PubMed:9402626, ECO:0000269|PubMed:9691085}.
uniprot
proteins
mass_dalton
49669
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by GRK4. {ECO:0000250|UniProtKB:P35462}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:P35462}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10432116
uniprot
proteins
pubmed
31626970
uniprot
proteins
pubmed
40523512
uniprot
proteins
pubmed
7598803
uniprot
proteins
pubmed
8449953
uniprot
proteins
pubmed
8700864
uniprot
proteins
pubmed
9402626
uniprot
proteins
pubmed
9691085
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