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P21728 (DRD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D(1A) dopamine receptor
Alternative name(s):
Dopamine D1 receptor
Gene names
Name:DRD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.

Subunit structure

Interacts with DNAJC14 via its C-terminus By similarity. Interacts with DRD1IP.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Transport from the endoplasmic reticulum to the cell surface is regulated by interaction with DNAJC14 By similarity.

Tissue specificity

Detected in caudate, nucleus accumbens and in the olfactory tubercle. Ref.1

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger

Inferred from direct assay PubMed 1282671. Source: BHF-UCL

activation of adenylate cyclase activity

Inferred from direct assay Ref.2. Source: BHF-UCL

adenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 11500503. Source: UniProtKB

adenylate cyclase-activating dopamine receptor signaling pathway

Inferred from direct assay PubMed 18403039Ref.1Ref.2. Source: BHF-UCL

adult walking behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

astrocyte development

Inferred from electronic annotation. Source: Ensembl

behavioral fear response

Inferred from electronic annotation. Source: Ensembl

behavioral response to cocaine

Inferred from electronic annotation. Source: Ensembl

cellular response to catecholamine stimulus

Inferred from direct assay PubMed 18403039. Source: BHF-UCL

cerebral cortex GABAergic interneuron migration

Inferred from sequence or structural similarity. Source: BHF-UCL

conditioned taste aversion

Inferred from electronic annotation. Source: Ensembl

dentate gyrus development

Inferred from electronic annotation. Source: Ensembl

dopamine metabolic process

Inferred by curator PubMed 8301582. Source: BHF-UCL

dopamine transport

Inferred from electronic annotation. Source: Ensembl

glucose import

Inferred from electronic annotation. Source: Ensembl

grooming behavior

Inferred from electronic annotation. Source: Ensembl

habituation

Inferred from electronic annotation. Source: Ensembl

long term synaptic depression

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

maternal behavior

Inferred from electronic annotation. Source: Ensembl

mating behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

memory

Inferred from electronic annotation. Source: Ensembl

neuronal action potential

Inferred from electronic annotation. Source: Ensembl

operant conditioning

Inferred from electronic annotation. Source: Ensembl

peristalsis

Inferred from electronic annotation. Source: Ensembl

phospholipase C-activating dopamine receptor signaling pathway

Inferred from direct assay PubMed 1282671. Source: BHF-UCL

positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

positive regulation of cAMP biosynthetic process

Inferred from direct assay PubMed 1282671PubMed 7838121. Source: BHF-UCL

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from direct assay PubMed 1282671. Source: BHF-UCL

positive regulation of potassium ion transport

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 1282671PubMed 7838121. Source: BHF-UCL

positive regulation of synaptic transmission, glutamatergic

Inferred from sequence or structural similarity. Source: BHF-UCL

prepulse inhibition

Inferred from sequence or structural similarity. Source: BHF-UCL

protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of dopamine uptake involved in synaptic transmission

Inferred by curator PubMed 8301582. Source: BHF-UCL

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from sequence or structural similarity. Source: BHF-UCL

sensitization

Inferred from electronic annotation. Source: Ensembl

striatum development

Inferred from electronic annotation. Source: Ensembl

synapse assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

synaptic transmission, dopaminergic

Inferred from electronic annotation. Source: Ensembl

temperature homeostasis

Inferred from electronic annotation. Source: Ensembl

transmission of nerve impulse

Inferred from sequence or structural similarity. Source: BHF-UCL

vasodilation

Inferred from electronic annotation. Source: InterPro

visual learning

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred by curator Ref.1. Source: BHF-UCL

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 11500503. Source: UniProtKB

   Molecular_functiondopamine binding

Inferred from mutant phenotype PubMed 1282671. Source: BHF-UCL

dopamine neurotransmitter receptor activity

Inferred from direct assay PubMed 1831904. Source: MGI

dopamine neurotransmitter receptor activity, coupled via Gs

Inferred from direct assay Ref.1Ref.2. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 15569306. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446D(1A) dopamine receptor
PRO_0000069373

Regions

Topological domain1 – 2323Extracellular Potential
Transmembrane24 – 4926Helical; Name=1; Potential
Topological domain50 – 6011Cytoplasmic Potential
Transmembrane61 – 8727Helical; Name=2; Potential
Topological domain88 – 969Extracellular Potential
Transmembrane97 – 11923Helical; Name=3; Potential
Topological domain120 – 13819Cytoplasmic Potential
Transmembrane139 – 16325Helical; Name=4; Potential
Topological domain164 – 19229Extracellular Potential
Transmembrane193 – 21826Helical; Name=5; Potential
Topological domain219 – 27254Cytoplasmic Potential
Transmembrane273 – 29927Helical; Name=6; Potential
Topological domain300 – 31213Extracellular Potential
Transmembrane313 – 33725Helical; Name=7; Potential
Topological domain338 – 446109Cytoplasmic Potential

Amino acid modifications

Lipidation3471S-palmitoyl cysteine Ref.10
Lipidation3511S-palmitoyl cysteine Ref.10
Glycosylation51N-linked (GlcNAc...) Potential
Disulfide bond96 ↔ 186 By similarity

Natural variations

Natural variant371T → P.
Corresponds to variant rs5327 [ dbSNP | Ensembl ].
VAR_014670
Natural variant371T → R.
Corresponds to variant rs5328 [ dbSNP | Ensembl ].
VAR_014671
Natural variant501R → S.
Corresponds to variant rs5330 [ dbSNP | Ensembl ].
VAR_014672
Natural variant811K → R. Ref.11
VAR_064577
Natural variant1991S → A.
Corresponds to variant rs5331 [ dbSNP | Ensembl ].
VAR_014673
Natural variant2591S → Y. Ref.11
Corresponds to variant rs74414188 [ dbSNP | Ensembl ].
VAR_064578

Experimental info

Sequence conflict4381I → M in CAA41734. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P21728 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 64E062D765D0DBA7

FASTA44649,293
        10         20         30         40         50         60 
MRTLNTSAMD GTGLVVERDF SVRILTACFL SLLILSTLLG NTLVCAAVIR FRHLRSKVTN 

        70         80         90        100        110        120 
FFVISLAVSD LLVAVLVMPW KAVAEIAGFW PFGSFCNIWV AFDIMCSTAS ILNLCVISVD 

       130        140        150        160        170        180 
RYWAISSPFR YERKMTPKAA FILISVAWTL SVLISFIPVQ LSWHKAKPTS PSDGNATSLA 

       190        200        210        220        230        240 
ETIDNCDSSL SRTYAISSSV ISFYIPVAIM IVTYTRIYRI AQKQIRRIAA LERAAVHAKN 

       250        260        270        280        290        300 
CQTTTGNGKP VECSQPESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI LNCILPFCGS 

       310        320        330        340        350        360 
GETQPFCIDS NTFDVFVWFG WANSSLNPII YAFNADFRKA FSTLLGCYRL CPATNNAIET 

       370        380        390        400        410        420 
VSINNNGAAM FSSHHEPRGS ISKECNLVYL IPHAVGSSED LKKEEAAGIA RPLEKLSPAL 

       430        440 
SVILDYDTDV SLEKIQPITQ NGQHPT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of the gene for a human D1 dopamine receptor."
Dearry A., Gingrich J.A., Falardeau P., Fremeau R.T. Jr., Bates M.D., Caron M.G.
Nature 347:72-76(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[2]"Cloning and expression of human and rat D1 dopamine receptors."
Zhou Q.-Y., Grandy D.K., Thambi L., Kushner J.A., van Tol H.H.M., Cone R., Pribnow D., Salon J., Bunzow J.R., Civelli O.
Nature 347:76-80(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Human dopamine D1 receptor encoded by an intronless gene on chromosome 5."
Sunahara R.K., Niznik H.B., Weiner D.M., Stormann T.M., Brann M.R., Kennedy J.L., Gelernter J.E., Rozmahel R., Yang Y., Israel Y., Seeman P., O'Dowd B.F.
Nature 347:80-83(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Schizophrenia: dopamine D1 receptor sequence is normal, but has DNA polymorphisms."
Ohara K., Ulpian C., Seeman P., Sunahara R.K., van Tol H.H.M., Niznik H.B.
Neuropsychopharmacology 8:131-135(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain.
[5]"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]"Palmitoylation occurs at cysteine 347 and cysteine 351 of the dopamine D(1) receptor."
Jin H., Xie Z., George S.R., O'Dowd B.F.
Eur. J. Pharmacol. 386:305-312(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-347 AND CYS-351.
[11]"A population-specific HTR2B stop codon predisposes to severe impulsivity."
Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L., Virkkunen M., Goldman D.
Nature 468:1061-1066(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-81 AND TYR-259.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55760 Genomic DNA. Translation: CAA39286.1.
X58987 mRNA. Translation: CAA41734.1.
X55758 Genomic DNA. Translation: CAA39284.1.
S58541 Genomic DNA. Translation: AAB26273.1.
AB065677 Genomic DNA. Translation: BAC05902.1.
AF498961 mRNA. Translation: AAM18131.1.
AK314031 mRNA. Translation: BAG36741.1.
CH471062 Genomic DNA. Translation: EAW61377.1.
BC074978 mRNA. Translation: AAH74978.1.
BC074979 mRNA. Translation: AAH74979.1.
BC096837 mRNA. Translation: AAH96837.1.
CCDSCCDS4393.1.
PIRDYHUD1. S11377.
RefSeqNP_000785.1. NM_000794.3.
UniGeneHs.2624.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OZ5model-A1-446[»]
ProteinModelPortalP21728.
SMRP21728. Positions 29-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108146. 6 interactions.
MINTMINT-123019.
STRING9606.ENSP00000327652.

Chemistry

BindingDBP21728.
ChEMBLCHEMBL2111341.
DrugBankDB01063. Acetophenazine.
DB00915. Amantadine.
DB00714. Apomorphine.
DB01038. Carphenazine.
DB01239. Chlorprothixene.
DB00363. Clozapine.
DB00907. Cocaine.
DB00988. Dopamine.
DB00800. Fenoldopam.
DB00875. Flupenthixol.
DB00623. Fluphenazine.
DB00502. Haloperidol.
DB01235. Levodopa.
DB00589. Lisuride.
DB00408. Loxapine.
DB00353. Methylergonovine.
DB00805. Minaprine.
DB00334. Olanzapine.
DB00061. Pegademase bovine.
DB01186. Pergolide.
DB00850. Perphenazine.
DB00433. Prochlorperazine.
DB00420. Promazine.
DB00777. Propiomazine.
DB01224. Quetiapine.
DB00372. Thiethylperazine.
DB00679. Thioridazine.
DB00508. Triflupromazine.
DB01624. Zuclopenthixol.
GuidetoPHARMACOLOGY214.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP21728.

Polymorphism databases

DMDM118228.

Proteomic databases

PaxDbP21728.
PRIDEP21728.

Protocols and materials databases

DNASU1812.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393752; ENSP00000377353; ENSG00000184845.
GeneID1812.
KEGGhsa:1812.
UCSCuc003mcz.3. human.

Organism-specific databases

CTD1812.
GeneCardsGC05M174800.
HGNCHGNC:3020. DRD1.
HPAHPA013393.
MIM126449. gene.
neXtProtNX_P21728.
PharmGKBPA147.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262978.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidP21728.
KOK04144.
OMASPTTFDV.
OrthoDBEOG780RMN.
PhylomeDBP21728.
TreeFamTF325181.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP21728.
CleanExHS_DRD1.
GenevestigatorP21728.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR001413. Dopamine_D1_rcpt.
IPR000929. Dopamine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00565. DOPAMINED1AR.
PR00242. DOPAMINER.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDopamine_receptor_D1.
GenomeRNAi1812.
NextBio7385.
PROP21728.
SOURCESearch...

Entry information

Entry nameDRD1_HUMAN
AccessionPrimary (citable) accession number: P21728
Secondary accession number(s): B2RA44, Q4QRJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries