DRD2_MELGA
ID DRD2_MELGA Reviewed; 436 AA.
AC O73810;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=D(2) dopamine receptor;
DE AltName: Full=Dopamine D2 receptor;
GN Name=DRD2;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Nicholas large white; TISSUE=Brain;
RA Schnell S.A., You S., Foster D.N., el Halawani M.E.;
RT "Molecular cloning and tissue distribution of an avian D2 dopamine receptor
RT from the domestic turkey (Meleagris gallopavo).";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC which inhibit adenylyl cyclase (By similarity). Positively regulates
CC postnatal regression of retinal hyaloid vessels via suppression of
CC VEGFR2/KDR activity, downstream of OPN5 (By similarity).
CC {ECO:0000250|UniProtKB:P14416, ECO:0000250|UniProtKB:P61168}.
CC -!- SUBUNIT: Forms homo- and heterooligomers with DRD4. The interaction
CC with DRD4 may modulate agonist-induced downstream signaling. Interacts
CC with CADPS and CADPS2 (By similarity). Interacts with GPRASP1, PPP1R9B
CC and CLIC6. Interacts with ARRB2 (By similarity). Interacts with HTR2A
CC (By similarity). Interacts with DRD1. Interacts with KCNA2 (By
CC similarity). {ECO:0000250|UniProtKB:P14416,
CC ECO:0000250|UniProtKB:P61168, ECO:0000250|UniProtKB:P61169}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14416};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Palmitoylated. Palmitoylation which is required for proper
CC localization to the plasma membrane and stability of the receptor could
CC be carried on by ZDHHC4, ZDHHC3 and ZDHHC8.
CC {ECO:0000250|UniProtKB:P14416}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF056201; AAD03818.1; -; mRNA.
DR RefSeq; NP_001290091.1; NM_001303162.1.
DR AlphaFoldDB; O73810; -.
DR SMR; O73810; -.
DR GeneID; 100303660; -.
DR KEGG; mgp:100303660; -.
DR CTD; 1813; -.
DR InParanoid; O73810; -.
DR OrthoDB; 384993at2759; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0035240; F:dopamine binding; NAS:AgBase.
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:0038023; F:signaling receptor activity; TAS:AgBase.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IEA:InterPro.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISS:UniProtKB.
DR GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; IMP:AgBase.
DR GO; GO:0090278; P:negative regulation of peptide hormone secretion; TAS:AgBase.
DR InterPro; IPR001922; Dopamine_D2_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; PR00567; DOPAMINED2R.
DR PRINTS; PR00242; DOPAMINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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 Golgi apparatus; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..436
FT /note="D(2) dopamine receptor"
FT /id="PRO_0000069391"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 35..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 58..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 68..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 91..105
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 106..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 128..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 149..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 170..185
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 186..210
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 211..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 367..388
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 389..402
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 403..424
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 425..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 221..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 436
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14416"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 392..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 436 AA; 49389 MW; 5FB13F684532C53B CRC64;
MDPLNLSWYN TGDRNWSEPV NESSADQKPQ YNYYAVLLTL LIFVIVFGNV LVCMAVSREK
ALQTTTNYLI VSLAVADLLV ATLVMPWVVY LEVVGEWRFS RIHCDIFVTL DVMMCTASIL
NLCAISIDRY TAAAMPMLYN TRYSSKRRVT VMIACVWVLS FAISSPILFG LNKADERECI
IANPAFVVYS SVVSFYVPFI VTLLVYVQIY MVLRRRRKRH TKRSSHGLDS DTHAPLKDKC
THPENVKLGT VIVKSNGSFQ VNKRKCEAES HIKMEMEMMS STSPPERTIV KAAAPSNHQL
VVPVASSRST LDSPGKVEKN GHAKENLHTA KVFEIQSMPN GKTRSTLLKA MNRRKLSQQK
EKKATQMLAI VLGVFIICWL PFFITHILNM HCDCNIPPAM YSAFTWLGYV NSAVNPIIYT
TFNIEFRKAF MKILHC
