DRD1_HUMAN
ID DRD1_HUMAN Reviewed; 446 AA.
AC P21728; B2RA44; Q4QRJ0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=D(1A) dopamine receptor;
DE AltName: Full=Dopamine D1 receptor;
GN Name=DRD1;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=2144334; DOI=10.1038/347072a0;
RA Dearry A., Gingrich J.A., Falardeau P., Fremeau R.T. Jr., Bates M.D.,
RA Caron M.G.;
RT "Molecular cloning and expression of the gene for a human D1 dopamine
RT receptor.";
RL Nature 347:72-76(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2168520; DOI=10.1038/347076a0;
RA Zhou Q.-Y., Grandy D.K., Thambi L., Kushner J.A., van Tol H.H.M., Cone R.,
RA Pribnow D., Salon J., Bunzow J.R., Civelli O.;
RT "Cloning and expression of human and rat D1 dopamine receptors.";
RL Nature 347:76-80(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1975640; DOI=10.1038/347080a0;
RA Sunahara R.K., Niznik H.B., Weiner D.M., Stormann T.M., Brann M.R.,
RA Kennedy J.L., Gelernter J.E., Rozmahel R., Yang Y., Israel Y., Seeman P.,
RA O'Dowd B.F.;
RT "Human dopamine D1 receptor encoded by an intronless gene on chromosome
RT 5.";
RL Nature 347:80-83(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=8471124; DOI=10.1038/npp.1993.14;
RA Ohara K., Ulpian C., Seeman P., Sunahara R.K., van Tol H.H.M., Niznik H.B.;
RT "Schizophrenia: dopamine D1 receptor sequence is normal, but has DNA
RT polymorphisms.";
RL Neuropsychopharmacology 8:131-135(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [10]
RP PALMITOYLATION AT CYS-347 AND CYS-351.
RX PubMed=10618483; DOI=10.1016/s0014-2999(99)00727-x;
RA Jin H., Xie Z., George S.R., O'Dowd B.F.;
RT "Palmitoylation occurs at cysteine 347 and cysteine 351 of the dopamine
RT D(1) receptor.";
RL Eur. J. Pharmacol. 386:305-312(1999).
RN [11]
RP VARIANTS ARG-81 AND TYR-259.
RX PubMed=21179162; DOI=10.1038/nature09629;
RA Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T.,
RA Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A.,
RA Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L.,
RA Virkkunen M., Goldman D.;
RT "A population-specific HTR2B stop codon predisposes to severe
RT impulsivity.";
RL Nature 468:1061-1066(2010).
CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC which activate adenylyl cyclase.
CC -!- SUBUNIT: Interacts with DNAJC14 via its C-terminus (By similarity).
CC Interacts with DRD2 (By similarity). {ECO:0000250|UniProtKB:P18901,
CC ECO:0000250|UniProtKB:Q61616}.
CC -!- INTERACTION:
CC P21728; Q92993: KAT5; NbExp=3; IntAct=EBI-6624459, EBI-399080;
CC P21728; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-6624459, EBI-11742507;
CC P21728; P17252: PRKCA; NbExp=3; IntAct=EBI-6624459, EBI-1383528;
CC P21728; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-6624459, EBI-9090795;
CC P21728; P61981: YWHAG; NbExp=3; IntAct=EBI-6624459, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18901};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P18901}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P18901}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P18901}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q61616}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q61616}. Note=Transport from the endoplasmic
CC reticulum to the cell surface is regulated by interaction with DNAJC14.
CC {ECO:0000250|UniProtKB:P18901}.
CC -!- TISSUE SPECIFICITY: Detected in caudate, nucleus accumbens and in the
CC olfactory tubercle. {ECO:0000269|PubMed:2144334}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X55760; CAA39286.1; -; Genomic_DNA.
DR EMBL; X58987; CAA41734.1; -; mRNA.
DR EMBL; X55758; CAA39284.1; -; Genomic_DNA.
DR EMBL; S58541; AAB26273.1; -; Genomic_DNA.
DR EMBL; AB065677; BAC05902.1; -; Genomic_DNA.
DR EMBL; AF498961; AAM18131.1; -; mRNA.
DR EMBL; AK314031; BAG36741.1; -; mRNA.
DR EMBL; CH471062; EAW61377.1; -; Genomic_DNA.
DR EMBL; BC074978; AAH74978.1; -; mRNA.
DR EMBL; BC074979; AAH74979.1; -; mRNA.
DR EMBL; BC096837; AAH96837.1; -; mRNA.
DR CCDS; CCDS4393.1; -.
DR PIR; S11377; DYHUD1.
DR RefSeq; NP_000785.1; NM_000794.3.
DR PDB; 7CKW; EM; 3.22 A; R=1-446.
DR PDB; 7CKX; EM; 3.54 A; R=1-446.
DR PDB; 7CKY; EM; 3.20 A; R=1-446.
DR PDB; 7CKZ; EM; 3.10 A; R=1-446.
DR PDB; 7CRH; EM; 3.30 A; R=1-446.
DR PDB; 7JOZ; X-ray; 3.80 A; R=21-347.
DR PDB; 7JV5; EM; 3.00 A; R=1-446.
DR PDB; 7JVP; EM; 2.90 A; R=1-446.
DR PDB; 7JVQ; EM; 3.00 A; R=1-446.
DR PDB; 7LJC; EM; 3.00 A; R=1-446.
DR PDB; 7LJD; EM; 3.20 A; R=1-446.
DR PDBsum; 7CKW; -.
DR PDBsum; 7CKX; -.
DR PDBsum; 7CKY; -.
DR PDBsum; 7CKZ; -.
DR PDBsum; 7CRH; -.
DR PDBsum; 7JOZ; -.
DR PDBsum; 7JV5; -.
DR PDBsum; 7JVP; -.
DR PDBsum; 7JVQ; -.
DR PDBsum; 7LJC; -.
DR PDBsum; 7LJD; -.
DR AlphaFoldDB; P21728; -.
DR SMR; P21728; -.
DR BioGRID; 108146; 14.
DR IntAct; P21728; 8.
DR STRING; 9606.ENSP00000377353; -.
DR BindingDB; P21728; -.
DR ChEMBL; CHEMBL2056; -.
DR DrugBank; DB01614; Acepromazine.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB01200; Bromocriptine.
DR DrugBank; DB00248; Cabergoline.
DR DrugBank; DB01038; Carphenazine.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB00568; Cinnarizine.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB12890; Dihydrexidine.
DR DrugBank; DB11274; Dihydro-alpha-ergocryptine.
DR DrugBank; DB13345; Dihydroergocristine.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB11275; Epicriptine.
DR DrugBank; DB01049; Ergoloid mesylate.
DR DrugBank; DB00696; Ergotamine.
DR DrugBank; DB00800; Fenoldopam.
DR DrugBank; DB00875; Flupentixol.
DR DrugBank; DB00623; Fluphenazine.
DR DrugBank; DB00502; Haloperidol.
DR DrugBank; DB04946; Iloperidone.
DR DrugBank; DB00458; Imipramine.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB01235; Levodopa.
DR DrugBank; DB00589; Lisuride.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB06077; Lumateperone.
DR DrugBank; DB01403; Methotrimeprazine.
DR DrugBank; DB00353; Methylergometrine.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB00805; Minaprine.
DR DrugBank; DB08804; Nandrolone decanoate.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB01267; Paliperidone.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB01186; Pergolide.
DR DrugBank; DB01608; Periciazine.
DR DrugBank; DB00850; Perphenazine.
DR DrugBank; DB00397; Phenylpropanolamine.
DR DrugBank; DB09286; Pipamperone.
DR DrugBank; DB01621; Pipotiazine.
DR DrugBank; DB11584; Pipradrol.
DR DrugBank; DB01224; Quetiapine.
DR DrugBank; DB09097; Quinagolide.
DR DrugBank; DB00734; Risperidone.
DR DrugBank; DB05271; Rotigotine.
DR DrugBank; DB12093; Tetrahydropalmatine.
DR DrugBank; DB01622; Thioproperazine.
DR DrugBank; DB00679; Thioridazine.
DR DrugBank; DB01623; Thiothixene.
DR DrugBank; DB00508; Triflupromazine.
DR DrugBank; DB00726; Trimipramine.
DR DrugBank; DB00246; Ziprasidone.
DR DrugBank; DB09225; Zotepine.
DR DrugBank; DB01624; Zuclopenthixol.
DR DrugCentral; P21728; -.
DR GuidetoPHARMACOLOGY; 214; -.
DR GlyGen; P21728; 1 site.
DR iPTMnet; P21728; -.
DR PhosphoSitePlus; P21728; -.
DR SwissPalm; P21728; -.
DR BioMuta; DRD1; -.
DR DMDM; 118228; -.
DR MassIVE; P21728; -.
DR PaxDb; P21728; -.
DR PeptideAtlas; P21728; -.
DR PRIDE; P21728; -.
DR ABCD; P21728; 2 sequenced antibodies.
DR Antibodypedia; 2811; 666 antibodies from 42 providers.
DR DNASU; 1812; -.
DR Ensembl; ENST00000393752.3; ENSP00000377353.1; ENSG00000184845.4.
DR GeneID; 1812; -.
DR KEGG; hsa:1812; -.
DR MANE-Select; ENST00000393752.3; ENSP00000377353.1; NM_000794.5; NP_000785.1.
DR UCSC; uc003mcz.4; human.
DR CTD; 1812; -.
DR DisGeNET; 1812; -.
DR GeneCards; DRD1; -.
DR HGNC; HGNC:3020; DRD1.
DR HPA; ENSG00000184845; Group enriched (brain, retina).
DR MIM; 126449; gene.
DR neXtProt; NX_P21728; -.
DR OpenTargets; ENSG00000184845; -.
DR PharmGKB; PA147; -.
DR VEuPathDB; HostDB:ENSG00000184845; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155857; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; P21728; -.
DR OMA; MDCQQPE; -.
DR OrthoDB; 1045889at2759; -.
DR PhylomeDB; P21728; -.
DR TreeFam; TF325181; -.
DR PathwayCommons; P21728; -.
DR Reactome; R-HSA-390651; Dopamine receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P21728; -.
DR SIGNOR; P21728; -.
DR BioGRID-ORCS; 1812; 9 hits in 1075 CRISPR screens.
DR GeneWiki; Dopamine_receptor_D1; -.
DR GenomeRNAi; 1812; -.
DR Pharos; P21728; Tclin.
DR PRO; PR:P21728; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P21728; protein.
DR Bgee; ENSG00000184845; Expressed in caudate nucleus and 89 other tissues.
DR Genevisible; P21728; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060170; C:ciliary membrane; IDA:SYSCILIA_CCNET.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0097730; C:non-motile cilium; IDA:SYSCILIA_CCNET.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035240; F:dopamine binding; IMP:BHF-UCL.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IDA:MGI.
DR GO; GO:0001588; F:dopamine neurotransmitter receptor activity, coupled via Gs; IDA:BHF-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IDA: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:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007628; P:adult walking behavior; ISS:BHF-UCL.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:UniProt.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; IDA:BHF-UCL.
DR GO; GO:1903351; P:cellular response to dopamine; IMP:CAFA.
DR GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; ISS:BHF-UCL.
DR GO; GO:0001661; P:conditioned taste aversion; IEA:Ensembl.
DR GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl.
DR GO; GO:0042417; P:dopamine metabolic process; IC:BHF-UCL.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0015872; P:dopamine transport; IEA:Ensembl.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IDA:BHF-UCL.
DR GO; GO:0046323; P:glucose import; IEA:Ensembl.
DR GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR GO; GO:0046959; P:habituation; IEA:Ensembl.
DR GO; GO:0043987; P:histone H3-S10 phosphorylation; IEA:Ensembl.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
DR GO; GO:0007617; P:mating behavior; ISS:BHF-UCL.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0035106; P:operant conditioning; IEA:Ensembl.
DR GO; GO:0030432; P:peristalsis; IEA:Ensembl.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
DR GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISS:BHF-UCL.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:0060134; P:prepulse inhibition; ISS:BHF-UCL.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl.
DR GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; IC:BHF-UCL.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:BHF-UCL.
DR GO; GO:0046960; P:sensitization; IEA:Ensembl.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
DR GO; GO:0019226; P:transmission of nerve impulse; ISS:BHF-UCL.
DR GO; GO:0042311; P:vasodilation; IEA:InterPro.
DR GO; GO:0008542; P:visual learning; ISS:BHF-UCL.
DR InterPro; IPR001413; Dopamine_D1_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; PR00565; DOPAMINED1AR.
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; Cell membrane; Cell projection; Disulfide bond;
KW Endoplasmic reticulum; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Synapse;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..446
FT /note="D(1A) dopamine receptor"
FT /id="PRO_0000069373"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..163
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..337
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 347
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10618483"
FT LIPID 351
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10618483"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 37
FT /note="T -> P (in dbSNP:rs5327)"
FT /id="VAR_014670"
FT VARIANT 37
FT /note="T -> R (in dbSNP:rs879844008)"
FT /id="VAR_014671"
FT VARIANT 50
FT /note="R -> S (in dbSNP:rs5330)"
FT /id="VAR_014672"
FT VARIANT 81
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:21179162"
FT /id="VAR_064577"
FT VARIANT 199
FT /note="S -> A (in dbSNP:rs5331)"
FT /id="VAR_014673"
FT VARIANT 259
FT /note="S -> Y (in dbSNP:rs74414188)"
FT /evidence="ECO:0000269|PubMed:21179162"
FT /id="VAR_064578"
FT CONFLICT 438
FT /note="I -> M (in Ref. 2; CAA41734)"
FT /evidence="ECO:0000305"
FT HELIX 21..50
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 95..126
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 137..160
FT /evidence="ECO:0007829|PDB:7JVP"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:7JV5"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 204..238
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 265..298
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 310..331
FT /evidence="ECO:0007829|PDB:7JVP"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:7JVP"
SQ SEQUENCE 446 AA; 49293 MW; 64E062D765D0DBA7 CRC64;
MRTLNTSAMD GTGLVVERDF SVRILTACFL SLLILSTLLG NTLVCAAVIR FRHLRSKVTN
FFVISLAVSD LLVAVLVMPW KAVAEIAGFW PFGSFCNIWV AFDIMCSTAS ILNLCVISVD
RYWAISSPFR YERKMTPKAA FILISVAWTL SVLISFIPVQ LSWHKAKPTS PSDGNATSLA
ETIDNCDSSL SRTYAISSSV ISFYIPVAIM IVTYTRIYRI AQKQIRRIAA LERAAVHAKN
CQTTTGNGKP VECSQPESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI LNCILPFCGS
GETQPFCIDS NTFDVFVWFG WANSSLNPII YAFNADFRKA FSTLLGCYRL CPATNNAIET
VSINNNGAAM FSSHHEPRGS ISKECNLVYL IPHAVGSSED LKKEEAAGIA RPLEKLSPAL
SVILDYDTDV SLEKIQPITQ NGQHPT
