DRD2_CHLAE
ID DRD2_CHLAE Reviewed; 443 AA.
AC P52702;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=D(2) dopamine receptor;
DE AltName: Full=Dopamine D2 receptor;
GN Name=DRD2;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=7783157; DOI=10.1021/jm00012a026;
RA Thurkauf A., Hutchinson A., Peterson J., Cornfield L., Meade R.,
RA Houston K., Harris K., Ross P.C., Gerber K., Ramabhadran T.V.;
RT "2-phenyl-4-(aminomethyl)imidazoles as potential antipsychotic agents.
RT Synthesis and dopamine D2 receptor binding.";
RL J. Med. Chem. 38:2251-2255(1995).
CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC which inhibit adenylyl cyclase (PubMed:7783157). Positively regulates
CC postnatal regression of retinal hyaloid vessels via suppression of
CC VEGFR2/KDR activity, downstream of OPN5 (By similarity).
CC {ECO:0000250|UniProtKB:P61168, ECO:0000269|PubMed:7783157}.
CC -!- SUBUNIT: Forms homo- and heterooligomers with DRD4. The interaction
CC with DRD4 may modulate agonist-induced downstream signaling. Interacts
CC with CADPS and CADPS2 (By similarity). Interacts with GPRASP1, PPP1R9B
CC and CLIC6. Interacts with ARRB2 (By similarity). Interacts with HTR2A
CC (By similarity). Interacts with DRD1. Interacts with KCNA2 (By
CC similarity). {ECO:0000250|UniProtKB:P14416,
CC ECO:0000250|UniProtKB:P61168, ECO:0000250|UniProtKB:P61169}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14416};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Palmitoylated. Palmitoylation which is required for proper
CC localization to the plasma membrane and stability of the receptor could
CC be carried on by ZDHHC4, ZDHHC3 and ZDHHC8.
CC {ECO:0000250|UniProtKB:P14416}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U18547; AAB60369.1; -; mRNA.
DR AlphaFoldDB; P52702; -.
DR SMR; P52702; -.
DR BindingDB; P52702; -.
DR ChEMBL; CHEMBL5456; -.
DR DrugCentral; P52702; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:UniProt.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB.
DR GO; GO:1903530; P:regulation of secretion by cell; IEA:UniProt.
DR InterPro; IPR001922; Dopamine_D2_rcpt.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00567; DOPAMINED2R.
DR PRINTS; PR00242; DOPAMINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Receptor; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..443
FT /note="D(2) dopamine receptor"
FT /id="PRO_0000069386"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 38..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 61..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 94..108
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 131..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 173..188
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 189..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 214..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 374..395
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 396..409
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 410..431
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 432..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 211..373
FT /note="Interaction with PPP1R9B"
FT /evidence="ECO:0000250"
FT REGION 281..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 194
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250"
FT LIPID 443
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14416"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 399..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 443 AA; 50590 MW; 34165BE6460B524D CRC64;
MDPLNLSWYD DDLERQNWSR PFNGSDGKAD RPHYNYYATL LTLLIAVIVF GNVLVCMAVS
REKALQTTTN YLIVSLAVAD LLVATLVMPW VVYLEVVGEW KFSKIHCDIF VTLDVMMCTA
SILNLCAISI DRYTAVAMPM LYNTRYSSKR RVTVMIAIVW VLSFTISCPL LFGLNNADQN
ECIIANPAFV VYSSIVSFYV PFIVTLLVYI KIYIVLRRRR KRVNTKRSSR AFRSHLRAPL
KGNCTHPEDM KLCTVIMKSN GSFPVNRRRV EAARRAQELE MEMLSSTSPP ERTRYSPIPP
SHHQLTLPDP SHHGLHSTPD SPAKPEKNGH AKNHPKIAKI FEIQTMPNGK TRTSLKTMSR
RKLSQQKEKK ATQMLAIVLG VFIICWLPFF ITHILNIHCD CNIPPVLYSA FTWLGYVNSA
VNPIIYTTFN IEFRKAFLKI LHC
