P41143 · OPRD_HUMAN
- ProteinDelta-type opioid receptor
- GeneOPRD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids372 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
G-protein coupled receptor that functions as a 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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDelta-type opioid receptor
- Short namesD-OR-1; DOR-1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP41143
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-47 | Extracellular | ||||
Sequence: MEPAPSAGAELQPPLFANASDAYPSACPSAGANASGPPGARSASSLA | ||||||
Transmembrane | 48-75 | Helical; Name=1 | ||||
Sequence: LAIAITALYSAVCAVGLLGNVLVMFGIV | ||||||
Topological domain | 76-85 | Cytoplasmic | ||||
Sequence: RYTKMKTATN | ||||||
Transmembrane | 86-110 | Helical; Name=2 | ||||
Sequence: IYIFNLALADALATSTLPFQSAKYL | ||||||
Topological domain | 111-122 | Extracellular | ||||
Sequence: METWPFGELLCK | ||||||
Transmembrane | 123-144 | Helical; Name=3 | ||||
Sequence: AVLSIDYYNMFTSIFTLTMMSV | ||||||
Topological domain | 145-163 | Cytoplasmic | ||||
Sequence: DRYIAVCHPVKALDFRTPA | ||||||
Transmembrane | 164-186 | Helical; Name=4 | ||||
Sequence: KAKLINICIWVLASGVGVPIMVM | ||||||
Topological domain | 187-206 | Extracellular | ||||
Sequence: AVTRPRDGAVVCMLQFPSPS | ||||||
Transmembrane | 207-238 | Helical; Name=5 | ||||
Sequence: WYWDTVTKICVFLFAFVVPILIITVCYGLMLL | ||||||
Topological domain | 239-261 | Cytoplasmic | ||||
Sequence: RLRSVRLLSGSKEKDRSLRRITR | ||||||
Transmembrane | 262-284 | Helical; Name=6 | ||||
Sequence: MVLVVVGAFVVCWAPIHIFVIVW | ||||||
Topological domain | 285-299 | Extracellular | ||||
Sequence: TLVDIDRRDPLVVAA | ||||||
Transmembrane | 300-321 | Helical; Name=7 | ||||
Sequence: LHLCIALGYANSSLNPVLYAFL | ||||||
Topological domain | 322-372 | Cytoplasmic | ||||
Sequence: DENFKRCFRQLCRKPCGRPDPSSFSRAREATARERVTACTPSDGPGGGAAA |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_012083 | 27 | improved maturation and increased expression at the cell surface; dbSNP:rs1042114 | |||
Sequence: C → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 459 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond, lipidation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000069962 | 1-372 | UniProt | Delta-type opioid receptor | |||
Sequence: MEPAPSAGAELQPPLFANASDAYPSACPSAGANASGPPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKMKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRKPCGRPDPSSFSRAREATARERVTACTPSDGPGGGAAA | |||||||
Glycosylation | 18 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 33 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 121↔198 | UniProt | |||||
Sequence: CKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTRPRDGAVVC | |||||||
Lipidation | 333 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
N-glycosylated.
Ubiquitinated. A basal ubiquitination seems not to be related to degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1 oligomers leading to proteasomal degradation; the ubiquitination is diminished by RTP4.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in oocytes (at protein level). Detected in brain cortex, hypothalamus, hippocampus and olfactory bulb. Detected in oocytes.
Gene expression databases
Organism-specific databases
Interaction
Subunit
May form homooligomers. Forms a heterodimer with OPRM1 (By similarity).
Interacts with GPRASP1 (PubMed:12142540, PubMed:15086532).
Interacts with RTP4; the interaction promotes cell surface localization of the OPRD1-OPRM1 heterodimer (By similarity).
Interacts with GPRASP1 (PubMed:12142540, PubMed:15086532).
Interacts with RTP4; the interaction promotes cell surface localization of the OPRD1-OPRM1 heterodimer (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P41143 | ATP2A2 P16615 | 3 | EBI-2624456, EBI-358933 | |
XENO | P41143 | ATP2A2 P11607 | 2 | EBI-2624456, EBI-8004986 | |
BINARY | P41143 | CANX P27824 | 2 | EBI-2624456, EBI-355947 | |
BINARY | P41143 | CTXN3 Q4LDR2 | 3 | EBI-2624456, EBI-12019274 | |
BINARY | P41143 | GPRASP1 Q5JY77 | 2 | EBI-2624456, EBI-2514717 | |
BINARY | P41143 | RPRM Q9NS64 | 3 | EBI-2624456, EBI-1052363 | |
BINARY | P41143 | SLC12A7 Q9Y666-2 | 3 | EBI-2624456, EBI-12854384 | |
BINARY | P41143 | SLC13A4 Q9UKG4 | 3 | EBI-2624456, EBI-12808018 | |
BINARY | P41143 | SMAGP Q0VAQ4 | 3 | EBI-2624456, EBI-10226799 | |
BINARY | P41143 | TMEM237 Q96Q45-2 | 3 | EBI-2624456, EBI-10982110 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 340-372 | Disordered | ||||
Sequence: PDPSSFSRAREATARERVTACTPSDGPGGGAAA |
Sequence similarities
Belongs to the G-protein coupled receptor 1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Length372
- Mass (Da)40,369
- Last updated2010-11-02 v4
- Checksum9D483FC39BA2BAE4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U07882 EMBL· GenBank· DDBJ | AAA18789.2 EMBL· GenBank· DDBJ | mRNA | ||
U10504 EMBL· GenBank· DDBJ | AAA83426.1 EMBL· GenBank· DDBJ | mRNA | ||
EU883570 EMBL· GenBank· DDBJ | ACG60644.1 EMBL· GenBank· DDBJ | mRNA | ||
AL009181 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |