DRD2_RAT
ID DRD2_RAT Reviewed; 444 AA.
AC P61169; P13953;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=D(2) dopamine receptor;
DE AltName: Full=Dopamine D2 receptor;
GN Name=Drd2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Brain;
RX PubMed=2974511; DOI=10.1038/336783a0;
RA Bunzow J.R., van Tol H.H.M., Grandy D.K., Albert P., Salon J., Christie M.,
RA Machida C.A., Neve K.A., Civelli O.;
RT "Cloning and expression of a rat D2 dopamine receptor cDNA.";
RL Nature 336:783-787(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND TISSUE SPECIFICITY.
RX PubMed=2531656;
RA Dal-Toso R., Sommer B., Ewert M., Herb A., Pritchett D.B., Bach A.,
RA Shivers B.D., Seeburg P.H.;
RT "The dopamine D2 receptor: two molecular forms generated by alternative
RT splicing.";
RL EMBO J. 8:4025-4034(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2531846; DOI=10.1038/342865a0;
RA Eidne K.A., Taylor P.L., Zabavnik J., Saunders P.T.K., Inglis J.D.;
RT "D2 receptor, a missing exon.";
RL Nature 342:865-865(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2531847; DOI=10.1038/342923a0;
RA Giros B., Sokoloff P., Martres M.-P., Riou J.-F., Emorine L.J.,
RA Schwartz J.-C.;
RT "Alternative splicing directs the expression of two D2 dopamine receptor
RT isoforms.";
RL Nature 342:923-926(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2480527; DOI=10.1038/342926a0;
RA Monsma F.J. Jr., McVittie L.D., Gerfen C.R., Mahan L.C., Sibley D.R.;
RT "Multiple D2 dopamine receptors produced by alternative RNA splicing.";
RL Nature 342:926-929(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2139615; DOI=10.1016/0014-5793(90)80695-f;
RA Rao D.D., McKelvy J., Kebabian J., MacKenzie R.G.;
RT "Two forms of the rat D2 dopamine receptor as revealed by the polymerase
RT chain reaction.";
RL FEBS Lett. 263:18-22(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC STRAIN=Sprague-Dawley;
RA Taylor P.L., Inglis J.D., Eidne K.A.;
RT "5'untranslated region of rat pituitary dopamine D2(B) receptor contains a
RT putative CpG island.";
RL Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 242-270.
RX PubMed=2137336; DOI=10.1016/0006-291x(90)91917-h;
RA Miller J.C., Wang Y., Filer D.;
RT "Identification by sequence analysis of a second rat brain cDNA encoding
RT the dopamine (D2) receptor.";
RL Biochem. Biophys. Res. Commun. 166:109-112(1990).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 242-270.
RX PubMed=2138567; DOI=10.1016/0014-5793(90)80140-e;
RA O'Dowd B.F., Nguyen T., Tirpak A., Jarvie K.R., Israel Y., Seeman P.,
RA Niznik H.B.;
RT "Cloning of two additional catecholamine receptors from rat brain.";
RL FEBS Lett. 262:8-12(1990).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND TISSUE SPECIFICITY.
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).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF SER-193; SER-194; SER-197 AND SER-420.
RX PubMed=1321233; DOI=10.1111/j.1471-4159.1992.tb09416.x;
RA Cox B.A., Henningsen R.A., Spanoyannis A., Neve R.L., Neve K.A.;
RT "Contributions of conserved serine residues to the interactions of ligands
RT with dopamine D2 receptors.";
RL J. Neurochem. 59:627-635(1992).
RN [12]
RP INTERACTION WITH PPP1R9B.
RX PubMed=10391935; DOI=10.1074/jbc.274.28.19894;
RA Smith F.D., Oxford G.S., Milgram S.L.;
RT "Association of the D2 dopamine receptor third cytoplasmic loop with
RT spinophilin, a protein phosphatase-1-interacting protein.";
RL J. Biol. Chem. 274:19894-19900(1999).
RN [13]
RP INTERACTION WITH CLIC6.
RX PubMed=14499480; DOI=10.1016/s0169-328x(03)00283-3;
RA Griffon N., Jeanneteau F., Prieur F., Diaz J., Sokoloff P.;
RT "CLIC6, a member of the intracellular chloride channel family, interacts
RT with dopamine D(2)-like receptors.";
RL Brain Res. Mol. Brain Res. 117:47-57(2003).
RN [14]
RP INTERACTION WITH GPRASP1.
RX PubMed=16049099; DOI=10.1073/pnas.0502418102;
RA Bartlett S.E., Enquist J., Hopf F.W., Lee J.H., Gladher F., Kharazia V.,
RA Waldhoer M., Mailliard W.S., Armstrong R., Bonci A., Whistler J.L.;
RT "Dopamine responsiveness is regulated by targeted sorting of D2
RT receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11521-11526(2005).
RN [15]
RP INTERACTION WITH ARRB2.
RX PubMed=19332542; DOI=10.1074/jbc.m900388200;
RA Namkung Y., Dipace C., Javitch J.A., Sibley D.R.;
RT "G protein-coupled receptor kinase-mediated phosphorylation regulates post-
RT endocytic trafficking of the D2 dopamine receptor.";
RL J. Biol. Chem. 284:15038-15051(2009).
RN [16]
RP 3D-STRUCTURE MODELING.
RX PubMed=1358063; DOI=10.1042/bj2870277;
RA Livingstone C.D., Strange P.G., Naylor L.H.;
RT "Molecular modelling of D2-like dopamine receptors.";
RL Biochem. J. 287:277-282(1992).
CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC which inhibit adenylyl cyclase (PubMed:1321233). 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:1321233}.
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 (PubMed:10391935,
CC PubMed:14499480, PubMed:16049099). Interacts with ARRB2
CC (PubMed:19332542). Interacts with HTR2A (By similarity). Interacts with
CC DRD1 (By similarity). Interacts with KCNA2 (By similarity).
CC {ECO:0000250|UniProtKB:P14416, ECO:0000250|UniProtKB:P61168}.
CC -!- INTERACTION:
CC P61169; O35274: Ppp1r9b; NbExp=2; IntAct=EBI-80012, EBI-80022;
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; Synonyms=D2A, D2in;
CC IsoId=P61169-1, P13953-1;
CC Sequence=Displayed;
CC Name=Short; Synonyms=D2B, D2o;
CC IsoId=P61169-2, P13953-2;
CC Sequence=VSP_001871;
CC -!- TISSUE SPECIFICITY: [Isoform Long]: Expressed in the anterior lobe of
CC the pituitary gland (PubMed:2531656). Expressed ventral tegmental area
CC of the midbrain and the pars compacta of the substantia nigra
CC (PubMed:2531656). Expressed seven times more than isoform short in the
CC caudate nucleus (PubMed:2137198). {ECO:0000269|PubMed:2137198,
CC ECO:0000269|PubMed:2531656}.
CC -!- TISSUE SPECIFICITY: [Isoform Short]: Expressed in the anterior lobe of
CC the pituitary gland (PubMed:2531656). Expressed in the caudate nucleus
CC (PubMed:2137198). Not expressed in the wider brain (PubMed:2531656).
CC {ECO:0000269|PubMed:2137198, ECO:0000269|PubMed:2531656}.
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; M36831; AAA41075.1; -; mRNA.
DR EMBL; X53278; CAA37373.1; -; mRNA.
DR EMBL; X56065; CAA39543.1; -; mRNA.
DR EMBL; M32241; AAA41074.1; -; mRNA.
DR PIR; S08146; S08146.
DR RefSeq; NP_036679.1; NM_012547.1. [P61169-1]
DR RefSeq; XP_006243041.1; XM_006242979.3. [P61169-2]
DR AlphaFoldDB; P61169; -.
DR SMR; P61169; -.
DR BioGRID; 246498; 11.
DR CORUM; P61169; -.
DR DIP; DIP-30883N; -.
DR IntAct; P61169; 5.
DR MINT; P61169; -.
DR STRING; 10116.ENSRNOP00000043759; -.
DR BindingDB; P61169; -.
DR ChEMBL; CHEMBL339; -.
DR DrugCentral; P61169; -.
DR GuidetoPHARMACOLOGY; 215; -.
DR GlyGen; P61169; 3 sites.
DR iPTMnet; P61169; -.
DR PhosphoSitePlus; P61169; -.
DR ABCD; P61169; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000045944; ENSRNOP00000043759; ENSRNOG00000008428. [P61169-1]
DR Ensembl; ENSRNOT00000083419; ENSRNOP00000074235; ENSRNOG00000008428. [P61169-2]
DR GeneID; 24318; -.
DR KEGG; rno:24318; -.
DR UCSC; RGD:2520; rat.
DR CTD; 1813; -.
DR RGD; 2520; Drd2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155539; -.
DR InParanoid; P61169; -.
DR OMA; APMDPLN; -.
DR OrthoDB; 1021787at2759; -.
DR PhylomeDB; P61169; -.
DR TreeFam; TF334382; -.
DR Reactome; R-RNO-390651; Dopamine receptors.
DR PRO; PR:P61169; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000008428; Expressed in cerebellum and 1 other tissue.
DR Genevisible; P61169; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0060170; C:ciliary membrane; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:RGD.
DR GO; GO:0030139; C:endocytic vesicle; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0036126; C:sperm flagellum; IDA:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0035240; F:dopamine binding; IMP:RGD.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; ISO:RGD.
DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IDA:BHF-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:RGD.
DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0097159; F:organic cyclic compound binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0046717; P:acid secretion; IDA:BHF-UCL.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:RGD.
DR GO; GO:0021984; P:adenohypophysis development; ISO:RGD.
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; IDA:BHF-UCL.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0050482; P:arachidonic acid secretion; ISO:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0031223; P:auditory behavior; IMP:RGD.
DR GO; GO:0006914; P:autophagy; IDA:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0048148; P:behavioral response to cocaine; ISO:RGD.
DR GO; GO:0048149; P:behavioral response to ethanol; ISO:RGD.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; ISO:RGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IC:BHF-UCL.
DR GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; ISO:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISO:RGD.
DR GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IDA:RGD.
DR GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IEA:Ensembl.
DR GO; GO:0042756; P:drinking behavior; IDA:RGD.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0007631; P:feeding behavior; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; IMP:RGD.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007625; P:grooming behavior; ISO:RGD.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; IMP:RGD.
DR GO; GO:0007616; P:long-term memory; IMP:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISO:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0042321; P:negative regulation of circadian sleep/wake cycle, sleep; IDA:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISO:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:RGD.
DR GO; GO:2001223; P:negative regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:RGD.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IDA:RGD.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:BHF-UCL.
DR GO; GO:0001976; P:nervous system process involved in regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; ISO:RGD.
DR GO; GO:0021769; P:orbitofrontal cortex development; IEP:RGD.
DR GO; GO:0030432; P:peristalsis; ISO:RGD.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0043473; P:pigmentation; ISO:RGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:RGD.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:RGD.
DR GO; GO:0051586; P:positive regulation of dopamine uptake involved in synaptic transmission; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:1900168; P:positive regulation of glial cell-derived neurotrophic factor production; ISO:RGD.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; ISO:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; TAS:BHF-UCL.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:RGD.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IDA:RGD.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:RGD.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0035810; P:positive regulation of urine volume; ISO:RGD.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0060134; P:prepulse inhibition; ISO:RGD.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IMP:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; IDA:RGD.
DR GO; GO:0051580; P:regulation of neurotransmitter uptake; ISO:RGD.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IMP:RGD.
DR GO; GO:0043266; P:regulation of potassium ion transport; IDA:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISO:RGD.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; IDA:RGD.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:BHF-UCL.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0034776; P:response to histamine; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IMP:RGD.
DR GO; GO:0014854; P:response to inactivity; IEP:RGD.
DR GO; GO:0010039; P:response to iron ion; IEP:RGD.
DR GO; GO:0009416; P:response to light stimulus; ISO:RGD.
DR GO; GO:0043278; P:response to morphine; ISO:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:BHF-UCL.
DR GO; GO:0007608; P:sensory perception of smell; ISO:RGD.
DR GO; GO:0001964; P:startle response; ISO:RGD.
DR GO; GO:0021756; P:striatum development; IEP:RGD.
DR GO; GO:0007416; P:synapse assembly; IEP:BHF-UCL.
DR GO; GO:0001659; P:temperature homeostasis; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; IDA:RGD.
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 1: Evidence at protein 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_0000069390"
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:0000269|PubMed:10391935"
FT REGION 282..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 194
FT /note="Important for receptor activation"
FT SITE 197
FT /note="Important for receptor activation"
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:2974511"
FT /id="VSP_001871"
FT MUTAGEN 193
FT /note="S->A: Moderate decrease in ligand binding. 200-fold
FT reduction of agonist-mediated cAMP inhibition."
FT /evidence="ECO:0000269|PubMed:1321233"
FT MUTAGEN 194
FT /note="S->A: Small decrease in agonist binding. Complete
FT loss of agonist-mediated cAMP inhibition."
FT /evidence="ECO:0000269|PubMed:1321233"
FT MUTAGEN 197
FT /note="S->A: Small decrease in agonist binding. 18-fold
FT reduction of agonist-mediated cAMP inhibition."
FT /evidence="ECO:0000269|PubMed:1321233"
FT MUTAGEN 420
FT /note="S->A: Moderate decrease in ligand binding."
FT /evidence="ECO:0000269|PubMed:1321233"
FT CONFLICT 99
FT /note="E -> D (in Ref. 6; CAA37373)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="G -> R (in Ref. 6; CAA37373)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="N -> G (in Ref. 6; CAA37373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 50904 MW; 216E56CEE5CA32FB CRC64;
MDPLNLSWYD DDLERQNWSR PFNGSEGKAD RPHYNYYAML LTLLIFIIVF GNVLVCMAVS
REKALQTTTN YLIVSLAVAD LLVATLVMPW VVYLEVVGEW KFSRIHCDIF VTLDVMMCTA
SILNLCAISI DRYTAVAMPM LYNTRYSSKR RVTVMIAIVW VLSFTISCPL LFGLNNTDQN
ECIIANPAFV VYSSIVSFYV PFIVTLLVYI KIYIVLRKRR KRVNTKRSSR AFRANLKTPL
KGNCTHPEDM KLCTVIMKSN GSFPVNRRRM DAARRAQELE MEMLSSTSPP ERTRYSPIPP
SHHQLTLPDP SHHGLHSNPD SPAKPEKNGH AKIVNPRIAK FFEIQTMPNG KTRTSLKTMS
RRKLSQQKEK KATQMLAIVL GVFIICWLPF FITHILNIHC DCNIPPVLYS AFTWLGYVNS
AVNPIIYTTF NIEFRKAFMK ILHC
