P18901 (DRD1_RAT) 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
Synonyms:	Drd1a

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 calcyon By similarity. Interacts with DNAJC14 via its C-terminus. Ref.5
Subcellular location	Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note: Transport from the endoplasmic reticulum to the cell surface is regulated by interaction with DNAJC14. Ref.5
Tissue specificity	Brain, in the striatum, the nucleus accumbens, and the olfactory tubercle.
Post-translational modification	N-glycosylated. Ref.5
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of adenylate cyclase activity Inferred from direct assay PubMed 8702641. Source: BHF-UCL adenylate cyclase-activating dopamine receptor signaling pathway Inferred from direct assay PubMed 18424554. Source: BHF-UCL behavioral response to cocaine Inferred from mutant phenotype PubMed 16377433. Source: RGD calcium-mediated signaling Inferred from direct assay PubMed 14983054. Source: RGD cellular response to insulin stimulus Inferred from expression pattern PubMed 12707290. Source: RGD eating behavior Inferred from mutant phenotype PubMed 11705777. Source: RGD intracellular protein transport Inferred from mutant phenotype PubMed 16641250. Source: RGD locomotory behavior Inferred from mutant phenotype PubMed 16377433. Source: RGD negative regulation of cell migration Inferred from mutant phenotype PubMed 12688394. Source: RGD negative regulation of circadian sleep/wake cycle, sleep Inferred from direct assay PubMed 12944496. Source: RGD negative regulation of protein kinase activity Inferred from mutant phenotype PubMed 12688394. Source: RGD operant conditioning Inferred from mutant phenotype PubMed 15245880. Source: RGD phosphatidylinositol catabolic process Inferred from direct assay PubMed 8702641. Source: BHF-UCL positive regulation of long-term synaptic potentiation Inferred from mutant phenotype PubMed 20377617. Source: RGD regulation of ion transport Inferred from direct assay PubMed 14983054. Source: RGD regulation of long-term neuronal synaptic plasticity Inferred from mutant phenotype PubMed 16855100. Source: RGD regulation of vasoconstriction Inferred from mutant phenotype PubMed 15778266. Source: RGD response to drug Inferred from expression pattern PubMed 15798088. Source: RGD synapse assembly Inferred from expression pattern PubMed 10051231. Source: BHF-UCL synaptic transmission, dopaminergic Inferred from direct assay PubMed 17314300. Source: RGD visual learning Inferred from mutant phenotype PubMed 16855100. Source: RGD
Cellular_component	axon Inferred from direct assay PubMed 17576511. Source: RGD caveola Inferred from direct assay PubMed 15265765. Source: RGD dendritic spine Inferred from direct assay PubMed 11818555. Source: RGD endoplasmic reticulum Inferred from direct assay PubMed 17576511. Source: RGD endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from direct assay PubMed 11818555. Source: RGD neuronal cell body Inferred from direct assay PubMed 17576511. Source: RGD
Molecular_function	dopamine neurotransmitter receptor activity, coupled via Gs Inferred from direct assay PubMed 11818555PubMed 17314300. Source: RGD drug binding Inferred from direct assay PubMed 16855100PubMed 17314300. Source: RGD
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_0000069378
Regions
	Topological domain	1 – 22	22	Extracellular Potential
	Transmembrane	23 – 48	26	Helical; Name=1; Potential
	Topological domain	49 – 59	11	Cytoplasmic Potential
	Transmembrane	60 – 86	27	Helical; Name=2; Potential
	Topological domain	87 – 95	9	Extracellular Potential
	Transmembrane	96 – 118	23	Helical; Name=3; Potential
	Topological domain	119 – 137	19	Cytoplasmic Potential
	Transmembrane	138 – 162	25	Helical; Name=4; Potential
	Topological domain	163 – 192	30	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 By similarity
	Lipidation	351	1	S-palmitoyl cysteine By similarity
	Glycosylation	4	1	N-linked (GlcNAc...) Potential
	Disulfide bond	95 ↔ 186		By similarity
Experimental info
	Mutagenesis	333	1	F → A: Loss of interaction with DNAJC14. Abolishes transport to the cell surface. Ref.5
	Mutagenesis	337	1	F → A: Loss of interaction with DNAJC14. Abolishes transport to the cell surface. Ref.5
	Mutagenesis	341	1	F → A: Loss of interaction with DNAJC14. Abolishes transport to the cell surface. Ref.5
	Sequence conflict	91	1	L → F Ref.3
	Sequence conflict	93	1	P → S Ref.3
	Sequence conflict	165	1	A → T Ref.2
	Sequence conflict	190	1	L → F Ref.2
	Sequence conflict	227	1	R → G Ref.2
	Sequence conflict	253	1	C → W Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P18901 [UniParc]. Last modified May 1, 1991. Version 2. Checksum: 0380042E8590F470	FASTA	446	49,428
	10 20 30 40 50 60 MAPNTSTMDE AGLPAERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF RHLRSKVTNF 70 80 90 100 110 120 FVISLAVSDL LVAVLVMPWK AVAEIAGFWP LGPFCNIWVA FDIMCSTASI LNLCVISVDR 130 140 150 160 170 180 YWAISSPFQY ERKMTPKAAF ILISVAWTLS VLISFIPVQL SWHKAKPTWP LDGNFTSLED 190 200 210 220 230 240 TEDDNCDTRL SRTYAISSSL ISFYIPVAIM IVTYTSIYRI AQKQIRRISA LERAAVHAKN 250 260 270 280 290 300 CQTTAGNGNP VECAQSESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI SNCMVPFCGS 310 320 330 340 350 360 EETQPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFQKA FSTLLGCYRL CPTTNNAIET 370 380 390 400 410 420 VSINNNGAVV FSSHHEPRGS ISKDCNLVYL IPHAVGSSED LKKEEAGGIA KPLEKLSPAL 430 440 SVILDYDTDV SLEKIQPVTH SGQHST

References

[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]	"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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M35077 mRNA. Translation: AAA70428.1. S46131 Genomic DNA. Translation: AAB23803.1.
IPI	IPI00324847.
PIR	DYRTD1. A36049.
RefSeq	NP_036678.2. NM_012546.2.
UniGene	Rn.24039.
3D structure databases
ProteinModelPortal	P18901.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-49024N.
STRING	10116.ENSRNOP00000034820.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P18901.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	24316.
KEGG	rno:24316.
Organism-specific databases
CTD	1812.
RGD	2518. Drd1.
Phylogenomic databases
eggNOG	NOG262978.
HOGENOM	HOG000239242.
HOVERGEN	HBG106962.
InParanoid	P18901.
KO	K04144.
OrthoDB	EOG4BG8W3.
Gene expression databases
Genevestigator	P18901.
GermOnline	ENSRNOG00000023688. Rattus norvegicus.
Family and domain databases
InterPro	IPR001413. Dopa_1A_rcpt. IPR000929. Dopamine_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
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
BindingDB	P18901.
ChEMBL	CHEMBL265.
NextBio	602967.

Entry information

Entry name

DRD1_RAT

Accession

Primary (citable) accession number: P18901
Secondary accession number(s): P21669

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	May 1, 1991
Last modified:	May 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program