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Protein

D(1A) dopamine receptor

Gene

Drd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

  • activation of adenylate cyclase activity Source: MGI
  • adenylate cyclase-activating dopamine receptor signaling pathway Source: MGI
  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
  • adult walking behavior Source: MGI
  • associative learning Source: MGI
  • astrocyte development Source: MGI
  • behavioral fear response Source: MGI
  • behavioral response to cocaine Source: MGI
  • calcium-mediated signaling Source: Ensembl
  • cellular response to catecholamine stimulus Source: MGI
  • cellular response to hypoxia Source: Ensembl
  • cellular response to insulin stimulus Source: Ensembl
  • cerebral cortex GABAergic interneuron migration Source: MGI
  • conditioned taste aversion Source: MGI
  • dentate gyrus development Source: MGI
  • dopamine receptor signaling pathway Source: MGI
  • dopamine transport Source: MGI
  • feeding behavior Source: MGI
  • glucose import Source: MGI
  • G-protein coupled receptor signaling pathway Source: MGI
  • G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: MGI
  • grooming behavior Source: MGI
  • habituation Source: MGI
  • hippocampus development Source: MGI
  • learning Source: MGI
  • locomotory behavior Source: MGI
  • long term synaptic depression Source: MGI
  • long-term synaptic potentiation Source: MGI
  • maternal behavior Source: MGI
  • mating behavior Source: MGI
  • memory Source: MGI
  • muscle contraction Source: MGI
  • negative regulation of cell migration Source: Ensembl
  • negative regulation of circadian sleep/wake cycle, sleep Source: Ensembl
  • negative regulation of protein kinase activity Source: Ensembl
  • neuronal action potential Source: MGI
  • operant conditioning Source: MGI
  • orbitofrontal cortex development Source: Ensembl
  • peristalsis Source: MGI
  • phospholipase C-activating dopamine receptor signaling pathway Source: MGI
  • positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: GO_Central
  • positive regulation of cAMP biosynthetic process Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: MGI
  • positive regulation of feeding behavior Source: Ensembl
  • positive regulation of long-term synaptic potentiation Source: Ensembl
  • positive regulation of membrane potential Source: Ensembl
  • positive regulation of release of sequestered calcium ion into cytosol Source: MGI
  • positive regulation of synaptic transmission, glutamatergic Source: MGI
  • protein import into nucleus Source: MGI
  • regulation of dopamine metabolic process Source: MGI
  • regulation of long-term neuronal synaptic plasticity Source: Ensembl
  • regulation of vasoconstriction Source: Ensembl
  • response to activity Source: Ensembl
  • response to amino acid Source: Ensembl
  • response to amphetamine Source: MGI
  • response to antidepressant Source: Ensembl
  • response to cocaine Source: MGI
  • response to drug Source: MGI
  • response to estradiol Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to food Source: Ensembl
  • response to morphine Source: Ensembl
  • response to nicotine Source: Ensembl
  • response to retinoic acid Source: Ensembl
  • sensitization Source: MGI
  • sensory perception of chemical stimulus Source: GO_Central
  • social behavior Source: Ensembl
  • striatum development Source: MGI
  • synaptic transmission, dopaminergic Source: MGI
  • temperature homeostasis Source: MGI
  • transmission of nerve impulse Source: MGI
  • vasodilation Source: InterPro
  • visual learning Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_294218. Dopamine receptors.
REACT_313192. G alpha (s) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
D(1A) dopamine receptor
Alternative name(s):
Dopamine D1 receptor
Gene namesi
Name:Drd1
Synonyms:Drd1a, Gpcr15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:99578. 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446D(1A) dopamine receptorPRO_0000069375Add
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

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ61616.
PRIDEiQ61616.

PTM databases

PhosphoSiteiQ61616.

Expressioni

Gene expression databases

BgeeiQ61616.
CleanExiMM_DRD1A.
ExpressionAtlasiQ61616. baseline and differential.
GenevisibleiQ61616. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi199305. 1 interaction.
STRINGi10090.ENSMUSP00000021932.

Structurei

3D structure databases

ProteinModelPortaliQ61616.
SMRiQ61616. Positions 28-346.
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.
GeneTreeiENSGT00760000118774.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiQ61616.
KOiK04144.
OMAiSSLNRMY.
OrthoDBiEOG780RMN.
PhylomeDBiQ61616.
TreeFamiTF325181.

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.

Q61616-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPNTSTMDE TGLPVERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF
60 70 80 90 100
RHLRSKVTNF FVISLAVSDL LVAVLVMPWK AVAEIAGFWP FGSFCNIWVA
110 120 130 140 150
FDIMCSTASI LNLCVISVDR YWAISSPFQY ERKMTPKAAF ILISVAWTLS
160 170 180 190 200
VLISFIPVQL SWHKAKPTWP LDGNFTSLED AEDDNCDTRL SRTYAISSSL
210 220 230 240 250
ISFYIPVAIM IVTYTSIYRI AQKQIRRISA LERAAVHAKN CQTTTGNGNP
260 270 280 290 300
VECSQSESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI SNCMVPFCGS
310 320 330 340 350
EETQPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFQKA FSTLLGCYRL
360 370 380 390 400
CPTTNNAIET VSINNNGAVM FSSHHEPRGS ISKDCNLVYL IPHAVGSSED
410 420 430 440
LKREEAGGIP KPLEKLSPAL SVILDYDTDV SLEKIQPVTH SGQHST
Length:446
Mass (Da):49,612
Last modified:May 30, 2003 - v2
Checksum:i509BA66F9DF82A74
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1964TYAI → DIRH (PubMed:8288218).Curated
Sequence conflicti240 – 2401N → S in AAA16848 (PubMed:8288218).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044723 mRNA. Translation: BAC32050.1.
BC137641 mRNA. Translation: AAI37642.1.
BC137655 mRNA. Translation: AAI37656.1.
L20336 mRNA. Translation: AAA16848.1.
CCDSiCCDS26524.1.
RefSeqiNP_001278730.1. NM_001291801.1.
NP_034206.1. NM_010076.3.
UniGeneiMm.54161.

Genome annotation databases

EnsembliENSMUST00000021932; ENSMUSP00000021932; ENSMUSG00000021478.
GeneIDi13488.
KEGGimmu:13488.
UCSCiuc011yzm.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044723 mRNA. Translation: BAC32050.1.
BC137641 mRNA. Translation: AAI37642.1.
BC137655 mRNA. Translation: AAI37656.1.
L20336 mRNA. Translation: AAA16848.1.
CCDSiCCDS26524.1.
RefSeqiNP_001278730.1. NM_001291801.1.
NP_034206.1. NM_010076.3.
UniGeneiMm.54161.

3D structure databases

ProteinModelPortaliQ61616.
SMRiQ61616. Positions 28-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199305. 1 interaction.
STRINGi10090.ENSMUSP00000021932.

Chemistry

BindingDBiQ61616.
ChEMBLiCHEMBL3071.
GuidetoPHARMACOLOGYi214.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiQ61616.

Proteomic databases

PaxDbiQ61616.
PRIDEiQ61616.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021932; ENSMUSP00000021932; ENSMUSG00000021478.
GeneIDi13488.
KEGGimmu:13488.
UCSCiuc011yzm.3. mouse.

Organism-specific databases

CTDi1812.
MGIiMGI:99578. Drd1.

Phylogenomic databases

eggNOGiNOG262978.
GeneTreeiENSGT00760000118774.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiQ61616.
KOiK04144.
OMAiSSLNRMY.
OrthoDBiEOG780RMN.
PhylomeDBiQ61616.
TreeFamiTF325181.

Enzyme and pathway databases

ReactomeiREACT_294218. Dopamine receptors.
REACT_313192. G alpha (s) signalling events.

Miscellaneous databases

NextBioi283997.
PROiQ61616.
SOURCEiSearch...

Gene expression databases

BgeeiQ61616.
CleanExiMM_DRD1A.
ExpressionAtlasiQ61616. baseline and differential.
GenevisibleiQ61616. MM.

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

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Retina.
  2. "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].
    Tissue: Brain.
  3. "Identification, chromosomal location, and genome organization of mammalian G-protein-coupled receptors."
    Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I., Copeland N.G., Jenkins N.A.
    Genomics 18:175-184(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 193-279.
    Tissue: Testis.

Entry informationi

Entry nameiDRD1_MOUSE
AccessioniPrimary (citable) accession number: Q61616
Secondary accession number(s): B2RPW8, Q8C8P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2003
Last modified: July 22, 2015
This is version 134 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.