ID DRD5_RAT Reviewed; 475 AA. AC P25115; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 08-NOV-2023, entry version 153. DE RecName: Full=D(1B) dopamine receptor; DE AltName: Full=D(5) dopamine receptor; DE AltName: Full=Dopamine D5 receptor; GN Name=Drd5; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Sprague-Dawley; RX PubMed=1831904; DOI=10.1073/pnas.88.17.7491; RA Tiberi M., Jarvie K.R., Silvia C., Falardeau P., Gingrich J.A., Godinot N., RA Bertrand L., Yang-Feng T.L., Fremeau R.T. Jr., Caron M.G.; RT "Cloning, molecular characterization, and chromosomal assignment of a gene RT encoding a second D1 dopamine receptor subtype: differential expression RT pattern in rat brain compared with the D1A receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7491-7495(1991). CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins CC which activate adenylyl cyclase. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Brain, in the lateral mammillary nuclei, the CC anterior pretectal nuclei, and several layers of the hippocampus. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M69118; AAA41072.1; -; Genomic_DNA. DR PIR; A41271; A41271. DR RefSeq; NP_036900.1; NM_012768.1. DR AlphaFoldDB; P25115; -. DR SMR; P25115; -. DR BioGRID; 247243; 1. DR STRING; 10116.ENSRNOP00000007074; -. DR BindingDB; P25115; -. DR ChEMBL; CHEMBL2281; -. DR DrugCentral; P25115; -. DR CarbonylDB; P25115; -. DR GlyCosmos; P25115; 1 site, No reported glycans. DR GlyGen; P25115; 1 site. DR PhosphoSitePlus; P25115; -. DR PaxDb; 10116-ENSRNOP00000007074; -. DR GeneID; 25195; -. DR KEGG; rno:25195; -. DR AGR; RGD:2523; -. DR CTD; 1816; -. DR RGD; 2523; Drd5. DR eggNOG; KOG3656; Eukaryota. DR InParanoid; P25115; -. DR OrthoDB; 2900736at2759; -. DR PhylomeDB; P25115; -. DR Reactome; R-RNO-390651; Dopamine receptors. DR PRO; PR:P25115; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0030424; C:axon; IDA:RGD. DR GO; GO:0031526; C:brush border membrane; IDA:RGD. DR GO; GO:0060170; C:ciliary membrane; ISO:RGD. DR GO; GO:0005929; C:cilium; ISO:RGD. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0043197; C:dendritic spine; IDA:RGD. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0097730; C:non-motile cilium; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0035240; F:dopamine binding; ISO:RGD. DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IDA:MGI. DR GO; GO:0001588; F:dopamine neurotransmitter receptor activity, coupled via Gs; ISO:RGD. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD. 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; IMP:RGD. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI. DR GO; GO:0008306; P:associative learning; ISO:RGD. DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:RGD. DR GO; GO:0007212; P:dopamine receptor signaling pathway; IDA:RGD. DR GO; GO:0060292; P:long-term synaptic depression; ISO:RGD. DR GO; GO:0007617; P:mating behavior; ISO:RGD. DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:RGD. DR GO; GO:0030336; P:negative regulation of cell migration; IMP:RGD. DR GO; GO:0001994; P:norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure; ISO:RGD. DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD. DR GO; GO:0045924; P:regulation of female receptivity; ISO:RGD. DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO. DR GO; GO:0001992; P:regulation of systemic arterial blood pressure by vasopressin; ISO:RGD. DR GO; GO:0001975; P:response to amphetamine; ISO:RGD. DR GO; GO:0042220; P:response to cocaine; ISO:RGD. DR GO; GO:0046960; P:sensitization; ISO:RGD. DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD. DR GO; GO:0008542; P:visual learning; IMP:RGD. DR GO; GO:0042060; P:wound healing; ISO:RGD. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000497; Dopamine_D5_rcpt. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR24248:SF136; D(1B) DOPAMINE RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00566; DOPAMINED1BR. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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..475 FT /note="D(1B) dopamine receptor" FT /id="PRO_0000069408" FT TOPO_DOM 1..38 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 39..64 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 65..75 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 76..102 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 103..111 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 112..134 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 135..153 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 154..179 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 180..215 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 216..240 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 241..289 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 290..317 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 318..335 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 336..357 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 358..475 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 415..443 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 370 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 7 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 111..211 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 475 AA; 52831 MW; 4B0C004539540D82 CRC64; MLPPGRNRTA QPARLGLQRQ LAQVDAPAGS ATPLGPAQVV TAGLLTLLIV WTLLGNVLVC AAIVRSRHLR AKMTNIFIVS LAVSDLFVAL LVMPWKAVAE VAGYWPFGTF CDIWVAFDIM CSTASILNLC IISVDRYWAI SRPFRYERKM TQRVALVMVG LAWTLSILIS FIPVQLNWHR DKAGSQGQEG LLSNGTPWEE GWELEGRTEN CDSSLNRTYA ISSSLISFYI PVAIMIVTYT RIYRIAQVQI RRISSLERAA EHAQSCRSRG AYEPDPSLRA SIKKETKVFK TLSMIMGVFV CCWLPFFILN CMVPFCSSGD AEGPKTGFPC VSETTFDIFV WFGWANSSLN PIIYAFNADF RKVFAQLLGC SHFCFRTPVQ TVNISNELIS YNQDTVFHKE IATAYVHMIP NAVSSGDREV GEEEEEGPFD HMSQISPTTP DGDLAAESVW ELDCEEEVSL GKISPLTPNC FDKTA //