ID   DRD1C_XENLA             Reviewed;         465 AA.
AC   P42291;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=D(1C) dopamine receptor;
GN   Name=drd1c;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7937989; DOI=10.1073/pnas.91.22.10536;
RA   Sugamori K.S., Demchyshyn L.L., Chung M., Niznik H.B.;
RT   "D1A, D1B, and D1C dopamine receptors from Xenopus laevis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:10536-10540(1994).
CC   -!- FUNCTION: This is one of the five types (D1 to D5) of receptors for
CC       dopamine. The activity of this receptor is mediated by G proteins which
CC       activate adenylyl cyclase.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain and kidney.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U07865; AAA50830.1; -; Genomic_DNA.
DR   PIR; I51661; I51661.
DR   AlphaFoldDB; P42291; -.
DR   SMR; P42291; -.
DR   Proteomes; UP000186698; 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..465
FT                   /note="D(1C) dopamine receptor"
FT                   /id="PRO_0000069381"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..54
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..92
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..124
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..168
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..219
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..264
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..291
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..309
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..334
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..465
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   LIPID           344
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        101..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   465 AA;  52641 MW;  F41DF85AF0D2F869 CRC64;
     MENFSIFNVT VNVWHADLDV GNSDLSLRAL TGLLLSLLIL STLLGNTLVC LAVIKFRHLR
     SKVTNFFVIS LAVSDLFVAL LVMPWKAVTE VAGFWVFGDF CDTWVAFDIM CSTASILNLC
     IISLDRYWAI ASPFRYERKM TQRVAFIMIG VAWTLSILIS FIPVQLSWHK SHEADEELNG
     VNHTENCDSS LNRTYAISSS LISFYIPVVI MIGTYTRIYR IAQTQIRRIS SLERAVEHAQ
     RCSSRLSNEN SLKTSFRKET KVLKTLSIIM GVFVFCWLPF FVLNCMIPFC HMNLPGQNEP
     EPPCVSETTF NIFVWFGWAN SSLNPVIYAF NADFRKAFTT ILGCNRFCSS NNVEAVNFSN
     ELVSYHHDTT FQKDIPVTFN NSHLPNVVDQ DQEVLEGTCF DKVSVLSTSH GTRSQKNLHL
     PAGVQFECEA EITLETITPF TSTGPLECLP QLVADEDRHY TTKLY