Q24563 (DOPR2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dopamine receptor 2

Gene names

Name:	DopR2
Synonyms:	DAMB, DopR99B
ORF Names:	CG18741

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Receptor for dopamine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Also capable of generating a calcium signal. In terms of antagonist responses, would be classed with the D1-like dopamine receptor group. This receptor is an attractive candidate for initiating biochemical cascades underlying olfactory learning. Ref.1 Ref.2
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in both central and peripheral nervous systems. Ref.2
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-activating dopamine receptor signaling pathway Inferred from direct assay Ref.1. Source: FlyBase
Cellular_component	integral to plasma membrane Inferred from sequence model Ref.1. Source: FlyBase integral to synaptic vesicle membrane Inferred by curator Ref.2. Source: UniProtKB
Molecular_function	G-protein coupled amine receptor activity Inferred from sequence or structural similarity PubMed 12163486. Source: FlyBase adrenergic receptor activity Inferred from electronic annotation. Source: InterPro dopamine neurotransmitter receptor activity, coupled via Gs Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q24563-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: Q24563-2)

The sequence of this isoform differs from the canonical sequence as follows:
     511-539: RFATRRCYSTCSLHGIQHVRHNSCEQTYI → CHVAAAMVAASTSFGYHSVNQIDRTLM

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 539	539	Dopamine receptor 2		PRO_0000069370
Regions
	Topological domain	1 – 113	113	Extracellular Potential
	Transmembrane	114 – 134	21	Helical; Name=1; Potential
	Topological domain	135 – 145	11	Cytoplasmic Potential
	Transmembrane	146 – 166	21	Helical; Name=2; Potential
	Topological domain	167 – 189	23	Extracellular Potential
	Transmembrane	190 – 206	17	Helical; Name=3; Potential
	Topological domain	207 – 227	21	Cytoplasmic Potential
	Transmembrane	228 – 248	21	Helical; Name=4; Potential
	Topological domain	249 – 266	18	Extracellular Potential
	Transmembrane	267 – 287	21	Helical; Name=5; Potential
	Topological domain	288 – 420	133	Cytoplasmic Potential
	Transmembrane	421 – 441	21	Helical; Name=6; Potential
	Topological domain	442 – 453	12	Extracellular Potential
	Transmembrane	454 – 474	21	Helical; Name=7; Potential
	Topological domain	475 – 539	65	Cytoplasmic Potential
	Compositional bias	86 – 89	4	Poly-Gly
	Compositional bias	338 – 351	14	Poly-Gly
	Compositional bias	357 – 367	11	Poly-His
Amino acid modifications
	Lipidation	492	1	S-palmitoyl cysteine Potential
	Lipidation	493	1	S-palmitoyl cysteine Potential
	Glycosylation	5	1	N-linked (GlcNAc...) Potential
	Glycosylation	31	1	N-linked (GlcNAc...) Potential
	Glycosylation	47	1	N-linked (GlcNAc...) Potential
	Glycosylation	68	1	N-linked (GlcNAc...) Potential
	Disulfide bond	182 ↔ 261		By similarity
Natural variations
	Alternative sequence	511 – 539	29	RFATR…EQTYI → CHVAAAMVAASTSFGYHSVN QIDRTLM in isoform B.		VSP_001877
Experimental info
	Sequence conflict	496	1	K → E in AAQ23530. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 32FDDC0E935AF4B3	FASTA	539	59,505
	10 20 30 40 50 60 MVDDNGSSPE VEGAEGAGAP LLALLRVDGL NQTQTRSPSP SFFGSYNISE DVYFYFNGLP 70 80 90 100 110 120 TSTELVLNAT TSATSATLSP AMVATGGGGT TTPEPDLSEF LEALPNDRVG LLAFLFLFSF 130 140 150 160 170 180 ATVFGNSLVI LAVIRERYLH TATNYFITSL AVADCLVGLV VMPFSALYEV LENTWFFGTD 190 200 210 220 230 240 WCDIWRSLDV LFSTASILNL CVISLDRYWA ITDPFSYPMR MTVKRAAGLI AAVWICSSAI 250 260 270 280 290 300 SFPAIVWWRA ARDGEMPAYK CTFTEHLGYL VFSSTISFYL PLLVMVFTYC RIYRAAVIQT 310 320 330 340 350 360 RSLKIGTKQV LMASGELQLT LRIHRGGTTR DQQNQVSGGG GGGGGGGGGG GSLSHSHSHS 370 380 390 400 410 420 HHHHHNHGGG TTTSTPEEPD DEPLSALHNN GLARHRHMGK NFSLSRKLAK FAKEKKAAKT 430 440 450 460 470 480 LGIVMGVFII CWLPFFVVNL LSGFCIECIE HEEIVSAIVT WLGWINSCMN PVIYACWSRD 490 500 510 520 530 FRRAFVRLLC MCCPRKIRRK YQPTMRSKSQ RFATRRCYST CSLHGIQHVR HNSCEQTYI
	Isoform B [UniParc]. Checksum: AEF4599C3B65A22F	FASTA	537	58,919
	10 20 30 40 50 60 MVDDNGSSPE VEGAEGAGAP LLALLRVDGL NQTQTRSPSP SFFGSYNISE DVYFYFNGLP 70 80 90 100 110 120 TSTELVLNAT TSATSATLSP AMVATGGGGT TTPEPDLSEF LEALPNDRVG LLAFLFLFSF 130 140 150 160 170 180 ATVFGNSLVI LAVIRERYLH TATNYFITSL AVADCLVGLV VMPFSALYEV LENTWFFGTD 190 200 210 220 230 240 WCDIWRSLDV LFSTASILNL CVISLDRYWA ITDPFSYPMR MTVKRAAGLI AAVWICSSAI 250 260 270 280 290 300 SFPAIVWWRA ARDGEMPAYK CTFTEHLGYL VFSSTISFYL PLLVMVFTYC RIYRAAVIQT 310 320 330 340 350 360 RSLKIGTKQV LMASGELQLT LRIHRGGTTR DQQNQVSGGG GGGGGGGGGG GSLSHSHSHS 370 380 390 400 410 420 HHHHHNHGGG TTTSTPEEPD DEPLSALHNN GLARHRHMGK NFSLSRKLAK FAKEKKAAKT 430 440 450 460 470 480 LGIVMGVFII CWLPFFVVNL LSGFCIECIE HEEIVSAIVT WLGWINSCMN PVIYACWSRD 490 500 510 520 530 FRRAFVRLLC MCCPRKIRRK YQPTMRSKSQ CHVAAAMVAA STSFGYHSVN QIDRTLM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional characterization of a novel dopamine receptor from Drosophila melanogaster." Feng G., Hannan F., Reale V., Hon Y.Y., Kousky C.T., Evans P.D., Hall L.M. J. Neurosci. 16:3925-3933(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION. Strain: Canton-S. Tissue: Head.
[2]	"DAMB, a novel dopamine receptor expressed specifically in Drosophila mushroom bodies." Han K.-A., Millar N.S., Grotewiel M.S., Davis R.L. Neuron 16:1127-1135(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY. Strain: Canton-S.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[5]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B). Strain: Berkeley. Tissue: Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U34383 mRNA. Translation: AAC47161.1. U61264 mRNA. Translation: AAB08000.1. AE014297 Genomic DNA. Translation: AAF56908.2. AE014297 Genomic DNA. Translation: AAN14180.1. BT010212 mRNA. Translation: AAQ23530.1.
RefSeq	NP_524548.1. NM_079824.3. NP_733299.1. NM_170420.2.
UniGene	Dm.2334.
3D structure databases
ProteinModelPortal	Q24563.
SMR	Q24563. Positions 110-489.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-22945N.
MINT	MINT-969408.
Protein family/group databases
GPCRDB	Search...
Proteomic databases
PRIDE	Q24563.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0085468; FBpp0084834; FBgn0015129.
GeneID	43484.
KEGG	dme:Dmel_CG18741.
Organism-specific databases
CTD	43484.
FlyBase	FBgn0015129. DopR2.
Phylogenomic databases
eggNOG	NOG253615.
GeneTree	ENSGT00700000104182.
InParanoid	Q24563.
OMA	IAHEEIV.
OrthoDB	EOG4C2FRX.
PhylomeDB	Q24563.
Gene expression databases
Bgee	Q24563.
GermOnline	CG18741. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002233. Adrnrgc_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR01103. ADRENERGICR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	43484.
NextBio	834177.

Entry information

Entry name

DOPR2_DROME

Accession

Primary (citable) accession number: Q24563
Secondary accession number(s): Q24569, Q9VAJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project