DRD2_PANTR
ID DRD2_PANTR Reviewed; 443 AA.
AC P60026; Q5IS49;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=D(2) dopamine receptor;
DE AltName: Full=Dopamine D2 receptor;
GN Name=DRD2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate #130;
RA Takahashi A., Hayasaka I., Noaki Y., Saitou N.;
RT "Dopamine receptor D2 (DRD2) gene in Pan troglodytes.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC which inhibit adenylyl cyclase (By similarity). 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:P14416, ECO:0000250|UniProtKB:P61168}.
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; AB080609; BAC10668.1; -; Genomic_DNA.
DR EMBL; AY665279; AAV74317.1; -; mRNA.
DR RefSeq; NP_001029100.1; NM_001033928.1.
DR RefSeq; XP_016775319.1; XM_016919830.1.
DR RefSeq; XP_016775320.1; XM_016919831.1.
DR AlphaFoldDB; P60026; -.
DR SMR; P60026; -.
DR STRING; 9598.ENSPTRP00000045741; -.
DR PaxDb; P60026; -.
DR Ensembl; ENSPTRT00000104721; ENSPTRP00000069210; ENSPTRG00000004295.
DR GeneID; 451553; -.
DR KEGG; ptr:451553; -.
DR CTD; 1813; -.
DR VGNC; VGNC:3283; DRD2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155539; -.
DR InParanoid; P60026; -.
DR OrthoDB; 384993at2759; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000004295; Expressed in pituitary gland and 7 other tissues.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IBA:GO_Central.
DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IBA:GO_Central.
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:0007194; P:negative regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0043266; P:regulation of potassium ion transport; IBA:GO_Central.
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;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..443
FT /note="D(2) dopamine receptor"
FT /id="PRO_0000069389"
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 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"
FT CONFLICT 258
FT /note="K -> R (in Ref. 2; AAV74317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 50619 MW; 9BF8EA36C988A2E2 CRC64;
MDPLNLSWYD DDLERQNWSR PFNGSDGKAD RPHYNYYATL LTLLIAVIVF GNVLVCMAVS
REKALQTTTN YLIVSLAVAD LLVATLVMPW VVYLEVVGEW KFSRIHCDIF VTLDVMMCTA
SILNLCAISI DRYTAVAMPM LYNTRYSSKR RVTVMISIVW VLSFTISCPL LFGLNNADQN
ECIIANPAFV VYSSIVSFYV PFIVTLLVYI KIYIVLRRRR KRVNTKRSSR AFRAHLRAPL
KGNCTHPEDM KLCTVIMKSN GSFPVNRRRV EAARRAQELE MEMLSSTSPP ERTRYSPIPP
SHHQLTLPDP SHHGLHSTPD SPAKPEKNGH AKDHPKIAKI FEIQTMPNGK TRTSLKTMSR
RKLSQQKEKK ATQMLAIVLG VFIICWLPFF ITHILNIHCD CNIPPVLYSA FTWLGYVNSA
VNPIIYTTFN IEFRKAFLKI LHC
