P21728 (DRD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D(1A) dopamine receptor

Alternative name(s):
Dopamine D1 receptor

Gene names

Name:

DRD1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cell membrane Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of adenylate cyclase activity by dopamine receptor signaling pathway Inferred from direct assay Ref.1Ref.2. Source: BHF-UCL activation of phospholipase C activity by dopamine receptor signaling pathway Inferred from direct assay. Source: BHF-UCL adult walking behavior Inferred from sequence or structural similarity. Source: BHF-UCL cerebral cortex GABAergic interneuron migration Inferred from sequence or structural similarity. Source: BHF-UCL dopamine metabolic process Inferred by curator. Source: BHF-UCL elevation of cytosolic calcium ion concentration involved in G-protein signaling coupled to IP3 second messenger Inferred from direct assay. Source: BHF-UCL mating behavior Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cAMP biosynthetic process Inferred from direct assay. Source: BHF-UCL positive regulation of cell migration Inferred from sequence or structural similarity. 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. 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 regulation of dopamine uptake Inferred by curator. Source: BHF-UCL response to drug Inferred from sequence or structural similarity. Source: BHF-UCL synapse assembly Inferred from sequence or structural similarity. Source: BHF-UCL visual learning Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred by curator Ref.1. Source: BHF-UCL membrane fraction Inferred from direct assay. Source: BHF-UCL
Molecular function	dopamine binding Inferred from mutant phenotype. Source: BHF-UCL dopamine receptor activity, coupled via Gs Inferred from direct assay Ref.1Ref.2. Source: BHF-UCL protein binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 446

446

D(1A) dopamine receptor

PRO_0000069373

Regions

Topological domain

1 – 23

23

Extracellular Potential

Transmembrane

24 – 49

26

Helical; Name=1; Potential

Topological domain

50 – 60

11

Cytoplasmic Potential

Transmembrane

61 – 87

27

Helical; Name=2; Potential

Topological domain

88 – 96

9

Extracellular Potential

Transmembrane

97 – 119

23

Helical; Name=3; Potential

Topological domain

120 – 138

19

Cytoplasmic Potential

Transmembrane

139 – 163

25

Helical; Name=4; Potential

Topological domain

164 – 192

29

Extracellular Potential

Transmembrane

193 – 218

26

Helical; Name=5; Potential

Topological domain

219 – 272

54

Cytoplasmic Potential

Transmembrane

273 – 299

27

Helical; Name=6; Potential

Topological domain

300 – 312

13

Extracellular Potential

Transmembrane

313 – 337

25

Helical; Name=7; Potential

Topological domain

338 – 446

109

Cytoplasmic Potential

Amino acid modifications

Lipidation

347

1

S-palmitoyl cysteine Ref.10

Lipidation

351

1

S-palmitoyl cysteine Ref.10

Glycosylation

5

1

N-linked (GlcNAc...) Potential

Disulfide bond

96 ↔ 186

By similarity

Natural variations

Natural variant

37

1

T → P.
Corresponds to variant rs5327 [ dbSNP | Ensembl ].

VAR_014670

Natural variant

37

1

T → R.
Corresponds to variant rs5328 [ dbSNP | Ensembl ].

VAR_014671

Natural variant

50

1

R → S.
Corresponds to variant rs5330 [ dbSNP | Ensembl ].

VAR_014672

Natural variant

81

1

K → R. Ref.11

VAR_064577

Natural variant

199

1

S → A.
Corresponds to variant rs5331 [ dbSNP | Ensembl ].

VAR_014673

Natural variant

259

1

S → Y. Ref.11
Corresponds to variant rs74414188 [ dbSNP | Ensembl ].

VAR_064578

Experimental info

Sequence conflict

438

1

I → M in CAA41734. Ref.2

Secondary structure

1

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446

Helix Strand Turn

Details...

Helix

26 – 50

25

Helix

52 – 56

5

Helix

59 – 85

27

Turn

86 – 88

3

Beta strand

89 – 92

4

Helix

96 – 126

31

Helix

137 – 156

20

Helix

158 – 165

8

Beta strand

170 – 172

3

Turn

187 – 189

3

Helix

191 – 202

12

Helix

204 – 216

13

Beta strand

217 – 219

3

Helix

232 – 239

8

Helix

243 – 248

6

Helix

263 – 283

21

Helix

286 – 298

13

Turn

302 – 305

4

Turn

312 – 314

3

Helix

315 – 318

4

Helix

319 – 322

4

Helix

323 – 329

7

Helix

330 – 333

4

Turn

335 – 337

3

Helix

338 – 344

7

Sequences

	Sequence		Length	Mass (Da)
	P21728 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 64E062D765D0DBA7	FASTA	446	49,293
	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

References

	« Hide 'large scale' referencesShow '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: 2144334] [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: 2168520] [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: 1975640] [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: 8471124] [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. , 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: 14702039] [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. , 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: 15489334] [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: 10618483] [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: 21179162] [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.

IPI

IPI00010289.

PIR

DYHUD1. S11377.

RefSeq

NP_000785.1. NM_000794.3.

UniGene

Hs.2624.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OZ5	model	-	A	1-446	[»]

ProteinModelPortal

P21728.

SMR

P21728. Positions 20-345.

ModBase

Search...

Protein-protein interaction databases

STRING

P21728.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P21728.

Polymorphism databases

DMDM

118228.

Proteomic databases

PRIDE

P21728.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000329144; ENSP00000327652; ENSG00000184845.
ENST00000393752; ENSP00000377353; ENSG00000184845.

GeneID

1812.

KEGG

hsa:1812.

UCSC

uc003mcz.1. human.

Organism-specific databases

CTD

1812.

GeneCards

GC05M174800.

H-InvDB

HIX0032003.

HGNC

HGNC:3020. DRD1.

HPA

HPA013393.

MIM

126449. gene.

neXtProt

NX_P21728.

PharmGKB

PA147.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13618.

HOGENOM

HBG445348.

HOVERGEN

HBG106962.

InParanoid

P21728.

OMA

ITFDVFV.

OrthoDB

EOG4BG8W3.

PhylomeDB

P21728.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P21728.

Bgee

P21728.

CleanEx

HS_DRD1.

Genevestigator

P21728.

GermOnline

ENSG00000184845. Homo sapiens.

Family and domain databases

InterPro

IPR000276. 7TM_GPCR_Rhodpsn.
IPR001413. Dopa_1A_rcpt.
IPR000929. Dopamine_rcpt.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]

KO

K04144.

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00565. DOPAMINED1AR.
PR00242. DOPAMINER.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01063. 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.

NextBio

7385.

SOURCE

Search...

Entry information

Entry name

DRD1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.