DRD1_PIG
ID DRD1_PIG Reviewed; 446 AA.
AC P50130;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=D(1A) dopamine receptor;
DE AltName: Full=Dopamine D1 receptor;
GN Name=DRD1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7900842; DOI=10.1152/ajprenal.1995.268.3.f423;
RA Grenader A.C., O'Rourke D.A., Healy D.P.;
RT "Cloning of the porcine D1A dopamine receptor gene expressed in renal
RT epithelial LLC-PK1 cells.";
RL Am. J. Physiol. 268:F423-F434(1995).
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 (By similarity).
CC Interacts with DRD2 (By similarity). {ECO:0000250|UniProtKB:P18901,
CC ECO:0000250|UniProtKB:Q61616}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18901};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P18901}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P18901}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P18901}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q61616}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q61616}. Note=Transport from the endoplasmic
CC reticulum to the cell surface is regulated by interaction with DNAJC14.
CC {ECO:0000250|UniProtKB:P18901}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U25681; AAA79848.1; -; Genomic_DNA.
DR PIR; I47217; I47217.
DR RefSeq; NP_001116580.1; NM_001123108.1.
DR AlphaFoldDB; P50130; -.
DR SMR; P50130; -.
DR STRING; 9823.ENSSSCP00000020447; -.
DR BindingDB; P50130; -.
DR ChEMBL; CHEMBL5067; -.
DR DrugCentral; P50130; -.
DR PaxDb; P50130; -.
DR PRIDE; P50130; -.
DR GeneID; 100144487; -.
DR KEGG; ssc:100144487; -.
DR CTD; 1812; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P50130; -.
DR PRO; PR:P50130; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
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:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0042311; P:vasodilation; IEA:InterPro.
DR InterPro; IPR001413; Dopamine_D1_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; PR00565; DOPAMINED1AR.
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; Cell projection; Disulfide bond; Endoplasmic reticulum;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..446
FT /note="D(1A) dopamine receptor"
FT /id="PRO_0000069376"
FT TOPO_DOM 1..23
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..163
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..337
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 347
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 351
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 446 AA; 49257 MW; A56BFA0D93D50DBB CRC64;
MRTLNTSTMD GTGLVVERDF SFRILTACFL SLLILSTLLG NTLVCAAVIR FRHLRSKVTN
FFVISLAVSD LLVAVLVMPW KAVAEIAGFW PFGSFCNIWV AFDIMCSTAS ILNLCVISVD
RYWAISSPFR YERKMTPKAA FILISVAWTL SVLISFIPVQ LSWHKAKPTS PSDGNVTSLG
KTTHNCDSSL SRTYAISSSL ISFYIPVAIM IVTYTRIYRI AQKQIRRISA LERAAVHAKN
CQTTAGNGNP AECSQPESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI LNCMVPFCGS
GETKPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFRKA FSTLLGCYRL CPTSTNAIET
VSINNNGAVV FSSHHEPRGS ISKDCNLVYL IPHAVGSSED LKKEEAGGIA SPLEKLSPAL
SVILDYDTDV SLEKIQPITQ NGQHPT
