Drd2
entrez
24318
canonical
uniprot
P61169
canonical
ensembl
ENSRNOG00000008428
resolver
ensembl
ENSRNOG00055027586
resolver
ensembl
ENSRNOG00060016643
resolver
ensembl
ENSRNOG00065018800
resolver
ensp
ENSRNOP00000043759
resolver
ensp
ENSRNOP00000074235
resolver
genesymbol
Drd2
resolver
uniprot
P13953
resolver
uniprot_entry
DRD2_RAT
resolver
uniprot_sec
P13953
resolver
amino_acid_sequence
MDPLNLSWYDDDLERQNWSRPFNGSEGKADRPHYNYYAMLLTLLIFIIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMIAIVWVLSFTISCPLLFGLNNTDQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRKRRKRVNTKRSSRAFRANLKTPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRMDAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSNPDSPAKPEKNGHAKIVNPRIAKFFEIQTMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFMKILHC
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:1321233, PubMed:27007845, PubMed:2953072, PubMed:8599115). 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:14581469, PubMed:8599115). 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:14581469, PubMed:8599115). In the central nervous system, DRD2 is mainly coupled to G(o)/GNAO1 (By similarity). 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). 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 (PubMed:27007845). DRD2 can also couple with G(q) by forming a heteromer with the ghrelin receptor GHSR in neurons independently of ghrelin (By similarity). 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 (By similarity). 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 (By similarity). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (By similarity). {ECO:0000250|UniProtKB:P14416, ECO:0000250|UniProtKB:P61168, ECO:0000269|PubMed:1321233, ECO:0000269|PubMed:14581469, ECO:0000269|PubMed:27007845, ECO:0000269|PubMed:2953072, ECO:0000269|PubMed:8599115}.
uniprot
proteins
mass_dalton
50904
uniprot
proteins
mutagenesis
MUTAGEN 193; /note="S->A: Moderate decrease in ligand binding. 200-fold reduction of agonist-mediated cAMP inhibition."; /evidence="ECO:0000269|PubMed:1321233"; MUTAGEN 194; /note="S->A: Small decrease in agonist binding. Complete loss of agonist-mediated cAMP inhibition."; /evidence="ECO:0000269|PubMed:1321233"; MUTAGEN 197; /note="S->A: Small decrease in agonist binding. 18-fold reduction of agonist-mediated cAMP inhibition."; /evidence="ECO:0000269|PubMed:1321233"; MUTAGEN 228..229; /note="SS->AA: Decreased phosphorylation by PRKCB."; /evidence="ECO:0000269|PubMed:15347675"; MUTAGEN 233; /note="R->G: Shows decreased preference for GNAI2 and increased preference ofr GNAI3."; /evidence="ECO:0000269|PubMed:14581469"; MUTAGEN 234; /note="A->T: Shows decreased preference for GNAI2 and increased preference ofr GNAI1."; /evidence="ECO:0000269|PubMed:14581469"; MUTAGEN 352..355; /note="TRTS->VRVA: Decreased phosphorylation by PRKCB."; /evidence="ECO:0000269|PubMed:15347675"; MUTAGEN 355; /note="S->A: Decreased phosphorylation by PRKCB."; /evidence="ECO:0000269|PubMed:15347675"; MUTAGEN 420; /note="S->A: Moderate decrease in ligand binding."; /evidence="ECO:0000269|PubMed:1321233
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 (PubMed:19332542). Constitutive phosphorylation (in absence of dopamine activation) by some isoforms of PKC-beta (PRKCB) inhibits G protein-coupled receptor signaling (PubMed:15347675). {ECO:0000269|PubMed:15347675, ECO:0000269|PubMed:19332542}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10391935
uniprot
proteins
pubmed
1321233
uniprot
proteins
pubmed
1358063
uniprot
proteins
pubmed
14499480
uniprot
proteins
pubmed
14581469
uniprot
proteins
pubmed
15347675
uniprot
proteins
pubmed
16049099
uniprot
proteins
pubmed
19332542
uniprot
proteins
pubmed
2137198
uniprot
proteins
pubmed
2137336
uniprot
proteins
pubmed
2138567
uniprot
proteins
pubmed
2139615
uniprot
proteins
pubmed
2480527
uniprot
proteins
pubmed
2531656
uniprot
proteins
pubmed
2531846
uniprot
proteins
pubmed
2531847
uniprot
proteins
pubmed
27007845
uniprot
proteins
pubmed
2953072
uniprot
proteins
pubmed
2974511
uniprot
proteins
pubmed
8415621
uniprot
proteins
pubmed
8599115
uniprot
proteins
sequence_length
444
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:8415621}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P14416}; 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:0000269|PubMed:8415621}.
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