ID   DRD1_RABIT              Reviewed;         180 AA.
AC   O02664;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=D(1A) dopamine receptor;
DE   AltName: Full=Dopamine D1 receptor;
DE   Flags: Fragment;
GN   Name=DRD1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=New Zealand;
RX   PubMed=9700720; DOI=10.1016/s0168-0102(98)00033-9;
RA   Bairam A., Frenette J., Dauphin C., Carroll J.L., Khandjian E.W.;
RT   "Expression of dopamine D1-receptor mRNA in the carotid body of adult
RT   rabbits, cats and rats.";
RL   Neurosci. Res. 31:147-154(1998).
CC   -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC       which activate adenylyl cyclase.
CC   -!- SUBUNIT: Interacts with DNAJC14 via its C-terminus. Interacts with
CC       DRD1IP. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}. Note=Transport from the
CC       endoplasmic reticulum to the cell surface is regulated by interaction
CC       with DNAJC14. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; Y10662; CAA71671.1; -; Genomic_DNA.
DR   STRING; 9986.ENSOCUP00000004170; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; O02664; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum 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:0004952; F:dopamine neurotransmitter receptor activity; IEA:UniProt.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007610; P:behavior; IEA:UniProt.
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   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; Endoplasmic reticulum;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..>180
FT                   /note="D(1A) dopamine receptor"
FT                   /id="PRO_0000069377"
FT   TRANSMEM        <1..10
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        11..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        22..48
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..80
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..124
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..153
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..179
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..>180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        57..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   NON_TER         1
FT   NON_TER         180
SQ   SEQUENCE   180 AA;  20114 MW;  54F74D7CFB4EB671 CRC64;
     NTLLVCAAVI RFRHLRSKVT NFFVISLAVS DLLVAVLVMP WKAVAEIAGF WPFGSFCNIW
     VAFDIMCSTA SILNLCVISV DRYWAISSPF RYERKMTPKA AFILIGVAWT LSVLISFIPV
     QLSWHKAKPT SPPDGNATSL DETVDNCDSS LSRTYSISSS LVNFYNPVAI MXVTYTRIHR