DRD3_HUMAN
ID DRD3_HUMAN Reviewed; 400 AA.
AC P35462; A1A4V5; Q4VBM8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=D(3) dopamine receptor {ECO:0000305};
DE AltName: Full=Dopamine D3 receptor;
GN Name=DRD3 {ECO:0000312|HGNC:HGNC:3024};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2129115;
RA Giros B., Martres M.-P., Sokoloff P., Schwartz J.-C.;
RT "Gene cloning of human dopaminergic D3 receptor and identification of its
RT chromosome.";
RL C. R. Acad. Sci. III, Sci. Vie 311:501-508(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT SER-9.
RC TISSUE=Brain;
RX PubMed=8415635; DOI=10.1073/pnas.90.19.8942;
RA Schmauss C., Haroutunian V., Davis K.L., Davidson M.;
RT "Selective loss of dopamine D3-type receptor mRNA expression in parietal
RT and motor cortices of patients with chronic schizophrenia.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8942-8946(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=7961889; DOI=10.1016/s0021-9258(19)62033-8;
RA Liu K., Bergson C., Levenson R., Schmauss C.;
RT "On the origin of mRNA encoding the truncated dopamine D3-type receptor
RT D3nf and detection of D3nf-like immunoreactivity in human brain.";
RL J. Biol. Chem. 269:29220-29226(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-9.
RA Fishburn C.S., Park B.-H., Fuchs S.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-9.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-9.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INVOLVEMENT IN SCZD, AND VARIANT SER-9.
RX PubMed=1362221; DOI=10.1136/jmg.29.12.858;
RA Crocq M.A., Mant R., Asherson P., Williams J., Hode Y., Mayerova A.,
RA Collier D., Lannfelt L., Sokoloff P., Schwartz J.C.;
RT "Association between schizophrenia and homozygosity at the dopamine D3
RT receptor gene.";
RL J. Med. Genet. 29:858-860(1992).
RN [9]
RP INVOLVEMENT IN SCZD, AND VARIANT SER-9.
RX PubMed=9514583;
RX DOI=10.1002/(sici)1096-8628(19980207)81:1<24::aid-ajmg5>3.0.co;2-n;
RA Spurlock G., Williams J., McGuffin P., Aschauer H.N., Lenzinger E.,
RA Fuchs K., Sieghart W.C., Meszaros K., Fathi N., Laurent C., Mallet J.,
RA Macciardi F., Pedrini S., Gill M., Hawi Z., Gibson S., Jazin E.E.,
RA Yang H.T., Adolfsson R., Pato C.N., Dourado A.M., Owen M.J.;
RT "European multicentre association study of schizophrenia: a study of the
RT DRD2 Ser311Cys and DRD3 Ser9Gly polymorphisms.";
RL Am. J. Med. Genet. 81:24-28(1998).
RN [10]
RP INTERACTION WITH PALM.
RX PubMed=16386234; DOI=10.1016/j.abb.2005.10.027;
RA Basile M., Lin R., Kabbani N., Karpa K., Kilimann M., Simpson I.,
RA Kester M.;
RT "Paralemmin interacts with D3 dopamine receptors: implications for membrane
RT localization and cAMP signaling.";
RL Arch. Biochem. Biophys. 446:60-68(2006).
RN [11]
RP PHOSPHORYLATION BY GRK4, SUBCELLULAR LOCATION, INTERACTION WITH GRK4, AND
RP FUNCTION.
RX PubMed=19520868; DOI=10.1074/jbc.m109.003665;
RA Villar V.A.M., Jones J.E., Armando I., Palmes-Saloma C., Yu P.,
RA Pascua A.M., Keever L., Arnaldo F.B., Wang Z., Luo Y., Felder R.A.,
RA Jose P.A.;
RT "G protein-coupled receptor kinase 4 (GRK4) regulates the phosphorylation
RT and function of the dopamine D3 receptor.";
RL J. Biol. Chem. 284:21425-21434(2009).
RN [12]
RP INTERACTION WITH FLNA.
RX PubMed=26460884; DOI=10.1021/acs.biochem.5b00975;
RA Tirupula K.C., Ithychanda S.S., Mohan M.L., Naga Prasad S.V., Qin J.,
RA Karnik S.S.;
RT "G Protein-Coupled Receptors Directly Bind Filamin A with High Affinity and
RT Promote Filamin Phosphorylation.";
RL Biochemistry 54:6673-6683(2015).
RN [13]
RP PALMITOYLATION.
RX PubMed=27659709; DOI=10.1016/j.bbrc.2016.09.094;
RA Zhang X., Kim K.M.;
RT "Palmitoylation of the carboxyl-terminal tail of dopamine D4 receptor is
RT required for surface expression, endocytosis, and signaling.";
RL Biochem. Biophys. Res. Commun. 479:398-403(2016).
RN [14] {ECO:0007744|PDB:3PBL}
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 2-221 AND 319-400 IN COMPLEX WITH
RP THE ANTAGONIST ETICLOPRIDE, DISULFIDE BONDS, AND MEMBRANE TOPOLOGY.
RX PubMed=21097933; DOI=10.1126/science.1197410;
RA Chien E.Y., Liu W., Zhao Q., Katritch V., Han G.W., Hanson M.A., Shi L.,
RA Newman A.H., Javitch J.A., Cherezov V., Stevens R.C.;
RT "Structure of the human dopamine D3 receptor in complex with a D2/D3
RT selective antagonist.";
RL Science 330:1091-1095(2010).
RN [15]
RP VARIANT SER-9.
RA Lannfelt T., Sokoloff P., Martres M.-P., Pilon C., Giros B., Joensson E.,
RA Sedvall G., Schwartz J.-C.;
RT "Amino-acid substitution in the dopamine D3 receptor as useful polymorphism
RT for investigating psychiatric disorders.";
RL Psychiatr. Genet. 2:249-256(1992).
RN [16]
RP VARIANT SER-9.
RX PubMed=9034004;
RX DOI=10.1002/(sici)1096-8628(19970221)74:1<40::aid-ajmg9>3.0.co;2-z;
RA Chen C.-H., Liu M.-Y., Wei F.-C., Koong F.-J., Hwu H.-G., Hsiao K.-J.;
RT "Further evidence of no association between Ser9Gly polymorphism of
RT dopamine D3 receptor gene and schizophrenia.";
RL Am. J. Med. Genet. 74:40-43(1997).
RN [17]
RP VARIANT SER-9.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [18]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
RN [19]
RP VARIANT SER-9, AND INVOLVEMENT IN SUSCEPTIBILITY TO ETM1.
RX PubMed=16650084; DOI=10.1111/j.1399-0004.2006.00600.x;
RA Lucotte G., Lagarde J.-P., Funalot B., Sokoloff P.;
RT "Linkage with the Ser9Gly DRD3 polymorphism in essential tremor families.";
RL Clin. Genet. 69:437-440(2006).
RN [20]
RP VARIANT SER-9, AND INVOLVEMENT IN SUSCEPTIBILITY TO ETM1.
RX PubMed=16809426; DOI=10.1073/pnas.0508189103;
RA Jeanneteau F., Funalot B., Jankovic J., Deng H., Lagarde J.-P., Lucotte G.,
RA Sokoloff P.;
RT "A functional variant of the dopamine D3 receptor is associated with risk
RT and age-at-onset of essential tremor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10753-10758(2006).
CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC which inhibit adenylyl cyclase. Promotes cell proliferation.
CC {ECO:0000269|PubMed:19520868}.
CC -!- SUBUNIT: Interacts with CLIC6 (By similarity). Interacts with GRK4
CC (PubMed:19520868). Interacts with PALM (PubMed:16386234). Interacts
CC with FLNA (via filamin repeat 21); increases PKA-mediated
CC phosphorylation of FLNA (PubMed:26460884).
CC {ECO:0000250|UniProtKB:P19020, ECO:0000269|PubMed:16386234,
CC ECO:0000269|PubMed:19520868, ECO:0000269|PubMed:26460884}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19520868};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19520868}. Note=Both
CC membrane-bound and scattered in the cytoplasm during basal conditions.
CC Receptor stimulation results in the rapid internalization and
CC sequestration of the receptors at the perinuclear area (5 and 15
CC minutes), followed by the dispersal of the receptors to the membrane
CC (30 minutes). DRD3 and GRK4 co-localize in lipid rafts of renal
CC proximal tubule cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=D3;
CC IsoId=P35462-1; Sequence=Displayed;
CC Name=3;
CC IsoId=P35462-3; Sequence=VSP_040570;
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- PTM: Phosphorylated by GRK4 (GRK4-alpha and GRK4-gamma).
CC {ECO:0000269|PubMed:19520868}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:27659709}.
CC -!- DISEASE: Tremor, hereditary essential 1 (ETM1) [MIM:190300]: A common
CC movement disorder mainly characterized by postural tremor of the arms.
CC Head, legs, trunk, voice, jaw, and facial muscles also may be involved.
CC The condition can be aggravated by emotions, hunger, fatigue and
CC temperature extremes, and may cause a functional disability or even
CC incapacitation. Inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:16650084, ECO:0000269|PubMed:16809426}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry. Glycine at position 9 results in gain
CC of function and is associated with susceptibility to essential tremor.
CC {ECO:0000269|PubMed:16650084, ECO:0000269|PubMed:16809426}.
CC -!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial
CC psychotic disorder or group of disorders characterized by disturbances
CC in the form and content of thought (e.g. delusions, hallucinations), in
CC mood (e.g. inappropriate affect), in sense of self and relationship to
CC the external world (e.g. loss of ego boundaries, withdrawal), and in
CC behavior (e.g bizarre or apparently purposeless behavior). Although it
CC affects emotions, it is distinguished from mood disorders in which such
CC disturbances are primary. Similarly, there may be mild impairment of
CC cognitive function, and it is distinguished from the dementias in which
CC disturbed cognitive function is considered primary. Some patients
CC manifest schizophrenic as well as bipolar disorder symptoms and are
CC often given the diagnosis of schizoaffective disorder.
CC {ECO:0000269|PubMed:1362221, ECO:0000269|PubMed:9514583}. Note=Disease
CC susceptibility may be associated with variants affecting the gene
CC represented in this entry. Glycine at position 9 results in gain of
CC function and may be a risk factor for schizophrenia.
CC {ECO:0000269|PubMed:1362221, ECO:0000269|PubMed:9514583}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA03543.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA64369.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=C&genename=DRD3";
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DR EMBL; L20469; AAA03543.1; ALT_FRAME; mRNA.
DR EMBL; AH003061; AAA64369.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U32499; AAA73929.1; -; mRNA.
DR EMBL; AC092896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79610.1; -; Genomic_DNA.
DR EMBL; BC095510; AAH95510.1; -; mRNA.
DR EMBL; BC128123; AAI28124.1; -; mRNA.
DR CCDS; CCDS2978.1; -. [P35462-1]
DR CCDS; CCDS33829.1; -. [P35462-3]
DR PIR; A48258; A48258.
DR PIR; A55419; A55419.
DR PIR; G01977; G01977.
DR RefSeq; NP_000787.2; NM_000796.5.
DR RefSeq; NP_001269492.1; NM_001282563.2.
DR RefSeq; NP_001277738.1; NM_001290809.1.
DR RefSeq; NP_387512.3; NM_033663.5.
DR PDB; 3PBL; X-ray; 2.89 A; A/B=2-221, A/B=319-400.
DR PDB; 7CMU; EM; 3.00 A; R=1-400.
DR PDB; 7CMV; EM; 2.70 A; R=1-400.
DR PDBsum; 3PBL; -.
DR PDBsum; 7CMU; -.
DR PDBsum; 7CMV; -.
DR AlphaFoldDB; P35462; -.
DR SMR; P35462; -.
DR BioGRID; 108148; 29.
DR DIP; DIP-5976N; -.
DR IntAct; P35462; 6.
DR STRING; 9606.ENSP00000373169; -.
DR BindingDB; P35462; -.
DR ChEMBL; CHEMBL234; -.
DR DrugBank; DB05766; ACP-104.
DR DrugBank; DB06288; Amisulpride.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB09207; AS-8112.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB09223; Blonanserin.
DR DrugBank; DB01200; Bromocriptine.
DR DrugBank; DB00490; Buspirone.
DR DrugBank; DB00248; Cabergoline.
DR DrugBank; DB09014; Captodiame.
DR DrugBank; DB06016; Cariprazine.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB11274; Dihydro-alpha-ergocryptine.
DR DrugBank; DB13345; Dihydroergocristine.
DR DrugBank; DB00320; Dihydroergotamine.
DR DrugBank; DB01184; Domperidone.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB11275; Epicriptine.
DR DrugBank; DB01049; Ergoloid mesylate.
DR DrugBank; DB00875; Flupentixol.
DR DrugBank; DB00502; Haloperidol.
DR DrugBank; DB04946; Iloperidone.
DR DrugBank; DB01235; Levodopa.
DR DrugBank; DB00589; Lisuride.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB01403; Methotrimeprazine.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB08804; Nandrolone decanoate.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB01267; Paliperidone.
DR DrugBank; DB12061; Pardoprunox.
DR DrugBank; DB01186; Pergolide.
DR DrugBank; DB01100; Pimozide.
DR DrugBank; DB09286; Pipamperone.
DR DrugBank; DB12478; Piribedil.
DR DrugBank; DB00413; Pramipexole.
DR DrugBank; DB01224; Quetiapine.
DR DrugBank; DB00409; Remoxipride.
DR DrugBank; DB00268; Ropinirole.
DR DrugBank; DB05271; Rotigotine.
DR DrugBank; DB06454; Sarizotan.
DR DrugBank; DB00391; Sulpiride.
DR DrugBank; DB06477; Sumanirole.
DR DrugBank; DB09289; Tianeptine.
DR DrugBank; DB13025; Tiapride.
DR DrugBank; DB01392; Yohimbine.
DR DrugBank; DB00246; Ziprasidone.
DR DrugCentral; P35462; -.
DR GuidetoPHARMACOLOGY; 216; -.
DR TCDB; 9.A.14.3.9; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P35462; 4 sites.
DR iPTMnet; P35462; -.
DR PhosphoSitePlus; P35462; -.
DR SwissPalm; P35462; -.
DR BioMuta; DRD3; -.
DR DMDM; 1169206; -.
DR PaxDb; P35462; -.
DR PeptideAtlas; P35462; -.
DR PRIDE; P35462; -.
DR ABCD; P35462; 1 sequenced antibody.
DR Antibodypedia; 16482; 284 antibodies from 38 providers.
DR DNASU; 1814; -.
DR Ensembl; ENST00000295881.9; ENSP00000295881.6; ENSG00000151577.13. [P35462-3]
DR Ensembl; ENST00000383673.5; ENSP00000373169.2; ENSG00000151577.13. [P35462-1]
DR Ensembl; ENST00000460779.5; ENSP00000419402.1; ENSG00000151577.13. [P35462-1]
DR Ensembl; ENST00000467632.5; ENSP00000420662.1; ENSG00000151577.13. [P35462-1]
DR GeneID; 1814; -.
DR KEGG; hsa:1814; -.
DR MANE-Select; ENST00000383673.5; ENSP00000373169.2; NM_000796.6; NP_000787.2.
DR CTD; 1814; -.
DR DisGeNET; 1814; -.
DR GeneCards; DRD3; -.
DR HGNC; HGNC:3024; DRD3.
DR HPA; ENSG00000151577; Tissue enriched (brain).
DR MalaCards; DRD3; -.
DR MIM; 126451; gene.
DR MIM; 181500; phenotype.
DR MIM; 190300; phenotype.
DR neXtProt; NX_P35462; -.
DR OpenTargets; ENSG00000151577; -.
DR Orphanet; 862; NON RARE IN EUROPE: Hereditary essential tremor.
DR PharmGKB; PA27479; -.
DR VEuPathDB; HostDB:ENSG00000151577; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000159661; -.
DR InParanoid; P35462; -.
DR PhylomeDB; P35462; -.
DR TreeFam; TF334382; -.
DR PathwayCommons; P35462; -.
DR Reactome; R-HSA-390651; Dopamine receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P35462; -.
DR SIGNOR; P35462; -.
DR BioGRID-ORCS; 1814; 7 hits in 1068 CRISPR screens.
DR GenomeRNAi; 1814; -.
DR Pharos; P35462; Tclin.
DR PRO; PR:P35462; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P35462; protein.
DR Bgee; ENSG00000151577; Expressed in nucleus accumbens and 13 other tissues.
DR ExpressionAtlas; P35462; baseline and differential.
DR Genevisible; P35462; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0046717; P:acid secretion; ISS:BHF-UCL.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050482; P:arachidonic acid secretion; IDA:BHF-UCL.
DR GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR GO; GO:0048148; P:behavioral response to cocaine; IEP:BHF-UCL.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:BHF-UCL.
DR GO; GO:0042417; P:dopamine metabolic process; IC:BHF-UCL.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IDA:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035483; P:gastric emptying; IEA:Ensembl.
DR GO; GO:0007612; P:learning; NAS:BHF-UCL.
DR GO; GO:0007611; P:learning or memory; NAS:BHF-UCL.
DR GO; GO:0007626; P:locomotory behavior; ISS:BHF-UCL.
DR GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; ISS:BHF-UCL.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISS:BHF-UCL.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:BHF-UCL.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:BHF-UCL.
DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:BHF-UCL.
DR GO; GO:0032416; P:negative regulation of sodium:proton antiporter activity; IEA:Ensembl.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
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:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
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:0060161; P:positive regulation of dopamine receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:BHF-UCL.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060134; P:prepulse inhibition; IMP:BHF-UCL.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IEA:Ensembl.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISS:BHF-UCL.
DR GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; IC:BHF-UCL.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IEA:Ensembl.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR GO; GO:0043266; P:regulation of potassium ion transport; IBA:GO_Central.
DR GO; GO:0042220; P:response to cocaine; IEP:BHF-UCL.
DR GO; GO:0034776; P:response to histamine; IDA:BHF-UCL.
DR GO; GO:0043278; P:response to morphine; ISS:BHF-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:BHF-UCL.
DR GO; GO:0035176; P:social behavior; NAS:BHF-UCL.
DR GO; GO:0008542; P:visual learning; ISS:BHF-UCL.
DR InterPro; IPR001620; Dopamine_D3_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; PR00568; DOPAMINED3R.
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 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Schizophrenia; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..400
FT /note="D(3) dopamine receptor"
FT /id="PRO_0000069397"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TRANSMEM 33..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TOPO_DOM 56..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TRANSMEM 66..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TOPO_DOM 89..104
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TOPO_DOM 127..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TOPO_DOM 171..187
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TRANSMEM 188..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TOPO_DOM 210..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TRANSMEM 330..351
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TOPO_DOM 352..366
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TRANSMEM 367..386
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:21097933"
FT TOPO_DOM 387..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21097933"
FT BINDING 110
FT /ligand="eticlopride"
FT /ligand_id="ChEBI:CHEBI:188152"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:21097933,
FT ECO:0007744|PDB:3PBL"
FT BINDING 345
FT /ligand="eticlopride"
FT /ligand_id="ChEBI:CHEBI:188152"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:21097933,
FT ECO:0007744|PDB:3PBL"
FT BINDING 349
FT /ligand="eticlopride"
FT /ligand_id="ChEBI:CHEBI:188152"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:21097933,
FT ECO:0007744|PDB:3PBL"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:21097933, ECO:0007744|PDB:3PBL"
FT DISULFID 355..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:21097933, ECO:0007744|PDB:3PBL"
FT VAR_SEQ 287..320
FT /note="SPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGV -> M (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:8415635"
FT /id="VSP_040570"
FT VARIANT 9
FT /note="G -> S (in dbSNP:rs6280)"
FT /evidence="ECO:0000269|PubMed:10391209,
FT ECO:0000269|PubMed:1362221, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16650084, ECO:0000269|PubMed:16809426,
FT ECO:0000269|PubMed:9034004, ECO:0000269|PubMed:9514583,
FT ECO:0000269|Ref.15"
FT /id="VAR_003463"
FT CONFLICT 396
FT /note="K -> L (in Ref. 7; AAH95510)"
FT /evidence="ECO:0000305"
FT HELIX 34..56
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:7CMU"
FT HELIX 63..81
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 100..133
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 144..169
FT /evidence="ECO:0007829|PDB:7CMV"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:3PBL"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 198..222
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 322..354
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 362..384
FT /evidence="ECO:0007829|PDB:7CMV"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:7CMV"
SQ SEQUENCE 400 AA; 44195 MW; 3E8426597D6C164D CRC64;
MASLSQLSGH LNYTCGAENS TGASQARPHA YYALSYCALI LAIVFGNGLV CMAVLKERAL
QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR ICCDVFVTLD VMMCTASILN
LCAISIDRYT AVVMPVHYQH GTGQSSCRRV ALMITAVWVL AFAVSCPLLF GFNTTGDPTV
CSISNPDFVI YSSVVSFYLP FGVTVLVYAR IYVVLKQRRR KRILTRQNSQ CNSVRPGFPQ
QTLSPDPAHL ELKRYYSICQ DTALGGPGFQ ERGGELKREE KTRNSLSPTI APKLSLEVRK
LSNGRLSTSL KLGPLQPRGV PLREKKATQM VAIVLGAFIV CWLPFFLTHV LNTHCQTCHV
SPELYSATTW LGYVNSALNP VIYTTFNIEF RKAFLKILSC
