DRD1_DIDVI
ID DRD1_DIDVI Reviewed; 446 AA.
AC P42288;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=D(1A) dopamine receptor;
DE AltName: Full=Dopamine D1 receptor;
GN Name=DRD1;
OS Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=8246914;
RA Nash S.R., Godinot N., Caron M.G.;
RT "Cloning and characterization of the opossum kidney cell D1 dopamine
RT receptor: expression of identical D1A and D1B dopamine receptor mRNAs in
RT opossum kidney and brain.";
RL Mol. Pharmacol. 44:918-925(1993).
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 -!- SUBUNIT: Interacts with DNAJC14 via its C-terminus.
CC {ECO:0000250|UniProtKB:P18901}.
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; S67258; AAB29143.1; -; mRNA.
DR AlphaFoldDB; P42288; -.
DR SMR; P42288; -.
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 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; Synapse; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..446
FT /note="D(1A) dopamine receptor"
FT /id="PRO_0000069372"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..298
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..340
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 350
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 354
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 446 AA; 49762 MW; A6B1FF3CBFE6476C CRC64;
MPLNDTTMDR RGLVVERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF RHLRSKVTNF
FVISLAVSDL LVAVLVMPWK AVAEIAGFWP FGSFCNIWVA FDIMCSTASI LNLCVISVDR
YWAISSPFRY ERKMTPKAAF ILISVAWTLS VLISFIPVQL NWHKARPLSS PDGNVSSQDE
TMDNCDSSLS RTYAISSSLI SFYIPVAIMI VTYTRIYRIA QKQIRRISAL ERAAVHAKNC
QNTTGNGANV ECSQPESSFK MSFKRETKVL KTLSVIMGVF VCCWLPFFIL NCMVPFCESD
LPSGETKPFC IDSITFDVFV WFGWANSSLN PIIYAFNADF RKAFSTLLGC YRLCPTANNA
IETVSINNNG AVFSSHHEPR GSISKDCNLV YLIPQAVTSR DPKKEEGGGS KPLEKTSPAL
SVILDYEVDL SLEKINPITQ NGQHKT
