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 27-MAR-2024, entry version 215. 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 may also 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. [P35462-1] DR RefSeq; NP_001269492.1; NM_001282563.2. [P35462-1] DR RefSeq; NP_001277738.1; NM_001290809.1. [P35462-1] DR RefSeq; NP_387512.3; NM_033663.5. [P35462-3] DR RefSeq; XP_016861318.1; XM_017005829.1. 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 PDB; 8IRT; EM; 2.70 A; R=1-400. DR PDBsum; 3PBL; -. DR PDBsum; 7CMU; -. DR PDBsum; 7CMV; -. DR PDBsum; 8IRT; -. DR AlphaFoldDB; P35462; -. DR EMDB; EMD-30410; -. DR EMDB; EMD-30411; -. DR EMDB; EMD-35685; -. DR SMR; P35462; -. DR BioGRID; 108148; 30. DR DIP; DIP-5976N; -. DR IntAct; P35462; 8. DR MINT; P35462; -. DR STRING; 9606.ENSP00000373169; -. DR BindingDB; P35462; -. DR ChEMBL; CHEMBL234; -. 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; DB05766; Norclozapine. 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 GlyCosmos; P35462; 4 sites, No reported glycans. DR GlyGen; P35462; 4 sites. DR iPTMnet; P35462; -. DR PhosphoSitePlus; P35462; -. DR SwissPalm; P35462; -. DR BioMuta; DRD3; -. DR DMDM; 1169206; -. DR PaxDb; 9606-ENSP00000373169; -. DR PeptideAtlas; P35462; -. DR ABCD; P35462; 1 sequenced antibody. DR Antibodypedia; 16482; 336 antibodies from 38 providers. DR DNASU; 1814; -. DR Ensembl; ENST00000295881.9; ENSP00000295881.6; ENSG00000151577.14. [P35462-3] DR Ensembl; ENST00000383673.5; ENSP00000373169.2; ENSG00000151577.14. [P35462-1] DR Ensembl; ENST00000460779.5; ENSP00000419402.1; ENSG00000151577.14. [P35462-1] DR Ensembl; ENST00000467632.5; ENSP00000420662.1; ENSG00000151577.14. [P35462-1] DR GeneID; 1814; -. DR KEGG; hsa:1814; -. DR MANE-Select; ENST00000383673.5; ENSP00000373169.2; NM_000796.6; NP_000787.2. DR AGR; HGNC:3024; -. 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 OMA; QINSTCG; -. DR OrthoDB; 2999405at2759; -. 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 1154 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 male germ line stem cell (sensu Vertebrata) in testis and 14 other cell types or tissues. DR ExpressionAtlas; P35462; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:GOC. 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: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:0048148; P:behavioral response to cocaine; IEP: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:0006874; P:intracellular calcium ion homeostasis; IDA:BHF-UCL. 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: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 phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:BHF-UCL. DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:BHF-UCL. DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IBA:GO_Central. DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB. 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:0060134; P:prepulse inhibition; IMP:BHF-UCL. 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: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 CDD; cd15310; 7tmA_D3_dopamine_R; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR001620; Dopamine_D3_rcpt. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR24248:SF154; D(3) DOPAMINE RECEPTOR; 1. 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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P35462; HS. 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:8IRT" 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:8IRT" 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 //