Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Delta-type opioid receptor

Gene

Oprd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_319210. Peptide ligand-binding receptors.
REACT_331048. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-type opioid receptor
Short name:
D-OR-1
Short name:
DOR-1
Alternative name(s):
K56
MSL-2
Gene namesi
Name:Oprd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:97438. Oprd1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4747Extracellular1 PublicationAdd
BLAST
Transmembranei48 – 7528Helical; Name=1Add
BLAST
Topological domaini76 – 8510Cytoplasmic1 Publication
Transmembranei86 – 11025Helical; Name=2Add
BLAST
Topological domaini111 – 12212Extracellular1 PublicationAdd
BLAST
Transmembranei123 – 14422Helical; Name=3Add
BLAST
Topological domaini145 – 16319Cytoplasmic1 PublicationAdd
BLAST
Transmembranei164 – 18623Helical; Name=4Add
BLAST
Topological domaini187 – 20620Extracellular1 PublicationAdd
BLAST
Transmembranei207 – 23832Helical; Name=5Add
BLAST
Topological domaini239 – 26123Cytoplasmic1 PublicationAdd
BLAST
Transmembranei262 – 28423Helical; Name=6Add
BLAST
Topological domaini285 – 29915Extracellular1 PublicationAdd
BLAST
Transmembranei300 – 32122Helical; Name=7Add
BLAST
Topological domaini322 – 37251Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are born at the expected Mendelian rate; they show no obvious phenotype and are fertile. Mutant mice show decreased analgesia in response to opioids, such as deltorphin-2. They do not develop analgesic tolerance to morphine.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Delta-type opioid receptorPRO_0000069963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi18 – 181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi121 ↔ 198PROSITE-ProRule annotation1 Publication
Lipidationi333 – 3331S-palmitoyl cysteineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiP32300.

PTM databases

PhosphoSiteiP32300.

Expressioni

Tissue specificityi

Brain, with high concentrations in the basal ganglia and limbic regions.2 Publications

Gene expression databases

BgeeiP32300.
CleanExiMM_OPRD1.
ExpressionAtlasiP32300. baseline and differential.
GenevisibleiP32300. MM.

Interactioni

Subunit structurei

May form homooligomers. Interacts with GPRASP1 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-46417N.
IntActiP32300. 7 interactions.
STRINGi10090.ENSMUSP00000050077.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 7635Combined sources
Helixi83 – 10018Combined sources
Helixi102 – 11110Combined sources
Helixi118 – 15134Combined sources
Helixi153 – 1597Combined sources
Helixi162 – 18625Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi203 – 2053Combined sources
Helixi206 – 22015Combined sources
Helixi223 – 23816Combined sources
Helixi258 – 28629Combined sources
Helixi294 – 32128Combined sources
Helixi323 – 3264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EJ4X-ray3.40A36-342[»]
ProteinModelPortaliP32300.
SMRiP32300. Positions 39-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG241795.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP32300.
KOiK04213.
OMAiLCRKPCG.
OrthoDBiEOG7BKCVQ.
PhylomeDBiP32300.
TreeFamiTF315737.

Family and domain databases

InterProiIPR000321. Delta_opi_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00525. DELTAOPIOIDR.
PR00237. GPCRRHODOPSN.
PR00384. OPIOIDR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELVPSARAE LQSSPLVNLS DAFPSAFPSA GANASGSPGA RSASSLALAI
60 70 80 90 100
AITALYSAVC AVGLLGNVLV MFGIVRYTKL KTATNIYIFN LALADALATS
110 120 130 140 150
TLPFQSAKYL METWPFGELL CKAVLSIDYY NMFTSIFTLT MMSVDRYIAV
160 170 180 190 200
CHPVKALDFR TPAKAKLINI CIWVLASGVG VPIMVMAVTQ PRDGAVVCML
210 220 230 240 250
QFPSPSWYWD TVTKICVFLF AFVVPILIIT VCYGLMLLRL RSVRLLSGSK
260 270 280 290 300
EKDRSLRRIT RMVLVVVGAF VVCWAPIHIF VIVWTLVDIN RRDPLVVAAL
310 320 330 340 350
HLCIALGYAN SSLNPVLYAF LDENFKRCFR QLCRTPCGRQ EPGSLRRPRQ
360 370
ATTRERVTAC TPSDGPGGGA AA
Length:372
Mass (Da):40,561
Last modified:October 1, 1993 - v1
Checksum:iBC3B3BBD2E52D3F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06322 mRNA. Translation: AAA37522.1.
L07271 mRNA. No translation available.
L11064 mRNA. Translation: AAA37520.1.
S65335 mRNA. Translation: AAA16009.1.
S66181 mRNA. Translation: AAB28546.1.
CCDSiCCDS18718.1.
PIRiB48227.
RefSeqiNP_038650.3. NM_013622.3.
UniGeneiMm.5243.

Genome annotation databases

EnsembliENSMUST00000056336; ENSMUSP00000050077; ENSMUSG00000050511.
GeneIDi18386.
KEGGimmu:18386.
UCSCiuc008vap.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06322 mRNA. Translation: AAA37522.1.
L07271 mRNA. No translation available.
L11064 mRNA. Translation: AAA37520.1.
S65335 mRNA. Translation: AAA16009.1.
S66181 mRNA. Translation: AAB28546.1.
CCDSiCCDS18718.1.
PIRiB48227.
RefSeqiNP_038650.3. NM_013622.3.
UniGeneiMm.5243.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EJ4X-ray3.40A36-342[»]
ProteinModelPortaliP32300.
SMRiP32300. Positions 39-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46417N.
IntActiP32300. 7 interactions.
STRINGi10090.ENSMUSP00000050077.

Chemistry

BindingDBiP32300.
ChEMBLiCHEMBL2221343.
GuidetoPHARMACOLOGYi317.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP32300.

Proteomic databases

PRIDEiP32300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056336; ENSMUSP00000050077; ENSMUSG00000050511.
GeneIDi18386.
KEGGimmu:18386.
UCSCiuc008vap.1. mouse.

Organism-specific databases

CTDi4985.
MGIiMGI:97438. Oprd1.

Phylogenomic databases

eggNOGiNOG241795.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP32300.
KOiK04213.
OMAiLCRKPCG.
OrthoDBiEOG7BKCVQ.
PhylomeDBiP32300.
TreeFamiTF315737.

Enzyme and pathway databases

ReactomeiREACT_319210. Peptide ligand-binding receptors.
REACT_331048. G alpha (i) signalling events.

Miscellaneous databases

NextBioi293976.
PROiP32300.
SOURCEiSearch...

Gene expression databases

BgeeiP32300.
CleanExiMM_OPRD1.
ExpressionAtlasiP32300. baseline and differential.
GenevisibleiP32300. MM.

Family and domain databases

InterProiIPR000321. Delta_opi_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00525. DELTAOPIOIDR.
PR00237. GPCRRHODOPSN.
PR00384. OPIOIDR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The delta-opioid receptor: isolation of a cDNA by expression cloning and pharmacological characterization."
    Kieffer B.L., Befort K., Gaveriaux-Ruff C., Hirth C.G.
    Proc. Natl. Acad. Sci. U.S.A. 89:12048-12052(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
  2. "Cloning of a delta opioid receptor by functional expression."
    Evans C.J., Keith D.E. Jr., Morrison H., Magendzo K., Edwards R.H.
    Science 258:1952-1955(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Cloning and functional comparison of kappa and delta opioid receptors from mouse brain."
    Yasuda K., Raynor K., Kong H., Breder C.D., Takeda J., Reisine T., Bell G.I.
    Proc. Natl. Acad. Sci. U.S.A. 90:6736-6740(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  4. "Characterization and mapping of a delta opioid receptor clone from NG108-15 cells."
    Keith D.E. Jr., Anton B., Evans C.J.
    Proc. West. Pharmacol. Soc. 36:299-306(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Regional expression and chromosomal localization of the delta opiate receptor gene."
    Bzdega T., Chin H., Kim K., Jung H.H., Kozak C.A., Klee W.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:9305-9309(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-372.
  6. "Retention of supraspinal delta-like analgesia and loss of morphine tolerance in delta opioid receptor knockout mice."
    Zhu Y., King M.A., Schuller A.G., Nitsche J.F., Reidl M., Elde R.P., Unterwald E., Pasternak G.W., Pintar J.E.
    Neuron 24:243-252(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "A 3D model of the delta opioid receptor and ligand-receptor complexes."
    Alkorta I., Loew G.H.
    Protein Eng. 9:573-583(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  8. "Structure of the delta-opioid receptor bound to naltrindole."
    Granier S., Manglik A., Kruse A.C., Kobilka T.S., Thian F.S., Weis W.I., Kobilka B.K.
    Nature 485:400-404(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 36-342 IN COMPLEX WITH NALTRINDOLE, SUBCELLULAR LOCATION, DISULFIDE BOND, TOPOLOGY.

Entry informationi

Entry nameiOPRD_MOUSE
AccessioniPrimary (citable) accession number: P32300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 24, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.