DRD3_RAT
ID DRD3_RAT Reviewed; 446 AA.
AC P19020; P70647;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=D(3) dopamine receptor;
DE AltName: Full=Dopamine D3 receptor;
GN Name=Drd3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=1975644; DOI=10.1038/347146a0;
RA Sokoloff P., Giros B., Martres M.-P., Bouthenet M.-L., Schwartz J.-C.;
RT "Molecular cloning and characterization of a novel dopamine receptor (D3)
RT as a target for neuroleptics.";
RL Nature 347:146-151(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=2039532; DOI=10.1016/0006-291x(91)90469-n;
RA Giros B., Martres M.-P., Pilon C., Sokoloff P., Schwartz J.-C.;
RT "Shorter variants of the D3 dopamine receptor produced through various
RT patterns of alternative splicing.";
RL Biochem. Biophys. Res. Commun. 176:1584-1592(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-106.
RX PubMed=8333859; DOI=10.1006/bbrc.1993.1842;
RA Pagliusi S., Chollet-Daemerius A., Losberger C., Mills A., Kawashima E.;
RT "Characterization of a novel exon within the D3 receptor gene giving rise
RT to an mRNA isoform expressed in rat brain.";
RL Biochem. Biophys. Res. Commun. 194:465-471(1993).
RN [4]
RP INTERACTION WITH CLIC6.
RX PubMed=14499480; DOI=10.1016/s0169-328x(03)00283-3;
RA Griffon N., Jeanneteau F., Prieur F., Diaz J., Sokoloff P.;
RT "CLIC6, a member of the intracellular chloride channel family, interacts
RT with dopamine D(2)-like receptors.";
RL Brain Res. Mol. Brain Res. 117:47-57(2003).
RN [5]
RP 3D-STRUCTURE MODELING.
RC TISSUE=Brain;
RX PubMed=1358063; DOI=10.1042/bj2870277;
RA Livingstone C.D., Strange P.G., Naylor L.H.;
RT "Molecular modelling of D2-like dopamine receptors.";
RL Biochem. J. 287:277-282(1992).
CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC which inhibit adenylyl cyclase. Promotes cell proliferation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CLIC6 (PubMed:14499480). Interacts with GRK4.
CC Interacts with PALM. Interacts with FLNA (via filamin repeat 21);
CC increases PKA-mediated phosphorylation of FLNA (By similarity).
CC {ECO:0000250|UniProtKB:P35462, ECO:0000269|PubMed:14499480}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P19020-1; Sequence=Displayed;
CC Name=D3(TM3-del);
CC IsoId=P19020-2; Sequence=VSP_001874, VSP_001875;
CC Name=D3(O2-DEL);
CC IsoId=P19020-3; Sequence=VSP_001876;
CC -!- TISSUE SPECIFICITY: Mainly in limbic areas of brain.
CC -!- PTM: Phosphorylated by GRK4. {ECO:0000250|UniProtKB:P35462}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:P35462}.
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; X53944; CAA37887.1; -; mRNA.
DR EMBL; M69194; AAA41076.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M69189; AAA41076.1; JOINED; Genomic_DNA.
DR EMBL; M69190; AAA41076.1; JOINED; Genomic_DNA.
DR EMBL; M69191; AAA41076.1; JOINED; Genomic_DNA.
DR EMBL; M69192; AAA41076.1; JOINED; Genomic_DNA.
DR EMBL; M69193; AAA41076.1; JOINED; Genomic_DNA.
DR EMBL; S63847; AAB27545.1; -; Genomic_DNA.
DR EMBL; S63846; AAB27545.1; JOINED; Genomic_DNA.
DR PIR; S11565; DYRTD3.
DR RefSeq; NP_058836.1; NM_017140.2. [P19020-1]
DR AlphaFoldDB; P19020; -.
DR SMR; P19020; -.
DR STRING; 10116.ENSRNOP00000031550; -.
DR BindingDB; P19020; -.
DR ChEMBL; CHEMBL3138; -.
DR DrugCentral; P19020; -.
DR GuidetoPHARMACOLOGY; 216; -.
DR GlyGen; P19020; 4 sites.
DR iPTMnet; P19020; -.
DR PhosphoSitePlus; P19020; -.
DR PaxDb; P19020; -.
DR PRIDE; P19020; -.
DR GeneID; 29238; -.
DR KEGG; rno:29238; -.
DR UCSC; RGD:2521; rat. [P19020-1]
DR CTD; 1814; -.
DR RGD; 2521; Drd3.
DR VEuPathDB; HostDB:ENSRNOG00000060806; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P19020; -.
DR OMA; YYSICQG; -.
DR OrthoDB; 384993at2759; -.
DR PhylomeDB; P19020; -.
DR TreeFam; TF334382; -.
DR Reactome; R-RNO-390651; Dopamine receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P19020; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000060806; Expressed in Ammon's horn and 1 other tissue.
DR Genevisible; P19020; RN.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:RGD.
DR GO; GO:0030139; C:endocytic vesicle; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; TAS:RGD.
DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IDA:BHF-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0046717; P:acid secretion; IDA:BHF-UCL.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050482; P:arachidonic acid secretion; ISO:RGD.
DR GO; GO:0006914; P:autophagy; IMP:RGD.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISO:RGD.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; TAS:RGD.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0035483; P:gastric emptying; IMP:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; ISO:RGD.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:RGD.
DR GO; GO:0032416; P:negative regulation of sodium:proton antiporter activity; IMP:RGD.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:RGD.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:BHF-UCL.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IDA:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0060134; P:prepulse inhibition; ISO:RGD.
DR GO; GO:0002016; P:regulation of blood volume by renin-angiotensin; ISO:RGD.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:RGD.
DR GO; GO:0040012; P:regulation of locomotion; IMP:RGD.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IMP:RGD.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0051580; P:regulation of neurotransmitter uptake; ISO:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0043266; P:regulation of potassium ion transport; IBA:GO_Central.
DR GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; ISO:RGD.
DR GO; GO:0034776; P:response to histamine; ISO:RGD.
DR GO; GO:0043278; P:response to morphine; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:BHF-UCL.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR InterPro; IPR001620; Dopamine_D3_rcpt.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00568; DOPAMINED3R.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..446
FT /note="D(3) dopamine receptor"
FT /id="PRO_0000069400"
FT TRANSMEM 33..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 66..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 188..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 376..397
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 413..432
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 401..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 92..100
FT /note="TGGVWNFSR -> HSGGHASSL (in isoform D3(TM3-del))"
FT /evidence="ECO:0000305"
FT /id="VSP_001874"
FT VAR_SEQ 101..446
FT /note="Missing (in isoform D3(TM3-del))"
FT /evidence="ECO:0000305"
FT /id="VSP_001875"
FT VAR_SEQ 176..193
FT /note="Missing (in isoform D3(O2-DEL))"
FT /evidence="ECO:0000305"
FT /id="VSP_001876"
FT CONFLICT 71
FT /note="L -> M (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Q -> E (in Ref. 2; AAA41076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 49516 MW; 180E36AFF217E9DB CRC64;
MAPLSQISTH LNSTCGAENS TGVNRARPHA YYALSYCALI LAIIFGNGLV CAAVLRERAL
QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR ICCDVFVTLD VMMCTASILN
LCAISIDRYT AVVMPVHYQH GTGQSSCRRV ALMITAVWVL AFAVSCPLLF GFNTTGDPSI
CSISNPDFVI YSSVVSFYVP FGVTVLVYAR IYIVLRQRQR KRILTRQNSQ CISIRPGFPQ
QSSCLRLHPI RQFSIRARFL SDATGQMEHI EDKQYPQKCQ DPLLSHLQPP SPGQTHGGLK
RYYSICQDTA LRHPSLEGGA GMSPVERTRN SLSPTMAPKL SLEVRKLSNG RLSTSLRLGP
LQPRGVPLRE KKATQMVVIV LGAFIVCWLP FFLTHVLNTH CQACHVSPEL YRATTWLGYV
NSALNPVIYT TFNVEFRKAF LKILSC
