DRD3_PANTR
ID DRD3_PANTR Reviewed; 400 AA.
AC Q5IS72;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=D(3) dopamine receptor;
DE AltName: Full=Dopamine D3 receptor;
GN Name=DRD3;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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 (By similarity). 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:P19020, ECO:0000250|UniProtKB:P35462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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}.
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DR EMBL; AY665256; AAV74294.1; -; mRNA.
DR RefSeq; NP_001029084.1; NM_001033912.1.
DR RefSeq; XP_009444264.1; XM_009445989.2.
DR AlphaFoldDB; Q5IS72; -.
DR SMR; Q5IS72; -.
DR STRING; 9598.ENSPTRP00000026285; -.
DR PaxDb; Q5IS72; -.
DR Ensembl; ENSPTRT00000076619; ENSPTRP00000062496; ENSPTRG00000015241.
DR GeneID; 470885; -.
DR KEGG; ptr:470885; -.
DR CTD; 1814; -.
DR VGNC; VGNC:1797; DRD3.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000159661; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; Q5IS72; -.
DR OrthoDB; 384993at2759; -.
DR TreeFam; TF334382; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000015241; Expressed in dorsolateral prefrontal cortex and 2 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IEA:Ensembl.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
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:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
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:0060134; P:prepulse inhibition; IEA:Ensembl.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0043266; P:regulation of potassium ion transport; IBA:GO_Central.
DR GO; GO:0034776; P:response to histamine; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..400
FT /note="D(3) dopamine receptor"
FT /id="PRO_0000069399"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 33..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TOPO_DOM 56..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 66..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TOPO_DOM 89..104
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TOPO_DOM 127..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TOPO_DOM 171..187
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 188..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TOPO_DOM 210..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 330..351
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TOPO_DOM 352..366
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TRANSMEM 367..386
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P35462"
FT TOPO_DOM 387..400
FT /note="Cytoplasmic"
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 355..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 400 AA; 44237 MW; 1F77A2B82B7FED9F CRC64;
MAPLSQLSGH LNYTCGAENS TGASQARPHA YYALSYCALI LAIVFGNGLV CMAVLKERAL
QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR ICCDVFVTLD VMMCTASILN
LCAISIDRYT AVVMPVHYQH GTGQSSCRRV ALMITAVWVL AFAVSCPLLF GFNTTGDPTV
CSISNPDFVI YSSVVSFYLP FGVTVLVYAR IYMVLKQRRR KRILTRQNSQ CNSVRPGFPQ
QTLSPDPAHL ELKRYYSICQ DTALGGPGFQ ERGGELKREE KTRNSLSPTI APKLSLEVRK
LSNGRLSTSL KLGPLQPRGV PLREKKATQM VAIVLGAFIV CWLPFFLTHV LNTHCQTCHV
SPELYSATTW LGYVNSALNP VIYTTFNIEF RKAFLKILSC
