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Entry version 159 (13 Feb 2019)
Sequence version 1 (01 Feb 1994)
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Protein

Mu-type opioid receptor

Gene

Oprm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Receptor for endogenous opioids such as beta-endorphin and endomorphin. Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone. Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors. The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15. They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B. Also couples to adenylate cyclase stimulatory G alpha proteins. The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization. Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction. The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins. The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation. Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling. Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling. Endogenous ligands induce rapid desensitization, endocytosis and recycling. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis.12 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionG-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-111885 Opioid Signalling
R-RNO-202040 G-protein activation
R-RNO-375276 Peptide ligand-binding receptors
R-RNO-418594 G alpha (i) signalling events

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Mu-type opioid receptor
Short name:
M-OR-1
Short name:
MOR-1
Alternative name(s):
Opioid receptor B
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Oprm1
Synonyms:Ror-b
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Rat genome database

More...
RGDi
3234 Oprm1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 66ExtracellularBy similarityAdd BLAST66
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei67 – 91Helical; Name=1By similarityAdd BLAST25
Topological domaini92 – 104CytoplasmicBy similarityAdd BLAST13
Transmembranei105 – 129Helical; Name=2By similarityAdd BLAST25
Topological domaini130 – 140ExtracellularBy similarityAdd BLAST11
Transmembranei141 – 163Helical; Name=3By similarityAdd BLAST23
Topological domaini164 – 183CytoplasmicBy similarityAdd BLAST20
Transmembranei184 – 205Helical; Name=4By similarityAdd BLAST22
Topological domaini206 – 228ExtracellularBy similarityAdd BLAST23
Transmembranei229 – 253Helical; Name=5By similarityAdd BLAST25
Topological domaini254 – 277CytoplasmicBy similarityAdd BLAST24
Transmembranei278 – 304Helical; Name=6By similarityAdd BLAST27
Topological domaini305 – 312ExtracellularBy similarity8
Transmembranei313 – 336Helical; Name=7By similarityAdd BLAST24
Topological domaini337 – 398CytoplasmicBy similarityAdd BLAST62

Keywords - Cellular componenti

Cell membrane, Cell projection, Endosome, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi91Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-96, A-166 and A-336. 1 Publication1
Mutagenesisi96Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-166 and A-336. 1 Publication1
Mutagenesisi114D → A or N: Impairs agonist affinity, agonist-induced inhibition of adenylate cyclase and coupling to G-proteins. 2 Publications1
Mutagenesisi114D → E: No effect on inhibition of adenylate cyclase. 2 Publications1
Mutagenesisi147D → A: No effect on constitutive activation. Impairs agonist affinity and agonist-induced inhibition of adenylate cyclase. 2 Publications1
Mutagenesisi147D → E: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase. 2 Publications1
Mutagenesisi147D → N: No effect on constitutive activation. 2 Publications1
Mutagenesisi164D → E: Reduces basal activity. 1 Publication1
Mutagenesisi164D → H, M, Q or Y: Constitutive active. 1 Publication1
Mutagenesisi166Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-96 and A-336. 2 Publications1
Mutagenesisi166Y → F: Decrease in phosphorylation, no decrease in G-protein binding. 2 Publications1
Mutagenesisi180T → A: Impairs ARRB2- and GRK3-mediated receptor desensitization. 1 Publication1
Mutagenesisi275L → E: No effect on constitutive activation. Some constitutive activity; when associated with K-279. 1 Publication1
Mutagenesisi279T → D: Receptor inactivation. 2 Publications1
Mutagenesisi279T → K: Constitutive active. Some constitutive activity; when associated with E-275. 2 Publications1
Mutagenesisi297H → A: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase. 1 Publication1
Mutagenesisi336Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-96 and A-166. 1 Publication1
Mutagenesisi346C → A: No change in palmitoylation. No change in palmitoylation; when associated with A-351. 1 Publication1
Mutagenesisi351C → A: No change in palmitoylation; when associated with A-346. 1 Publication1
Mutagenesisi363S → A: Abolishes basal phosphorylation; when associated with A-370. Abolishes basal and agonist-induced phosphorylation; when associated with A-370 and A-375. Accelerates agonist-induced receptor internalization. 2 Publications1
Mutagenesisi370T → A: Abolishes basal phosphorylation; when associated with A-363. Abolishes basal and agonist-induced phosphorylation; when associated with A-363 and A-375. Accelerates agonist-induced receptor internalization. 2 Publications1
Mutagenesisi375S → A: Reduces agonist-induced receptor internalization. Abolishes morphine-induced phosphorylation. Restores agonist-specific PRKCE activity. Abolishes basal and agonist-induced phosphorylation; when associated with A-363 and A-370. 3 Publications1
Mutagenesisi394T → A: Impairs phosphorylation and abolishes agonist-mediated acute receptor desensitization. 2 Publications1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL270

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
319

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000699781 – 398Mu-type opioid receptorAdd BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi9N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi31N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi46N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi140 ↔ 217PROSITE-ProRule annotation
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei166Phosphotyrosine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi351S-palmitoyl cysteineSequence analysis1
Modified residuei363Phosphoserine1 Publication1
Modified residuei370Phosphothreonine1 Publication1
Modified residuei375Phosphoserine1 Publication1
Modified residuei394Phosphothreonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Differentially phosphorylated in basal and agonist-induced conditions. Agonist-mediated phosphorylation modulates receptor internalization. Phosphorylated by GRK2 in a agonist-dependent manner. Phosphorylation at Tyr-166 requires receptor activation, is dependent on non-receptor protein tyrosine kinase Src and results in a decrease in agonist efficacy by reducing G-protein coupling efficiency. Phosphorylated on tyrosine residues; the phosphorylation is involved in agonist-induced G-protein-independent receptor down-regulation. Phosphorylation at Ser-375 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway.5 Publications
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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P33535

PRoteomics IDEntifications database

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PRIDEi
P33535

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P33535

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P33535

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P33535

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Brain. Is expressed in the cerebral cortex, caudate putamen, nucleus accumbens, septal nuclei, thalamus, hippocampus, and habenula. Not detected in cerebellum.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000018191 Expressed in 1 organ(s), highest expression level in brain

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P33535 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P33535 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms homooligomers and heterooligomers with other GPCRs, such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5 (probably in dimeric forms) (PubMed:10842167, PubMed:11896051, PubMed:14645661, PubMed:14729105, PubMed:17384143, PubMed:16682964). Interacts with heterotrimeric G proteins; interaction with a heterotrimeric complex containing GNAI1, GNB1 and GNG2 stabilizes the active conformation of the receptor and increases its affinity for endomorphin-2, the synthetic opioid peptide DAMGO and for morphinan agonists (By similarity). Interacts with PPL; the interaction disrupts agonist-mediated G-protein activation. Interacts (via C-terminus) with DNAJB4 (via C-terminus). Interacts with calmodulin; the interaction inhibits the constitutive activity of OPRM1; it abolishes basal and attenuates agonist-stimulated G-protein coupling (By similarity). Interacts with FLNA, PLD2, RANBP9 and WLS and GPM6A (PubMed:12519790, PubMed:17548356). Interacts with RTP4 (By similarity). Interacts with SYP and GNAS (PubMed:15857684, PubMed:17005904). Interacts with RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1 (By similarity).By similarity11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P33535

Protein interaction database and analysis system

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IntActi
P33535, 6 interactors

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000051290

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P33535

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P33535

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P33535

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi332 – 336NPxxY; plays a role in stabilizing the activated conformation of the receptorBy similarity5

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3656 Eukaryota
ENOG410XRW9 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158236

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230486

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG106919

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P33535

KEGG Orthology (KO)

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KOi
K04215

Identification of Orthologs from Complete Genome Data

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OMAi
PAWYWEN

Database of Orthologous Groups

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OrthoDBi
1011272at2759

TreeFam database of animal gene trees

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TreeFami
TF315737

Family and domain databases

Conserved Domains Database

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CDDi
cd15090 7tmA_Mu_opioid_R, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
IPR000105 Mu_opioid_rcpt
IPR001418 Opioid_rcpt

Pfam protein domain database

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Pfami
View protein in Pfam
PF00001 7tm_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00237 GPCRRHODOPSN
PR00537 MUOPIOIDR
PR00384 OPIOIDR

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 8 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P33535-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL
60 70 80 90 100
GGNDSLCPQT GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK
110 120 130 140 150
TATNIYIFNL ALADALATST LPFQSVNYLM GTWPFGTILC KIVISIDYYN
160 170 180 190 200
MFTSIFTLCT MSVDRYIAVC HPVKALDFRT PRNAKIVNVC NWILSSAIGL
210 220 230 240 250
PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA FIMPVLIITV
260 270 280 290 300
CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV
310 320 330 340 350
IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF
360 370 380 390
CIPTSSTIEQ QNSTRVRQNT REHPSTANTV DRTNHQLENL EAETAPLP
Length:398
Mass (Da):44,494
Last modified:February 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9C916DE7C1C33743
GO
Isoform 2 (identifier: P33535-2) [UniParc]FASTAAdd to basket
Also known as: MOR1A

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → VCAF

Show »
Length:390
Mass (Da):43,636
Checksum:i1880D1C9918035A4
GO
Isoform 3 (identifier: P33535-3) [UniParc]FASTAAdd to basket
Also known as: MOR1R

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → GAEL

Show »
Length:390
Mass (Da):43,586
Checksum:i166612B3218035A4
GO
Isoform 4 (identifier: P33535-4) [UniParc]FASTAAdd to basket
Also known as: MOR1B

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KIVLF

Show »
Length:391
Mass (Da):43,816
Checksum:i81767FCF38618035
GO
Isoform 5 (identifier: P33535-5) [UniParc]FASTAAdd to basket
Also known as: MOR1B2

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → EPQSVET

Show »
Length:393
Mass (Da):43,986
Checksum:iA9819A64EBC80041
GO
Isoform 6 (identifier: P33535-6) [UniParc]FASTAAdd to basket
Also known as: MOR1C1

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → PALAVSVAQI...ALIYNNVNFI

Show »
Length:451
Mass (Da):50,445
Checksum:iF1130789E14DF1F7
GO
Isoform 7 (identifier: P33535-7) [UniParc]FASTAAdd to basket
Also known as: MOR-1C2

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → PALAVSVAQI...MPAHVLVRPW

Show »
Length:468
Mass (Da):52,410
Checksum:i55F763EE13B2B6D1
GO
Isoform 8 (identifier: P33535-8) [UniParc]FASTAAdd to basket
Also known as: rMOR-1D

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → T

Show »
Length:387
Mass (Da):43,317
Checksum:iBAF18035A454EB66
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A125U2D0A0A125U2D0_RAT
Mu-type opioid receptor
Oprm1
222Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAQ77387 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti237F → G in AAA79180 (PubMed:8189219).Curated1
Sequence conflicti238I → V in AAQ77386 (Ref. 7) Curated1
Sequence conflicti245V → I in AAA41630 (PubMed:8393525).Curated1
Sequence conflicti245V → I in AAA70049 (Ref. 4) Curated1
Sequence conflicti245V → I in S77863 (PubMed:7733926).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041828387 – 398LENLE…TAPLP → VCAF in isoform 2. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041829387 – 398LENLE…TAPLP → GAEL in isoform 3. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041830387 – 398LENLE…TAPLP → KIVLF in isoform 4. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041831387 – 398LENLE…TAPLP → EPQSVET in isoform 5. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041832387 – 398LENLE…TAPLP → PALAVSVAQIFTGYPSPTHG EKPCKSYRDRPRPCGRTWSL KSRAESNVEHFHCGAALIYN NVNFI in isoform 6. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041833387 – 398LENLE…TAPLP → PALAVSVAQIFTGYPSPTHG EKPCKSYRDRPRPCGRTWSL KSRAESNVEHFHCGAALIYN NELKIGPVSWLQMPAHVLVR PW in isoform 7. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041834387 – 398LENLE…TAPLP → T in isoform 8. 1 PublicationAdd BLAST12

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D16349 mRNA Translation: BAA03852.1
L20684 mRNA Translation: AAA41643.1
L13069 mRNA Translation: AAA41630.1
U02083 mRNA Translation: AAA70049.1
L22455 mRNA Translation: AAA16075.1
U35424 mRNA Translation: AAA79180.1
AY309003 mRNA Translation: AAQ77387.1 Frameshift.
AY309004 mRNA Translation: AAQ77388.1
AY225402 mRNA Translation: AAP44725.1
AY225403 mRNA Translation: AAP44726.1
AY309000 mRNA Translation: AAQ77384.1
AY309002 mRNA Translation: AAQ77386.1
S77863 mRNA No translation available.
S75669 mRNA Translation: AAB33530.2

Protein sequence database of the Protein Information Resource

More...
PIRi
I56504
I56517
S69010

NCBI Reference Sequences

More...
RefSeqi
NP_001033686.1, NM_001038597.2 [P33535-2]
NP_001033688.2, NM_001038599.2 [P33535-5]
NP_001033689.1, NM_001038600.2 [P33535-6]
NP_001033690.1, NM_001038601.2 [P33535-7]
NP_001291664.1, NM_001304735.1 [P33535-1]
NP_001291666.1, NM_001304737.1 [P33535-1]
NP_001291667.1, NM_001304738.1 [P33535-1]
NP_001291669.1, NM_001304740.1 [P33535-1]
NP_037203.1, NM_013071.2 [P33535-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.10118

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000024682; ENSRNOP00000024682; ENSRNOG00000018191 [P33535-6]
ENSRNOT00000079628; ENSRNOP00000072626; ENSRNOG00000018191 [P33535-8]
ENSRNOT00000083308; ENSRNOP00000074079; ENSRNOG00000018191 [P33535-1]
ENSRNOT00000092034; ENSRNOP00000068988; ENSRNOG00000018191 [P33535-7]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25601

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25601

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16349 mRNA Translation: BAA03852.1
L20684 mRNA Translation: AAA41643.1
L13069 mRNA Translation: AAA41630.1
U02083 mRNA Translation: AAA70049.1
L22455 mRNA Translation: AAA16075.1
U35424 mRNA Translation: AAA79180.1
AY309003 mRNA Translation: AAQ77387.1 Frameshift.
AY309004 mRNA Translation: AAQ77388.1
AY225402 mRNA Translation: AAP44725.1
AY225403 mRNA Translation: AAP44726.1
AY309000 mRNA Translation: AAQ77384.1
AY309002 mRNA Translation: AAQ77386.1
S77863 mRNA No translation available.
S75669 mRNA Translation: AAB33530.2
PIRiI56504
I56517
S69010
RefSeqiNP_001033686.1, NM_001038597.2 [P33535-2]
NP_001033688.2, NM_001038599.2 [P33535-5]
NP_001033689.1, NM_001038600.2 [P33535-6]
NP_001033690.1, NM_001038601.2 [P33535-7]
NP_001291664.1, NM_001304735.1 [P33535-1]
NP_001291666.1, NM_001304737.1 [P33535-1]
NP_001291667.1, NM_001304738.1 [P33535-1]
NP_001291669.1, NM_001304740.1 [P33535-1]
NP_037203.1, NM_013071.2 [P33535-1]
UniGeneiRn.10118

3D structure databases

ProteinModelPortaliP33535
SMRiP33535
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP33535
IntActiP33535, 6 interactors
STRINGi10116.ENSRNOP00000051290

Chemistry databases

BindingDBiP33535
ChEMBLiCHEMBL270
GuidetoPHARMACOLOGYi319

Protein family/group databases

Information system for G protein-coupled receptors (GPCRs)

More...
GPCRDBi
Search...

PTM databases

iPTMnetiP33535
PhosphoSitePlusiP33535
SwissPalmiP33535

Proteomic databases

PaxDbiP33535
PRIDEiP33535

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024682; ENSRNOP00000024682; ENSRNOG00000018191 [P33535-6]
ENSRNOT00000079628; ENSRNOP00000072626; ENSRNOG00000018191 [P33535-8]
ENSRNOT00000083308; ENSRNOP00000074079; ENSRNOG00000018191 [P33535-1]
ENSRNOT00000092034; ENSRNOP00000068988; ENSRNOG00000018191 [P33535-7]
GeneIDi25601
KEGGirno:25601

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4988
RGDi3234 Oprm1

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00940000158236
HOGENOMiHOG000230486
HOVERGENiHBG106919
InParanoidiP33535
KOiK04215
OMAiPAWYWEN
OrthoDBi1011272at2759
TreeFamiTF315737

Enzyme and pathway databases

ReactomeiR-RNO-111885 Opioid Signalling
R-RNO-202040 G-protein activation
R-RNO-375276 Peptide ligand-binding receptors
R-RNO-418594 G alpha (i) signalling events

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P33535

Gene expression databases

BgeeiENSRNOG00000018191 Expressed in 1 organ(s), highest expression level in brain
ExpressionAtlasiP33535 baseline and differential
GenevisibleiP33535 RN

Family and domain databases

CDDicd15090 7tmA_Mu_opioid_R, 1 hit
InterProiView protein in InterPro
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
IPR000105 Mu_opioid_rcpt
IPR001418 Opioid_rcpt
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PRINTSiPR00237 GPCRRHODOPSN
PR00537 MUOPIOIDR
PR00384 OPIOIDR
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOPRM_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P33535
Secondary accession number(s): Q2TV20
, Q2TV21, Q4VWM5, Q4VWM7, Q4VWX7, Q4VWX8, Q62846, Q64064, Q64120
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 13, 2019
This is version 159 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
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