DOPR1_DROME
ID DOPR1_DROME Reviewed; 511 AA.
AC P41596; A4VCK3; E1JIK5; Q24038; Q9VFM1; S4X4E2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Dopamine receptor 1;
DE Short=D-DOP1;
DE Short=DmDop1;
DE Short=dDA1;
DE AltName: Full=Dopamine 1-like receptor 1;
DE Flags: Precursor;
GN Name=Dop1R1; Synonyms=DopR, DopR1, DopR35EF; ORFNames=CG9652;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Berlin; TISSUE=Head;
RX PubMed=7953290;
RA Gotzes F., Balfanz S., Baumann A.;
RT "Primary structure and functional characterization of a Drosophila dopamine
RT receptor with high homology to human D1/5 receptors.";
RL Recept. Channels 2:131-141(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley;
RA Stapleton M., Booth B., Carlson J.W., Frise E., Kapadia B., Park S.,
RA Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF N-TERMINUS, FUNCTION,
RP AND VARIANTS LEU-60 AND ILE-69.
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=8630055; DOI=10.1006/bbrc.1996.0708;
RA Gotzes F., Baumann A.;
RT "Functional properties of Drosophila dopamine D1-receptors are not altered
RT by the size of the N-terminus.";
RL Biochem. Biophys. Res. Commun. 222:121-126(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 127-511 (ISOFORM A), FUNCTION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=7720859; DOI=10.1016/0014-5793(95)00224-w;
RA Sugamori K.S., Demchyshyn L.L., McConkey F., Forte M.A., Niznik H.B.;
RT "A primordial dopamine D1-like adenylyl cyclase-linked receptor from
RT Drosophila melanogaster displaying poor affinity for benzazepines.";
RL FEBS Lett. 362:131-138(1995).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12711555; DOI=10.1016/s1567-133x(02)00098-4;
RA Kim Y.-C., Lee H.-G., Seong C.-S., Han K.-A.;
RT "Expression of a D1 dopamine receptor dDA1/DmDOP1 in the central nervous
RT system of Drosophila melanogaster.";
RL Gene Expr. Patterns 3:237-245(2003).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17634358; DOI=10.1523/jneurosci.1167-07.2007;
RA Kim Y.-C., Lee H.-G., Han K.-A.;
RT "D1 dopamine receptor dDA1 is required in the mushroom body neurons for
RT aversive and appetitive learning in Drosophila.";
RL J. Neurosci. 27:7640-7647(2007).
RN [9]
RP FUNCTION.
RX PubMed=18674913; DOI=10.1016/j.cub.2008.07.028;
RA Seugnet L., Suzuki Y., Vine L., Gottschalk L., Shaw P.J.;
RT "D1 receptor activation in the mushroom bodies rescues sleep-loss-induced
RT learning impairments in Drosophila.";
RL Curr. Biol. 18:1110-1117(2008).
CC -!- FUNCTION: Receptor for dopamine. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase. Might be
CC involved in the processing of visual information and/or visual
CC learning. Important for Pavlovian conditioning: required in the
CC mushroom body as a receptor conveying unconditional stimuli
CC information, has a role in memory formation for aversive and appetitive
CC learning. Sleep-deprivation-induced impairments in learning can be
CC partially explained through alterations in dopamine signaling, Dop1R1
CC expression levels are reduced; sleep may have a role in restoring
CC dopamine homeostasis. {ECO:0000269|PubMed:17634358,
CC ECO:0000269|PubMed:18674913, ECO:0000269|PubMed:7720859,
CC ECO:0000269|PubMed:7953290, ECO:0000269|PubMed:8630055}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=P41596-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P41596-2; Sequence=VSP_037471;
CC Name=C;
CC IsoId=P41596-3; Sequence=VSP_053645, VSP_037471;
CC -!- TISSUE SPECIFICITY: Expressed in the larval and adult CNS in structures
CC that mediate higher-order brain functions such as learning, memory and
CC motor control: in the mushroom body neuropil and four unpaired neurons
CC in each thoracic segment. The adult CNS has intense expression in the
CC central complex, moderate expression in several neurosecretory cells,
CC and weak expression in two unpaired neurons in the mesothoracic
CC neuromere. Also seen in the somata of the optic lobes.
CC {ECO:0000269|PubMed:12711555, ECO:0000269|PubMed:17634358,
CC ECO:0000269|PubMed:7953290}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:7720859}.
CC -!- MISCELLANEOUS: Potency of neurotransmitter agonists in stimulating cAMP
CC production and the lack of stimulation by other transmitters and
CC metabolites suggests this is a D1-like receptor. Low homology to
CC vertebrate D1 receptors suggests this may be a progenitor of the D1
CC receptor subfamily.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X77234; CAA54451.1; -; mRNA.
DR EMBL; AE014297; AAF55030.3; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94904.1; -; Genomic_DNA.
DR EMBL; BT030444; ABP87886.1; -; mRNA.
DR EMBL; BT150144; AGP25446.1; -; mRNA.
DR EMBL; U22106; AAA85716.1; -; mRNA.
DR PIR; S44275; S44275.
DR PIR; S68780; S68780.
DR RefSeq; NP_001163607.1; NM_001170136.2. [P41596-3]
DR RefSeq; NP_001247092.1; NM_001260163.1. [P41596-1]
DR RefSeq; NP_477007.2; NM_057659.4.
DR AlphaFoldDB; P41596; -.
DR SMR; P41596; -.
DR BioGRID; 66803; 3.
DR STRING; 7227.FBpp0300511; -.
DR GlyGen; P41596; 5 sites.
DR PaxDb; P41596; -.
DR PRIDE; P41596; -.
DR DNASU; 41726; -.
DR EnsemblMetazoa; FBtr0301351; FBpp0290565; FBgn0011582. [P41596-3]
DR EnsemblMetazoa; FBtr0308191; FBpp0300511; FBgn0011582. [P41596-1]
DR GeneID; 41726; -.
DR KEGG; dme:Dmel_CG9652; -.
DR CTD; 41726; -.
DR FlyBase; FBgn0011582; Dop1R1.
DR VEuPathDB; VectorBase:FBgn0011582; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154484; -.
DR InParanoid; P41596; -.
DR OMA; DCKAKPS; -.
DR PhylomeDB; P41596; -.
DR Reactome; R-DME-381753; Olfactory Signaling Pathway.
DR Reactome; R-DME-390666; Serotonin receptors.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 41726; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41726; -.
DR PRO; PR:P41596; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0011582; Expressed in brain and 5 other tissues.
DR ExpressionAtlas; P41596; baseline and differential.
DR Genevisible; P41596; DM.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; ISS:FlyBase.
DR GO; GO:0001588; F:dopamine neurotransmitter receptor activity, coupled via Gs; IDA:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:FlyBase.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0008306; P:associative learning; IMP:UniProtKB.
DR GO; GO:0071329; P:cellular response to sucrose stimulus; IDA:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISS:FlyBase.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0007612; P:learning; IMP:FlyBase.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0090328; P:regulation of olfactory learning; IMP:FlyBase.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IMP:FlyBase.
DR GO; GO:1990834; P:response to odorant; IMP:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR GO; GO:0009744; P:response to sucrose; IMP:FlyBase.
DR GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR GO; GO:0043052; P:thermotaxis; IMP:FlyBase.
DR GO; GO:0008542; P:visual learning; IMP:UniProtKB.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00242; DOPAMINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..511
FT /note="Dopamine receptor 1"
FT /id="PRO_0000012718"
FT TOPO_DOM 20..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..169
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..206
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..239
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..450
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 468
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 469
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 216..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_053645"
FT VAR_SEQ 133..147
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_037471"
FT VARIANT 60
FT /note="I -> L (in strain: Canton-S)"
FT /evidence="ECO:0000269|PubMed:8630055"
FT VARIANT 69
FT /note="T -> I (in strain: Canton-S)"
FT /evidence="ECO:0000269|PubMed:8630055"
FT CONFLICT 109
FT /note="G -> V (in Ref. 4; ABP87886)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..172
FT /note="ER -> DG (in Ref. 1; CAA54451)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="R -> P (in Ref. 1; CAA54451)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="Y -> D (in Ref. 4; ABP87886)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="A -> T (in Ref. 4; ABP87886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56170 MW; F044C00EDBF14749 CRC64;
MYTPHPFGFL IILVPMTNAM RAIAAIAAGV GSVAATVATS TTSSISSSTT IINTSSATTI
GGNHTSGSTG FSTNSTLLDA DHLPLQLTTA KVDLDIEIDI QLLTNGYDGT TLTSFYNESS
WTNASEMDTI VGEEPEPLSL VSIVVVGIFL SVLIFLSVAG NILVCLAIYT ERSLRRIGNL
FLASLAIADL FVASLVMTFA GVNDLLGYWI FGAQFCDTWV AFDVMCSTAS ILNLCAISMD
RYIHIKDPLR YGRWVTRRVA VITIAAIWLL AAFVSFVPIS LGIHRPDQPL IFEDNGKKYP
TCALDLTPTY AVVSSCISFY FPCVVMIGIY CRLYCYAQKH VKSIKAVTRP GEVAEKQRYK
SIRRPKNQPK KFKVRNLHTH SSPYHVSDHK AAVTVGVIMG VFLICWVPFF CVNITAAFCK
TCIGGQTFKI LTWLGYSNSA FNPIIYSIFN KEFRDAFKRI LTMRNPWCCA QDVGNIHPRN
SDRFITDYAA KNVVVMNSGR SSAELEQVSA I
