DRD2_BOVIN
ID DRD2_BOVIN Reviewed; 444 AA.
AC P20288;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=D(2) dopamine receptor;
DE AltName: Full=Dopamine D2 receptor;
GN Name=DRD2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=2137198; DOI=10.1038/343266a0;
RA Chio C.L., Hess G.F., Graham R.S., Huff R.M.;
RT "A second molecular form of D2 dopamine receptor in rat and bovine caudate
RT nucleus.";
RL Nature 343:266-269(1990).
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 (By similarity). The
CC interaction with DRD4 may modulate agonist-induced downstream signaling
CC (By similarity). Interacts with CADPS and CADPS2 (By similarity).
CC Interacts with GPRASP1, PPP1R9B and CLIC6 (By similarity). Interacts
CC with ARRB2 (By similarity). Interacts with HTR2A (By similarity).
CC Interacts with DRD1 (By similarity). 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P20288-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P20288-2; Sequence=VSP_001869;
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; X51657; CAA35970.1; -; mRNA.
DR PIR; S08163; DYBOD2.
DR RefSeq; NP_776468.1; NM_174043.2. [P20288-1]
DR AlphaFoldDB; P20288; -.
DR SMR; P20288; -.
DR STRING; 9913.ENSBTAP00000014422; -.
DR BindingDB; P20288; -.
DR ChEMBL; CHEMBL3998; -.
DR DrugCentral; P20288; -.
DR PaxDb; P20288; -.
DR PRIDE; P20288; -.
DR GeneID; 281126; -.
DR KEGG; bta:281126; -.
DR CTD; 1813; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P20288; -.
DR OrthoDB; 384993at2759; -.
DR Proteomes; UP000009136; Unplaced.
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: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:1903488; P:negative regulation of lactation; IMP:AgBase.
DR GO; GO:1902721; P:negative regulation of prolactin secretion; IMP:AgBase.
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:1903521; P:positive regulation of mammary gland involution; IMP:AgBase.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..444
FT /note="D(2) dopamine receptor"
FT /id="PRO_0000069384"
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..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 375..396
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 397..410
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 411..432
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 433..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 211..374
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 in receptor activation"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250"
FT LIPID 444
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 400..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 242..270
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:2137198"
FT /id="VSP_001869"
SQ SEQUENCE 444 AA; 50672 MW; 67437197629301C7 CRC64;
MDPLNLSWYD DDPESRNWSR PFNGSEGKAD RPPYNYYAML LTLLIFVIVF GNVLVCMAVS
REKALQTTTN YLIVSLAVAD LLVATLVMPW VVYLEVVGEW KFSRIHCDIF VTLDVMMCTA
SILNLCAISI DRYTAVAMPM LYNTRYSSKR RVTVMIAIVW VLSFTISCPM LFGLNNTDQN
ECIIANPAFV VYSSIVSFYV PFIVTLLVYI KIYIVLRRRR KRVNTKRSSR AFRANLKAPL
KGNCTHPEDM KLCTVIMKSN GSFPVNRRRV EAARRAQELE MEMLSSTSPP ERTRYSPIPP
SHHQLTLPDP SHHGLHSTPD SPAKPEKNGH AKTVNPKIAK IFEIQSMPNG KTRTSLKTMS
RRKLSQQKEK KATQMLAIVL GVFIICWLPF FITHILNIHC DCNIPPVLYS AFTWLGYVNS
AVNPIIYTTF NIEFRKAFLK ILHC
