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P51436 (DRD4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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(4) dopamine receptor
Alternative name(s):
D(2C) dopamine receptor
Dopamine D4 receptor
Gene names
Name:Drd4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Modulates the circadian rhythm of contrast sensitivity by regulating the rhythmic expression of NPAS2 in the retinal ganglion cells. Ref.7

Subunit structure

Forms homo- and heterooligomers with DRD2 By similarity. The interaction with DRD2 may modulate agonist-induced downstream signaling By similarity. Interacts with CLIC6 and GPRASP1 By similarity. May interact with ADORA2A By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Disruption phenotype

Mice show a significant reduction in daytime contrast sensitivity. Ref.7

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Caution

In contrast to human protein, does not interact with KLHL12 and is not ubiquitinated by the BCR(KLHL12) complex (Ref.6).

Ontologies

Keywords
   Biological processBiological rhythms
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-inhibiting dopamine receptor signaling pathway

Inferred from mutant phenotype PubMed 14684868. Source: MGI

adult locomotory behavior

Inferred from mutant phenotype PubMed 9323127. Source: MGI

arachidonic acid secretion

Inferred from electronic annotation. Source: Ensembl

behavioral fear response

Inferred from electronic annotation. Source: Ensembl

behavioral response to cocaine

Inferred from mutant phenotype PubMed 12783155PubMed 9323127. Source: MGI

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

fear response

Inferred from mutant phenotype PubMed 11860516. Source: MGI

negative regulation of adenylate cyclase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of voltage-gated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

olfactory learning

Inferred from electronic annotation. Source: Ensembl

photoperiodism

Inferred from electronic annotation. Source: Ensembl

positive regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

positive regulation of penile erection

Inferred from electronic annotation. Source: Ensembl

positive regulation of sodium:proton antiporter activity

Inferred from electronic annotation. Source: Ensembl

regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

regulation of circadian rhythm

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of dopamine metabolic process

Inferred from mutant phenotype PubMed 9323127. Source: MGI

regulation of inhibitory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 11356863PubMed 14684868. Source: MGI

regulation of neurotransmitter secretion

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from mutant phenotype PubMed 9323127. Source: MGI

response to histamine

Inferred from electronic annotation. Source: Ensembl

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

short-term memory

Inferred from electronic annotation. Source: Ensembl

synaptic transmission, dopaminergic

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

terminal bouton

Inferred from electronic annotation. Source: Ensembl

vesicle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondopamine binding

Inferred from electronic annotation. Source: Ensembl

dopamine neurotransmitter receptor activity, coupled via Gi/Go

Inferred from mutant phenotype PubMed 11356863. Source: MGI

drug binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387D(4) dopamine receptor
PRO_0000069402

Regions

Topological domain1 – 3434Extracellular Potential
Transmembrane35 – 5723Helical; Name=1; Potential
Topological domain58 – 6710Cytoplasmic Potential
Transmembrane68 – 9023Helical; Name=2; Potential
Topological domain91 – 10616Extracellular Potential
Transmembrane107 – 12822Helical; Name=3; Potential
Topological domain129 – 14618Cytoplasmic Potential
Transmembrane147 – 17024Helical; Name=4; Potential
Topological domain171 – 18616Extracellular Potential
Transmembrane187 – 20822Helical; Name=5; Potential
Topological domain209 – 314106Cytoplasmic Potential
Transmembrane315 – 33723Helical; Name=6; Potential
Topological domain338 – 3469Extracellular Potential
Transmembrane347 – 36923Helical; Name=7; Potential
Topological domain370 – 38718Cytoplasmic Potential

Amino acid modifications

Glycosylation31N-linked (GlcNAc...) Potential
Disulfide bond105 ↔ 180 By similarity

Experimental info

Sequence conflict11M → L in BAC31893. Ref.3
Sequence conflict191E → K in BAC31893. Ref.3
Sequence conflict471A → T in AAB50730. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P51436 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: BEA306D5E8AA02E9

FASTA38741,487
        10         20         30         40         50         60 
MGNSSATEDG GLLAGRGPES LGTGAGLGGA GAAALVGGVL LIGLVLAGNS LVCVSVASER 

        70         80         90        100        110        120 
TLQTPTNYFI VSLAAADLLL AVLVLPLFVY SEVQGGVWLL SPRLCDTLMA MDVMLCTASI 

       130        140        150        160        170        180 
FNLCAISVDR FVAVTVPLRY NQQGQCQLLL IAATWLLSAA VASPVVCGLN DVPGRDPAVC 

       190        200        210        220        230        240 
CLENRDYVVY SSVCSFFLPC PLMLLLYWAT FRGLRRWEAA RHTKLHSRAP RRPSGPGPPV 

       250        260        270        280        290        300 
SDPTQGPFFP DCPPPLPSLR TSPSDSSRPE SELSQRPCSP GCLLADAALP QPPEPSSRRR 

       310        320        330        340        350        360 
RGAKITGRER KAMRVLPVVV GAFLVCWTPF FVVHITRALC PACFVSPRLV SAVTWLGYVN 

       370        380 
SALNPIIYTI FNAEFRSVFR KTLRLRC 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterisation of the gene encoding the murine D4 dopamine receptor."
Fishburn C.S., Carmon S., Fuchs S.
FEBS Lett. 361:215-219(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[2]"Genomic structure and tissue distribution of the mouse dopamine D4 receptor."
Suzuki T., Kobayashi K., Nagatsu T.
Neurosci. Lett. 199:69-72(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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. expand/collapse author list , 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/6.
Tissue: Retina.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Strain: C57BL/6.
Tissue: Retina.
[6]"BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by a Cul3-based E3 ligase."
Rondou P., Haegeman G., Vanhoenacker P., Van Craenenbroeck K.
J. Biol. Chem. 283:11083-11096(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]"Circadian rhythm of contrast sensitivity is regulated by a dopamine-neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling pathway in retinal ganglion cells."
Hwang C.K., Chaurasia S.S., Jackson C.R., Chan G.C., Storm D.R., Iuvone P.M.
J. Neurosci. 33:14989-14997(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19880 Genomic DNA. Translation: AAC52190.1.
S80929 expand/collapse EMBL AC list , S80920, S80927, S80928 Genomic DNA. Translation: AAB50730.1.
AK044379 mRNA. Translation: BAC31893.1.
CH466531 Genomic DNA. Translation: EDL18041.1.
BC016086 mRNA. Translation: AAH16086.1.
BC051421 mRNA. Translation: AAH51421.2.
CCDSCCDS22007.1.
PIRI49246.
RefSeqNP_031904.1. NM_007878.2.
UniGeneMm.41075.

3D structure databases

ProteinModelPortalP51436.
SMRP51436. Positions 32-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000026569.

Chemistry

BindingDBP51436.
ChEMBLCHEMBL2111359.
GuidetoPHARMACOLOGY217.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP51436.

Proteomic databases

PRIDEP51436.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026569; ENSMUSP00000026569; ENSMUSG00000025496.
GeneID13491.
KEGGmmu:13491.
UCSCuc009kkm.1. mouse.

Organism-specific databases

CTD1815.
MGIMGI:94926. Drd4.

Phylogenomic databases

eggNOGNOG256691.
GeneTreeENSGT00750000117240.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidQ7TT80.
KOK04147.
OMADPAVCRL.
OrthoDBEOG769ZMG.
PhylomeDBP51436.
TreeFamTF334382.

Gene expression databases

BgeeP51436.
CleanExMM_DRD4.
GenevestigatorP51436.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR002185. Dopamine_D4_rcpt.
IPR000929. Dopamine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24249:SF37. PTHR24249:SF37. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00569. DOPAMINED4R.
PR00242. DOPAMINER.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284009.
PROP51436.
SOURCESearch...

Entry information

Entry nameDRD4_MOUSE
AccessionPrimary (citable) accession number: P51436
Secondary accession number(s): O35838, Q7TT80, Q8BXS4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries