OPRD_PIG
ID OPRD_PIG Reviewed; 228 AA.
AC P79291;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Delta-type opioid receptor;
DE Short=D-OR-1;
DE Short=DOR-1;
DE Flags: Fragment;
GN Name=OPRD1;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain cortex;
RX PubMed=9690372; DOI=10.1023/a:1018877823534;
RA Brown D.R., Poonyachoti S., Osinski M.A., Kowalski T.R., Pampusch M.S.,
RA Elde R.P., Murtaugh M.P.;
RT "Delta-opioid receptor mRNA expression and immunohistochemical localization
RT in porcine ileum.";
RL Dig. Dis. Sci. 43:1402-1410(1998).
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:9690372}.
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; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in myenteric plexus and smooth muscle (at
CC protein level). Detected in brain and intestine.
CC {ECO:0000269|PubMed:9690372}.
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}.
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; U71149; AAB39694.1; -; mRNA.
DR AlphaFoldDB; P79291; -.
DR SMR; P79291; -.
DR STRING; 9823.ENSSSCP00000024665; -.
DR BindingDB; P79291; -.
DR ChEMBL; CHEMBL4103; -.
DR PaxDb; P79291; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P79291; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P79291; SS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0038046; F:G protein-coupled enkephalin receptor activity; IBA:GO_Central.
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:0038003; P:G protein-coupled opioid receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN <1..>228
FT /note="Delta-type opioid receptor"
FT /id="PRO_0000069964"
FT TRANSMEM <1..3
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 4..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 14..38
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 39..50
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 51..72
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 73..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 92..114
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 115..134
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 135..166
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 167..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..212
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 213..227
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT DISULFID 49..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 228
SQ SEQUENCE 228 AA; 25725 MW; C8C1A8984A4711DE CRC64;
GIVRYTKMKT ATNIYIFNLA LADALATSTL PFQSAKYLME TWPFGELLCK AVLSIDYYNM
FTSIFTLTMM SVDRYIAVCH PVKALDFRTP AKAKLINICI WVLASGVGVP IMVMAVTRPR
DGAVVCMLQF PSPSWYWDTV TKICVFLFAF VVPILVITVC YGLMLLRLRS VRLLSGSKEK
DRSLRRITRM VLVVVGAFVV CWAPIHIFVI VWTLVDIDRR DPLVVAAL
