ID   DRD2L_TAKRU             Reviewed;         463 AA.
AC   P53453;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=D(2)-like dopamine receptor;
GN   Name=d215;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7789977; DOI=10.1016/0888-7543(95)80044-m;
RA   Machae A.D., Brenner S.;
RT   "Analysis of the dopamine receptor family in the compact genome of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 25:436-446(1995).
CC   -!- FUNCTION: Receptor for dopamine.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X80175; CAA56456.1; -; Genomic_DNA.
DR   RefSeq; XP_003968417.1; XM_003968368.2.
DR   AlphaFoldDB; P53453; -.
DR   SMR; P53453; -.
DR   STRING; 31033.ENSTRUP00000037540; -.
DR   Ensembl; ENSTRUT00000037674; ENSTRUP00000037539; ENSTRUG00000014690.
DR   GeneID; 101074274; -.
DR   KEGG; tru:101074274; -.
DR   CTD; 282557; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000155539; -.
DR   InParanoid; P53453; -.
DR   Proteomes; UP000005226; Chromosome 11.
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: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:0065008; P:regulation of biological quality; IEA:UniProt.
DR   GO; GO:1903530; P:regulation of secretion by cell; IEA:UniProt.
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; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..463
FT                   /note="D(2)-like dopamine receptor"
FT                   /id="PRO_0000069392"
FT   TOPO_DOM        1..35
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        36..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        59..68
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        69..91
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        92..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        107..128
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        129..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        150..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        171..189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        190..214
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        215..392
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        393..414
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        415..429
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        430..451
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        452..463
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          295..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        16
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        22
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        418..421
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   463 AA;  52120 MW;  A54B178D7718AF6B CRC64;
     MDVFTQYAYN DSIFDNGTWS ANETTKDETH PYNYYAMLLT LLIFVIVFGN VLVCMAVSRE
     KALQTTTNYL IVSLAVADLL VATLVMPWVV YLEVVGEWRF SKIHCDIFVT LDVMMCTASI
     LNLCAISIDR YTAVAMPMLY NTRYSSRRRV TVMISVVWVL SFAISCPLLF GLNNTATRDQ
     SLCFIANPAF VVYSSIVSFY VPFIVTLLVY VQIYVVLRKR RKRVNTKPKQ RLCQAADPDI
     PTSLKDKCTH PEDVRLCTMI VKSNGSFPVN KKKVIFIKDG VNEVEGLELD ELNYCGGSHK
     QPPPQQQPRA LGDTPATSHQ LLMSTKANAS PTSTPPTPPE EGQRTEKNGD PTKEAQGNPA
     PVVALRNGKT QTSLKTLSKR KISQQKEKKA TQMLAIVLGV FIICWLPFFI THILNTHCTR
     CKVPAEMYNA FTWLGYVNSA VNPIIYTTFN VEFRKAFIKI LHC