Drd2
entrez
13489
canonical
uniprot
P61168
canonical
ensembl
ENSMUSG00000032259
resolver
ensp
ENSMUSP00000075170
resolver
ensp
ENSMUSP00000208183
resolver
genesymbol
Drd2
resolver
uniprot
P13953
resolver
uniprot
Q0VGH9
resolver
uniprot_entry
DRD2_MOUSE
resolver
uniprot_sec
P13953
resolver
uniprot_sec
Q0VGH9
resolver
amino_acid_sequence
MDPLNLSWYDDDLERQNWSRPFNGSEGKPDRPHYNYYAMLLTLLIFIIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMIAIVWVLSFTISCPLLFGLNNTDQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRKRRKRVNTKRSSRAFRANLKTPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRMDAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSNPDSPAKPEKNGHAKIVNPRIAKFFEIQTMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFMKILHC
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:11248120, PubMed:39415006, PubMed:40335693, PubMed:7566118, PubMed:9252189). 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:11248120). Dopamine receptors can be classified in two categories: (1) DRD2 (together with DRD3 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:11248120). In the central nervous system, DRD2 is mainly coupled to G(o)/GNAO1 (PubMed:11248120). 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 (PubMed:39415006, PubMed:40335693). DRD1 and DRD2 are the most abundant dopamine receptors in the central nervous system, especially in the basal ganglia and the prefrontal cortex (By similarity). DRD2 receptor plays a key role in risky decision-making by modulating reward sensitivity and executive control; DRD2 activation in nucleus accumbens cells leading to increased risk-taking and impulsivity (By similarity). DRD2 can also couple with G(q) by forming a heteromer with the ghrelin receptor GHSR in neurons independently of ghrelin (PubMed:22284186, PubMed:40441153). Following DRD2 activation by dopamine in lumbosacral defecation centers, GHSR acts as a coreceptor promoting DRD2 coupling to G(q) at the expense of G(i)/G(o), regulating defecation (PubMed:22284186, PubMed:40441153). In addition to dopamine, also acts as a receptor for tryptophan-derived metabolites in intestinal epithelial cells: activation by tryptophan metabolites produced by the gut microbiota initiates a phospholipase-C-dependent signaling that promotes colonization resistance by pathogens by controlling actin cytoskeletal organization in the gut epithelium (PubMed:38480886). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (PubMed:30936473). {ECO:0000250|UniProtKB:P14416, ECO:0000250|UniProtKB:P61169, ECO:0000269|PubMed:11248120, ECO:0000269|PubMed:22284186, ECO:0000269|PubMed:30936473, ECO:0000269|PubMed:38480886, ECO:0000269|PubMed:39415006, ECO:0000269|PubMed:40335693, ECO:0000269|PubMed:40441153, ECO:0000269|PubMed:7566118, ECO:0000269|PubMed:9252189}.
uniprot
proteins
mass_dalton
50930
uniprot
proteins
post_translational_modification
PTM: Palmitoylated. Palmitoylation which is required for proper localization to the plasma membrane and stability of the receptor could be carried on by ZDHHC4, ZDHHC3 and ZDHHC8. {ECO:0000250|UniProtKB:P14416}.; PTM: Phosphorylation of intracellular loop 3 by GRK2 and GRK3 following prolonged stimulation by dopamine, promoting association with beta-arrestin (ARRB1 or ARRB2), leading to receptor desensitization and negative regulation of G protein-coupled receptor signaling (By similarity). Constitutive phosphorylation (in absence of dopamine activation) by some isoforms of PKC-beta (PRKCB) inhibits G protein-coupled receptor signaling (By similarity). {ECO:0000250|UniProtKB:P14416}.; PTM: N-glycosylation is required for localization to the plasma membrane. {ECO:0000269|PubMed:8530376}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
11248120
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1991517
uniprot
proteins
pubmed
21233214
uniprot
proteins
pubmed
22284186
uniprot
proteins
pubmed
25865831
uniprot
proteins
pubmed
30936473
uniprot
proteins
pubmed
38480886
uniprot
proteins
pubmed
39415006
uniprot
proteins
pubmed
40335693
uniprot
proteins
pubmed
40441153
uniprot
proteins
pubmed
7566118
uniprot
proteins
pubmed
8530376
uniprot
proteins
pubmed
9252189
uniprot
proteins
sequence_length
444
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P61169}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:8530376}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly active on postsynaptic membrane. {ECO:0000250|UniProtKB:P61169}.
uniprot
proteins
transmembrane_region
TRANSMEM 38..60; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P14416"; TRANSMEM 71..93; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P14416"; TRANSMEM 109..130; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P14416"; TRANSMEM 152..172; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P14416"; TRANSMEM 189..213; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P14416"; TRANSMEM 375..396; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P14416"; TRANSMEM 411..432; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P14416
uniprot
proteins