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Protein

D(1A) dopamine receptor

Gene

Drd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • angiotensin receptor binding Source: RGD
  • ATPase binding Source: RGD
  • D3 dopamine receptor binding Source: RGD
  • dopamine binding Source: GO_Central
  • dopamine neurotransmitter receptor activity, coupled via Gs Source: RGD
  • drug binding Source: RGD
  • G-protein alpha-subunit binding Source: RGD
  • G-protein coupled amine receptor activity Source: GO_Central
  • G-protein coupled receptor activity Source: RGD
  • protein complex binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein phosphatase binding Source: RGD
  • receptor binding Source: RGD

GO - Biological processi

  • activation of adenylate cyclase activity Source: BHF-UCL
  • adenylate cyclase-activating dopamine receptor signaling pathway Source: BHF-UCL
  • associative learning Source: RGD
  • behavioral response to cocaine Source: RGD
  • calcium-mediated signaling Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • dopamine receptor signaling pathway Source: RGD
  • intracellular protein transport Source: RGD
  • locomotory behavior Source: RGD
  • negative regulation of cell migration Source: RGD
  • negative regulation of circadian sleep/wake cycle, sleep Source: RGD
  • negative regulation of protein kinase activity Source: RGD
  • operant conditioning Source: RGD
  • orbitofrontal cortex development Source: RGD
  • phosphatidylinositol catabolic process Source: BHF-UCL
  • phosphatidylinositol metabolic process Source: BHF-UCL
  • phospholipase C-activating dopamine receptor signaling pathway Source: GO_Central
  • positive regulation of adenylate cyclase activity Source: BHF-UCL
  • positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: GO_Central
  • positive regulation of cAMP biosynthetic process Source: RGD
  • positive regulation of feeding behavior Source: RGD
  • positive regulation of long-term synaptic potentiation Source: RGD
  • positive regulation of membrane potential Source: RGD
  • regulation of ion transport Source: RGD
  • regulation of long-term neuronal synaptic plasticity Source: RGD
  • regulation of vasoconstriction Source: RGD
  • response to activity Source: RGD
  • response to amino acid Source: RGD
  • response to amphetamine Source: RGD
  • response to antidepressant Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to food Source: RGD
  • response to morphine Source: RGD
  • response to nicotine Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organonitrogen compound Source: RGD
  • response to retinoic acid Source: RGD
  • response to steroid hormone Source: RGD
  • sensory perception of chemical stimulus Source: GO_Central
  • social behavior Source: RGD
  • striatum development Source: RGD
  • synapse assembly Source: BHF-UCL
  • synaptic transmission, dopaminergic Source: RGD
  • vasodilation Source: InterPro
  • visual learning Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Names & Taxonomyi

Protein namesi
Recommended name:
D(1A) dopamine receptor
Alternative name(s):
Dopamine D1 receptor
Gene namesi
Name:Drd1
Synonyms:Drd1a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2518. Drd1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222ExtracellularSequence AnalysisAdd
BLAST
Transmembranei23 – 4826Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini49 – 5911CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei60 – 8627Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini87 – 959ExtracellularSequence Analysis
Transmembranei96 – 11823Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini119 – 13719CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei138 – 16225Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini163 – 19230ExtracellularSequence AnalysisAdd
BLAST
Transmembranei193 – 21826Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini219 – 27254CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei273 – 29927Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini300 – 31213ExtracellularSequence AnalysisAdd
BLAST
Transmembranei313 – 33725Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini338 – 446109CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • axon Source: RGD
  • axon terminus Source: RGD
  • caveola Source: RGD
  • dendrite Source: RGD
  • dendritic shaft Source: RGD
  • dendritic spine Source: RGD
  • dendritic spine head Source: RGD
  • dendritic spine neck Source: RGD
  • endoplasmic reticulum Source: RGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: RGD
  • integral component of plasma membrane Source: GO_Central
  • neuronal cell body Source: RGD
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi333 – 3331F → A: Loss of interaction with DNAJC14. Abolishes transport to the cell surface. 1 Publication
Mutagenesisi337 – 3371F → A: Loss of interaction with DNAJC14. Abolishes transport to the cell surface. 1 Publication
Mutagenesisi341 – 3411F → A: Loss of interaction with DNAJC14. Abolishes transport to the cell surface. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446D(1A) dopamine receptorPRO_0000069378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi95 ↔ 186PROSITE-ProRule annotation
Lipidationi347 – 3471S-palmitoyl cysteineBy similarity
Lipidationi351 – 3511S-palmitoyl cysteineBy similarity

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

PTM databases

PhosphoSiteiP18901.

Expressioni

Tissue specificityi

Brain, in the striatum, the nucleus accumbens, and the olfactory tubercle.

Gene expression databases

GenevisibleiP18901. RN.

Interactioni

Subunit structurei

Interacts with calcyon (By similarity). Interacts with DNAJC14 via its C-terminus.By similarity1 Publication

Protein-protein interaction databases

BioGridi246496. 3 interactions.
DIPiDIP-49024N.
STRINGi10116.ENSRNOP00000034820.

Structurei

3D structure databases

ProteinModelPortaliP18901.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG262978.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP18901.
PhylomeDBiP18901.

Family and domain databases

InterProiIPR001413. Dopamine_D1_rcpt.
IPR000929. Dopamine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00565. DOPAMINED1AR.
PR00242. DOPAMINER.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPNTSTMDE AGLPAERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF
60 70 80 90 100
RHLRSKVTNF FVISLAVSDL LVAVLVMPWK AVAEIAGFWP LGPFCNIWVA
110 120 130 140 150
FDIMCSTASI LNLCVISVDR YWAISSPFQY ERKMTPKAAF ILISVAWTLS
160 170 180 190 200
VLISFIPVQL SWHKAKPTWP LDGNFTSLED TEDDNCDTRL SRTYAISSSL
210 220 230 240 250
ISFYIPVAIM IVTYTSIYRI AQKQIRRISA LERAAVHAKN CQTTAGNGNP
260 270 280 290 300
VECAQSESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI SNCMVPFCGS
310 320 330 340 350
EETQPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFQKA FSTLLGCYRL
360 370 380 390 400
CPTTNNAIET VSINNNGAVV FSSHHEPRGS ISKDCNLVYL IPHAVGSSED
410 420 430 440
LKKEEAGGIA KPLEKLSPAL SVILDYDTDV SLEKIQPVTH SGQHST
Length:446
Mass (Da):49,428
Last modified:May 1, 1991 - v2
Checksum:i0380042E8590F470
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911L → F (PubMed:1402930).Curated
Sequence conflicti93 – 931P → S (PubMed:1402930).Curated
Sequence conflicti165 – 1651A → T (PubMed:2168520).Curated
Sequence conflicti190 – 1901L → F (PubMed:2168520).Curated
Sequence conflicti227 – 2271R → G (PubMed:2168520).Curated
Sequence conflicti253 – 2531C → W (PubMed:2168520).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35077 mRNA. Translation: AAA70428.1.
S46131 Genomic DNA. Translation: AAB23803.1.
PIRiA36049. DYRTD1.
UniGeneiRn.24039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35077 mRNA. Translation: AAA70428.1.
S46131 Genomic DNA. Translation: AAB23803.1.
PIRiA36049. DYRTD1.
UniGeneiRn.24039.

3D structure databases

ProteinModelPortaliP18901.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246496. 3 interactions.
DIPiDIP-49024N.
STRINGi10116.ENSRNOP00000034820.

Chemistry

BindingDBiP18901.
ChEMBLiCHEMBL265.
GuidetoPHARMACOLOGYi214.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP18901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi2518. Drd1.

Phylogenomic databases

eggNOGiNOG262978.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP18901.
PhylomeDBiP18901.

Miscellaneous databases

NextBioi602967.
PROiP18901.

Gene expression databases

GenevisibleiP18901. RN.

Family and domain databases

InterProiIPR001413. Dopamine_D1_rcpt.
IPR000929. Dopamine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00565. DOPAMINED1AR.
PR00242. DOPAMINER.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of a D1 dopamine receptor linked to adenylyl cyclase activation."
    Monsma F.J. Jr., Mahan L.C., McVittie L.D., Gerfen C.R., Sibley D.R.
    Proc. Natl. Acad. Sci. U.S.A. 87:6723-6727(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Characterization of gene organization and promoter region of the rat dopamine D1 receptor gene."
    Zhou Q.Y., Li C., Civelli O.
    J. Neurochem. 59:1875-1883(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning of two additional catecholamine receptors from rat brain."
    O'Dowd B.F., Nguyen T., Tirpak A., Jarvie K.R., Israel Y., Seeman P., Niznik H.B.
    FEBS Lett. 262:8-12(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 114-263.
    Tissue: Corpus striatum.
  5. "Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein."
    Bermak J.C., Li M., Bullock C.M., Zhou Q.-Y.
    Nat. Cell Biol. 3:492-498(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNAJC14, GLYCOSYLATION, MUTAGENESIS OF PHE-333; PHE-337 AND PHE-341, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiDRD1_RAT
AccessioniPrimary (citable) accession number: P18901
Secondary accession number(s): P21669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 1, 1991
Last modified: July 22, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.