Q61616 (DRD1_MOUSE) 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, Gpcr15

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity.
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.
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 12488442. Source: MGI adenylate cyclase-activating dopamine receptor signaling pathway Inferred from direct assay PubMed 11923452PubMed 12665504PubMed 8738226. Source: MGI adult walking behavior Inferred from mutant phenotype PubMed 7954836. Source: MGI astrocyte development Inferred from mutant phenotype PubMed 17360497. Source: MGI behavioral fear response Inferred from mutant phenotype PubMed 11172752PubMed 11409899. Source: MGI behavioral response to cocaine Inferred from mutant phenotype PubMed 16014726. Source: MGI cellular response to catecholamine stimulus Inferred from electronic annotation. Source: Compara cerebral cortex GABAergic interneuron migration Inferred from mutant phenotype PubMed 17409246. Source: MGI conditioned taste aversion Inferred from mutant phenotype PubMed 15932618. Source: MGI dentate gyrus development Inferred from mutant phenotype PubMed 17360497. Source: MGI dopamine transport Inferred from mutant phenotype PubMed 11404425. Source: MGI elevation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Inferred from electronic annotation. Source: Compara glucose import Inferred from mutant phenotype PubMed 11251190. Source: MGI grooming behavior Inferred from mutant phenotype PubMed 9749770PubMed 9988094. Source: MGI long term synaptic depression Inferred from mutant phenotype PubMed 14981263. Source: MGI long-term synaptic potentiation Inferred from mutant phenotype PubMed 13679419PubMed 14981263PubMed 9427321. Source: MGI mating behavior Inferred from direct assay PubMed 9829800. Source: MGI memory Inferred from mutant phenotype PubMed 10585522. Source: MGI operant conditioning Inferred from mutant phenotype PubMed 12603275. Source: MGI peristalsis Inferred from genetic interaction PubMed 15272078. Source: MGI phospholipase C-activating dopamine receptor signaling pathway Inferred from direct assay PubMed 15016423. Source: MGI positive regulation of cell migration Inferred from mutant phenotype PubMed 17409246. Source: MGI positive regulation of release of sequestered calcium ion into cytosol Inferred from electronic annotation. Source: Compara positive regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype PubMed 8795639. Source: MGI protein import into nucleus Inferred from mutant phenotype PubMed 18496528. Source: MGI regulation of action potential in neuron Inferred from mutant phenotype PubMed 16908842. Source: MGI regulation of dopamine metabolic process Inferred from mutant phenotype PubMed 11438590. Source: MGI response to amphetamine Inferred from mutant phenotype PubMed 10222120PubMed 10661513PubMed 16014726PubMed 18486343PubMed 9261820. Source: MGI response to drug Inferred from direct assay PubMed 7549459. Source: MGI sensitization Inferred from genetic interaction PubMed 11823893. Source: MGI striatum development Inferred from mutant phenotype PubMed 17360497. Source: MGI synaptic transmission, dopaminergic Inferred from mutant phenotype PubMed 16908842. Source: MGI temperature homeostasis Inferred from mutant phenotype PubMed 18486343. Source: MGI visual learning Inferred from mutant phenotype PubMed 10585522PubMed 10884517PubMed 15684065PubMed 9692749. Source: MGI
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay PubMed 7809078PubMed 8738226PubMed 9016340. Source: MGI nucleus Inferred from direct assay PubMed 9387887. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dopamine binding Inferred from electronic annotation. Source: Compara dopamine neurotransmitter receptor activity, coupled via Gs Inferred from direct assay PubMed 11069937PubMed 12097513PubMed 12930822PubMed 16962565PubMed 7566118PubMed 7954836PubMed 8294904PubMed 8738226. Source: MGI
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_0000069375
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
	Sequence conflict	193 – 196	4	TYAI → DIRH Ref.3
	Sequence conflict	240	1	N → S in AAA16848. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q61616 [UniParc]. Last modified May 30, 2003. Version 2. Checksum: 509BA66F9DF82A74	FASTA	446	49,612
	10 20 30 40 50 60 MAPNTSTMDE TGLPVERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF RHLRSKVTNF 70 80 90 100 110 120 FVISLAVSDL LVAVLVMPWK AVAEIAGFWP FGSFCNIWVA FDIMCSTASI LNLCVISVDR 130 140 150 160 170 180 YWAISSPFQY ERKMTPKAAF ILISVAWTLS VLISFIPVQL SWHKAKPTWP LDGNFTSLED 190 200 210 220 230 240 AEDDNCDTRL SRTYAISSSL ISFYIPVAIM IVTYTSIYRI AQKQIRRISA LERAAVHAKN 250 260 270 280 290 300 CQTTTGNGNP VECSQSESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI SNCMVPFCGS 310 320 330 340 350 360 EETQPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFQKA FSTLLGCYRL CPTTNNAIET 370 380 390 400 410 420 VSINNNGAVM FSSHHEPRGS ISKDCNLVYL IPHAVGSSED LKREEAGGIP KPLEKLSPAL 430 440 SVILDYDTDV SLEKIQPVTH SGQHST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK044723 mRNA. Translation: BAC32050.1. BC137641 mRNA. Translation: AAI37642.1. BC137655 mRNA. Translation: AAI37656.1. L20336 mRNA. Translation: AAA16848.1.
IPI	IPI00123490.
RefSeq	NP_034206.1. NM_010076.3.
UniGene	Mm.54161.
3D structure databases
ProteinModelPortal	Q61616.
SMR	Q61616. Positions 28-346.
ModBase	Search...
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	Q61616.
Proteomic databases
PaxDb	Q61616.
PRIDE	Q61616.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021932; ENSMUSP00000021932; ENSMUSG00000021478.
GeneID	13488.
KEGG	mmu:13488.
UCSC	uc011yzm.1. mouse.
Organism-specific databases
CTD	13488.
MGI	MGI:99578. Drd1a.
Phylogenomic databases
eggNOG	NOG262978.
GeneTree	ENSGT00700000104081.
HOGENOM	HOG000239242.
HOVERGEN	HBG106962.
InParanoid	B2RPW8.
KO	K04144.
OMA	SPTTFDV.
OrthoDB	EOG4BG8W3.
Gene expression databases
ArrayExpress	Q61616.
Bgee	Q61616.
CleanEx	MM_DRD1A.
Genevestigator	Q61616.
GermOnline	ENSMUSG00000021478. Mus musculus.
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	Q61616.
ChEMBL	CHEMBL3071.
NextBio	283997.
SOURCE	Search...

Entry information

Entry name

DRD1_MOUSE

Accession

Primary (citable) accession number: Q61616
Secondary accession number(s): B2RPW8, Q8C8P8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 30, 2003
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program