DRD5
entrez
1816
canonical
uniprot
P21918
canonical
ensembl
ENSG00000169676
resolver
ensp
ENSP00000306129
resolver
ensp
ENSP00000558703
resolver
ensp
ENSP00000623104
resolver
enst
ENST00000304374
resolver
enst
ENST00000888644
resolver
enst
ENST00000953045
resolver
genesymbol
DRD5
resolver
genesymbol_syn
DRD1B
resolver
genesymbol_syn
DRD1L2
resolver
hgnc
HGNC:3026
resolver
uniprot
B2R9S3
resolver
uniprot
Q8NEQ8
resolver
uniprot_entry
DRD5_HUMAN
resolver
uniprot_sec
B2R9S3
resolver
uniprot_sec
Q8NEQ8
resolver
activity_regulation
ACTIVITY REGULATION: Activated by the pan-agonist rotigotine, which activates all five dopamine receptors. {ECO:0000269|PubMed:37221270}.
uniprot
proteins
amino_acid_sequence
MLPPGSNGTAYPGQFALYQQLAQGNAVGGSAGAPPLGPSQVVTACLLTLLIIWTLLGNVLVCAAIVRSRHLRANMTNVFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDVWVAFDIMCSTASILNLCVISVDRYWAISRPFRYKRKMTQRMALVMVGLAWTLSILISFIPVQLNWHRDQAASWGGLDLPNNLANWTPWEEDFWEPDVNAENCDSSLNRTYAISSSLISFYIPVAIMIVTYTRIYRIAQVQIRRISSLERAAEHAQSCRSSAACAPDTSLRASIKKETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCSGHPEGPPAGFPCVSETTFDVFVWFGWANSSLNPVIYAFNADFQKVFAQLLGCSHFCSRTPVETVNISNELISYNQDIVFHKEIAAAYIHMMPNAVTPGNREVDNDEEEGPFDRMFQIYQTSPDGDPVAESVWELDCEGEISLDKITPFTPNGFH
uniprot
proteins
disease_involvement
DISEASE: Benign essential blepharospasm (BEB) [MIM:606798]: A primary focal dystonia affecting the orbicularis oculi muscles. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. BEB usually begins in middle age. Initial symptoms include eye irritation and frequent blinking, progressing to involuntary spasms of eyelid closure. Patients have normal eyes. The visual disturbance is due solely to the forced closure of the eyelids. In severe cases, this can lead to functional blindness. {ECO:0000269|PubMed:11781417}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry.
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:11500503, PubMed:1826762, PubMed:1834671, PubMed:37221270). 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:11500503, PubMed:1826762, PubMed:1834671, PubMed:37221270). Dopamine receptors can be classified in two categories: (1) DRD5 (together with DRD1) is a D1-type receptor and is coupled to G(s) G proteins, mediating activation of adenylate cyclase activity, while D2-type receptors (DRD2, DRD3 and DRD4) are coupled to G(i)/G(o) G proteins and promote inhibition of adenylate cyclase activity (PubMed:11500503, PubMed:1826762, PubMed:1834671, PubMed:37221270). 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:11500503, PubMed:1826762, PubMed:1834671, PubMed:37221270). DRD5 acts as a key regulator of blood pressure: negatively regulates the renin-angiotensin system (RAS), thereby reducing renal sodium absorption by the kidney (By similarity). {ECO:0000250|UniProtKB:Q8BLD9, ECO:0000269|PubMed:11500503, ECO:0000269|PubMed:1826762, ECO:0000269|PubMed:1834671, ECO:0000269|PubMed:37221270}.
uniprot
proteins
mass_dalton
52951
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="N->Q: Impairs subcellular location."; /evidence="ECO:0000269|PubMed:10531415"; MUTAGEN 98; /note="K->A: Does not affect activation by rotigotine."; /evidence="ECO:0000269|PubMed:37221270"; MUTAGEN 341; /note="F->A: Reduced activation by rotigotine."; /evidence="ECO:0000269|PubMed:37221270
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10531415
uniprot
proteins
pubmed
11500503
uniprot
proteins
pubmed
11781417
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1826762
uniprot
proteins
pubmed
1833775
uniprot
proteins
pubmed
1834671
uniprot
proteins
pubmed
37221270
uniprot
proteins
pubmed
7633397
uniprot
proteins
sequence_length
477
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10531415, ECO:0000269|PubMed:11500503}; Multi-pass membrane protein {ECO:0000269|PubMed:37221270}.
uniprot
proteins
transmembrane_region
TRANSMEM 41..66; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:37221270, ECO:0007744|PDB:8IRV"; TRANSMEM 76..99; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:37221270, ECO:0007744|PDB:8IRV"; TRANSMEM 112..138; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:37221270, ECO:0007744|PDB:8IRV"; TRANSMEM 155..180; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:37221270, ECO:0007744|PDB:8IRV"; TRANSMEM 223..248; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:37221270, ECO:0007744|PDB:8IRV"; TRANSMEM 292..317; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:37221270, ECO:0007744|PDB:8IRV"; TRANSMEM 340..361; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:37221270, ECO:0007744|PDB:8IRV
uniprot
proteins