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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
 
 
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