DRD3_CHLAE
ID DRD3_CHLAE Reviewed; 400 AA.
AC P52703;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=D(3) dopamine receptor;
DE AltName: Full=Dopamine D3 receptor;
GN Name=DRD3;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Ross P.C.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
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}.
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; U21307; AAA75379.1; -; mRNA.
DR PIR; G00013; G00013.
DR AlphaFoldDB; P52703; -.
DR SMR; P52703; -.
DR BindingDB; P52703; -.
DR ChEMBL; CHEMBL2304406; -.
DR DrugCentral; P52703; -.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:UniProt.
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; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..400
FT /note="D(3) dopamine receptor"
FT /id="PRO_0000069396"
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; 44336 MW; 9358843CB0BA698B CRC64;
MAPLSQLSGH LNYTCGVENS TGASQARPHA YYALSYCALI LAIVFGNGLV CMAVLKERAL
QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR VCCDVFVTLD VMMCTASILN
LCAISIDRYT AVVMPVHYQH GTGQSSCRRV TLMITAVWVL AFAVSCPLLF GFNTTGDPTV
CSISNPDFVI YSSVVSFYLP FGVTVLVYAR IYVVLKQRRR KRILTRQNSQ CNSVRPGFPQ
QTLSPDRAHL ELKRYYSICQ DTALGGPGFQ ERGGELKREE RTRNSLSPTI APKLSLEVRK
LSNGRLSTSL KLGPLQPRGV PLREKKATQM VAIVLGAFIV CWLPFFLTHV LNTHCQTCHV
SPELYSATTW LGYVNSALNP VIYTTFNIEF RKAFLKILSC
