ID   DRD1_CARAU              Reviewed;         363 AA.
AC   P35406;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=D(1) dopamine receptor;
DE   AltName: Full=Dopamine D1 receptor;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Retina;
RX   PubMed=8264547;
RA   Frail D.E., Manelli A.M., Witte D.G., Lin C.W., Steffey M.E.,
RA   MacKenzie R.G.;
RT   "Cloning and characterization of a truncated dopamine D1 receptor from
RT   goldfish retina: stimulation of cyclic AMP production and calcium
RT   mobilization.";
RL   Mol. Pharmacol. 44:1113-1118(1993).
CC   -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC       which activate adenylyl cyclase. Could be involved in growth hormone
CC       release.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Retina.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; L08602; AAA16322.1; -; Unassigned_DNA.
DR   PIR; I50475; I50475.
DR   AlphaFoldDB; P35406; -.
DR   SMR; P35406; -.
DR   BindingDB; P35406; -.
DR   ChEMBL; CHEMBL2368; -.
DR   Proteomes; UP000515129; Genome assembly.
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:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0065008; P:regulation of biological quality; IEA:UniProt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
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..363
FT                   /note="D(1) dopamine receptor"
FT                   /id="PRO_0000069379"
FT   TOPO_DOM        1..24
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..61
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..81
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..98
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..120
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..164
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..219
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..297
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..310
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..330
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        331..363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           345
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        7
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        97..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   363 AA;  40652 MW;  4B47FDE240D65DD0 CRC64;
     MAVLDLNLTT VIDSGFMESD RSVRVLTGCF LSVLILSTLL GNTLVCAAVT KFRHLRSKVT
     NFFVISLAVS DLLVAVLVMP WKAVTEVAGF WPFGAFCDIW VAFDIMCSTA SILNLCVISV
     DRYWAISSPF RYERKMTPRV AFVMISGAWT LSVLISFIPV QLKWHKAQPI GFLEVNASRR
     DLPTDNCDSS LNRTYAISSS LISFYIPVAI MIVTYTQIYR IAQKQIRRIS ALERAAESAQ
     IRHDSMGSGS NMDLESSFKL SFKRETKVLK TLSVIMGVFV CCWLPFFILN CMVPFCKRTS
     NGLPCISPTT FDVFVWFGWA NSSLNPIIYA FNADFRRAFA ILLGCQRLCP GSISMETPSL
     NKN