OPRD_RAT
ID OPRD_RAT Reviewed; 372 AA.
AC P33533;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Delta-type opioid receptor;
DE Short=D-OR-1;
DE Short=DOR-1;
DE AltName: Full=Opioid receptor A;
GN Name=Oprd1; Synonyms=Ror-a;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8394245; DOI=10.1016/0014-5793(93)81011-n;
RA Fukuda K., Kato S., Mori K., Nishi M., Takeshima H.;
RT "Primary structures and expression from cDNAs of rat opioid receptor
RT delta- and mu-subtypes.";
RL FEBS Lett. 327:311-314(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7519274; DOI=10.1002/jnr.490370605;
RA Abood M.E., Noel M.A., Farnsworth J.S., Tao Q.;
RT "Molecular cloning and expression of a delta-opioid receptor from rat
RT brain.";
RL J. Neurosci. Res. 37:714-719(1994).
CC -!- FUNCTION: G-protein coupled receptor that functions as receptor for
CC endogenous enkephalins and for a subset of other opioids. Ligand
CC binding causes a conformation change that triggers signaling via
CC guanine nucleotide-binding proteins (G proteins) and modulates the
CC activity of down-stream effectors, such as adenylate cyclase. Signaling
CC leads to the inhibition of adenylate cyclase activity. Inhibits
CC neurotransmitter release by reducing calcium ion currents and
CC increasing potassium ion conductance. Plays a role in the perception of
CC pain and in opiate-mediated analgesia. Plays a role in developing
CC analgesic tolerance to morphine. {ECO:0000269|PubMed:7519274,
CC ECO:0000269|PubMed:8394245}.
CC -!- SUBUNIT: May form homooligomers. Forms a heterodimer with OPRM1.
CC Interacts with GPRASP1. Interacts with RTP4; the interaction promotes
CC cell surface localization of the OPRD1-OPRM1 heterodimer.
CC {ECO:0000250|UniProtKB:P32300, ECO:0000250|UniProtKB:P41143}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7519274,
CC ECO:0000269|PubMed:8394245}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:7519274, ECO:0000269|PubMed:8394245}.
CC -!- TISSUE SPECIFICITY: Detected in brain, brain stem and brain cortex.
CC {ECO:0000269|PubMed:7519274, ECO:0000269|PubMed:8394245}.
CC -!- PTM: Ubiquitinated. A basal ubiquitination seems not to be related to
CC degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1
CC oligomers leading to proteasomal degradation; the ubiquitination is
CC diminished by RTP4. {ECO:0000250|UniProtKB:P32300}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D16348; BAA03851.1; -; mRNA.
DR EMBL; U00475; AAA19939.1; -; mRNA.
DR PIR; S34592; S34592.
DR RefSeq; NP_036749.1; NM_012617.1.
DR AlphaFoldDB; P33533; -.
DR SMR; P33533; -.
DR BioGRID; 246752; 1.
DR STRING; 10116.ENSRNOP00000014084; -.
DR BindingDB; P33533; -.
DR ChEMBL; CHEMBL269; -.
DR DrugCentral; P33533; -.
DR GuidetoPHARMACOLOGY; 317; -.
DR GlyGen; P33533; 2 sites.
DR iPTMnet; P33533; -.
DR PhosphoSitePlus; P33533; -.
DR PaxDb; P33533; -.
DR Ensembl; ENSRNOT00000014084; ENSRNOP00000014084; ENSRNOG00000010531.
DR GeneID; 24613; -.
DR KEGG; rno:24613; -.
DR UCSC; RGD:3233; rat.
DR CTD; 4985; -.
DR RGD; 3233; Oprd1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000157669; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P33533; -.
DR OMA; SEARNKP; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P33533; -.
DR TreeFam; TF315737; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P33533; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000010531; Expressed in frontal cortex and 2 other tissues.
DR Genevisible; P33533; RN.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0097444; C:spine apparatus; IDA:SynGO.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0038046; F:G protein-coupled enkephalin receptor activity; IDA:RGD.
DR GO; GO:0004985; F:G protein-coupled opioid receptor activity; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0097237; P:cellular response to toxic substance; ISO:RGD.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0038003; P:G protein-coupled opioid receptor signaling pathway; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:RGD.
DR InterPro; IPR000321; Delta_opi_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001418; Opioid_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00525; DELTAOPIOIDR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00384; OPIOIDR.
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; Ubl conjugation.
FT CHAIN 1..372
FT /note="Delta-type opioid receptor"
FT /id="PRO_0000069965"
FT TOPO_DOM 1..47
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 48..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 76..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 86..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..122
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 145..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 164..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 187..206
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 207..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 239..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 262..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 285..299
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 300..321
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 322..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 340..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 333
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 372 AA; 40450 MW; F578BD1F64C61D50 CRC64;
MEPVPSARAE LQFSLLANVS DTFPSAFPSA SANASGSPGA RSASSLALAI AITALYSAVC
AVGLLGNVLV MFGIVRYTKL KTATNIYIFN LALADALATS TLPFQSAKYL METWPFGELL
CKAVLSIDYY NMFTSIFTLT MMSVDRYIAV CHPVKALDFR TPAKAKLINI CIWVLASGVG
VPIMVMAVTQ PRDGAVVCTL QFPSPSWYWD TVTKICVFLF AFVVPILIIT VCYGLMLLRL
RSVRLLSGSK EKDRSLRRIT RMVLVVVGAF VVCWAPIHIF VIVWTLVDIN RRDPLVVAAL
HLCIALGYAN SSLNPVLYAF LDENFKRCFR QLCRAPCGGQ EPGSLRRPRQ ATARERVTAC
TPSDGPGGGA AA
