DRD1_BOVIN
ID DRD1_BOVIN Reviewed; 446 AA.
AC Q95136; A4IFG9; Q8WND7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=D(1A) dopamine receptor;
DE AltName: Full=Dopamine D1 receptor;
GN Name=DRD1; Synonyms=D1AR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12873217; DOI=10.1046/j.1365-2052.2003.00994.x;
RA Haegeman A., Williams J.L., Law A., Van Zeveren A., Peelman L.J.;
RT "Characterization and mapping of bovine dopamine receptors 1 and 5.";
RL Anim. Genet. 34:290-293(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-277.
RA Gibert J.-M., Botteri C., Cardinaud B., Vernier P.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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; AF381032; AAL37945.1; -; mRNA.
DR EMBL; BC134576; AAI34577.1; -; mRNA.
DR EMBL; U73042; AAB17281.1; -; Genomic_DNA.
DR RefSeq; NP_776467.1; NM_174042.2.
DR RefSeq; XP_005211234.1; XM_005211177.3.
DR RefSeq; XP_005211235.1; XM_005211178.3.
DR AlphaFoldDB; Q95136; -.
DR SMR; Q95136; -.
DR STRING; 9913.ENSBTAP00000054107; -.
DR BindingDB; Q95136; -.
DR ChEMBL; CHEMBL2967; -.
DR DrugCentral; Q95136; -.
DR PaxDb; Q95136; -.
DR Ensembl; ENSBTAT00000062955; ENSBTAP00000054107; ENSBTAG00000047719.
DR GeneID; 281125; -.
DR KEGG; bta:281125; -.
DR CTD; 1812; -.
DR VEuPathDB; HostDB:ENSBTAG00000047719; -.
DR VGNC; VGNC:28207; DRD1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155857; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q95136; -.
DR OMA; MDCQQPE; -.
DR OrthoDB; 1045889at2759; -.
DR TreeFam; TF325181; -.
DR Reactome; R-BTA-390651; Dopamine receptors.
DR PRO; PR:Q95136; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000047719; Expressed in retina and 23 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IEA:Ensembl.
DR GO; GO:0035240; F:dopamine binding; IEA:Ensembl.
DR GO; GO:0001588; F:dopamine neurotransmitter receptor activity, coupled via Gs; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IEA:Ensembl.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
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 2: Evidence at transcript level;
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_0000069371"
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 CARBOHYD 175
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; 49317 MW; 00F13996BA7CB8EE CRC64;
MRTLNTSTME GTGLVAERDF SFRILTACFL SLLILSTLLG NTLVCAAVIR FRHLRSKVTN
FFVISLAVSD LLVAVLVMPW KAVAEIAGFW PFGSFCNIWV AFDIMCSTAS ILNLCVISVD
RYWAISSPFR YERKMTPKAA FILISVAWTL SVLISFIPVQ LSWHKAKPTG PSEGNATSLG
KTINNCDSSL SRTYAISSSL ISFYIPVAIM IVTYTRIYRI AQKQIRRISA LERAAVHAKN
CQTTTGNGNP MECSQPESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI LNCMVPFCGS
GETKPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFRKA FSTLLGCYRL CPTTNNAIET
VSINNNGAVV FSSHHEPRGS ISKDCNVVYL IPHAVGSSEG LKKEEAVGIA KPLEKLSPAL
SVILDYDTDV SLEKIQPITQ NGQHPT
