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P42866 (OPRM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mu-type opioid receptor

Short name=M-OR-1
Short name=MOR-1
Gene names
Name:Oprm1
Synonyms:Mor, Oprm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for endogenous opioids such as beta-endorphin and endomorphin. 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 extend 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. Isoform 9 is involved in morphine-induced scratching and seems to cross-activate GRPR in response to morphine. Ref.3 Ref.17 Ref.19 Ref.25 Ref.29 Ref.31 Ref.32

Subunit structure

Forms homooligomers and heterooligomers with other GPCRs, such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5 (probably in dimeric forms). 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. Interacts with FLNA, PLD2, RANBP9 and WLS and GPM6A. Interacts with RTP4. Interacts with SYP and GNAS By similarity. Interacts with RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1. Isoform 9 interacts with GRPR. Ref.19 Ref.20 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.3 Ref.21 Ref.32.

Post-translational modification

Phosphorylated. Differentially phosphorylated in basal and agonist-induced conditions. Agonist-mediated phosphorylation modulates receptor internalization. Phosphorylated by ADRBK1 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.

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. Ref.28

Disruption phenotype

During adult neurogenesis in hippocampus, increased numbers of granule cells maturing into neurons, larger granule cell layers and increased numbers of granule cells. Ref.25

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-activating dopamine receptor signaling pathway

Inferred from direct assay PubMed 8738226. Source: MGI

adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 8738226. Source: MGI

behavioral response to ethanol

Inferred from electronic annotation. Source: Ensembl

calcium ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

cellular response to stress

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from mutant phenotype PubMed 10835636. Source: MGI

negative regulation of Wnt protein secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of adenylate cyclase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cAMP-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

opioid receptor signaling pathway

Inferred from direct assay PubMed 8738226. Source: GOC

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of neurogenesis

Inferred from mutant phenotype Ref.25. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of N-methyl-D-aspartate selective glutamate receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of behavior

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from mutant phenotype Ref.17. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 8738226. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionG-protein alpha-subunit binding

Inferred from sequence or structural similarity. Source: UniProtKB

G-protein coupled receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

beta-endorphin receptor activity

Inferred from electronic annotation. Source: Ensembl

morphine receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

opioid receptor activity

Inferred from direct assay PubMed 8738226. Source: MGI

protein binding

Inferred from physical interaction Ref.29PubMed 22177524. Source: IntAct

voltage-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GNASP63092-22EBI-5282656,EBI-7607528From a different organism.
GrprP217294EBI-6049667,EBI-6049651

Alternative products

This entry describes 19 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Functional relevance for short isoforms with one transmembrane domain only is unsure and these isoforms are not included.
Isoform 1 (identifier: P42866-1)

Also known as: MOR-1; MOR-H; MOR-1J; MOR-1T;

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.
Isoform 2 (identifier: P42866-2)

Also known as: MOR-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → VCAF
Isoform 3 (identifier: P42866-3)

Also known as: MOR-1B1;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KIDLF
Isoform 4 (identifier: P42866-4)

Also known as: MOR-1B2;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KLLMWRAMPTFKRHLAIMLSLDN
Isoform 5 (identifier: P42866-5)

Also known as: MOR-1B3; MOR-1Q;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → TSLTLQ
Isoform 6 (identifier: P42866-6)

Also known as: MOR-1B4; MOR-1R;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → AHQKPQECLKCRCLSLTILVICLHFQHQQFFIMIKKNVS
Isoform 7 (identifier: P42866-7)

Also known as: MOR-1B5; MOR-1P;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → CV
Isoform 8 (identifier: P42866-8)

Also known as: MOR-1C;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → PTLAVSVAQIFTGYPSPTHVEKPCKSCMDRGMRNLLPDDGPRQESGEGQLGR
Isoform 9 (identifier: P42866-9)

Also known as: MOR-1D;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → RNEEPSS
Isoform 10 (identifier: P42866-10)

Also known as: MOR-1E; MOR-1Eiii; MOR-1Eiv;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KKKLDSQRGCVQHPV
Isoform 11 (identifier: P42866-11)

Also known as: MOR-1F;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → APCACVPGANRGQTKASDLLDLELETVGSHQADAETNPGPYEGSKCAEPLAISLVPLY
Isoform 12 (identifier: P42866-12)

Also known as: MOR-1O;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → PTLAVSVAQIFTGYPSPTHVEKPCKSCMDR
Isoform 13 (identifier: P42866-13)

Also known as: MOR-1P; MOR-1R;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → IMKFEAIYPK...LRHMGPSYPS
Isoform 14 (identifier: P42866-14)

Also known as: MOR-1G;

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MDSSAGPGNI...GNFLVMYVIV → MMEAFSKSAFQKLRQRDGNQEGKSYL
Isoform 15 (identifier: P42866-15)

Also known as: MOR-1M;

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MDSSAGPGNI...GNFLVMYVIV → MMEAFSKSAFQKLRQRDGNQEGKSYL
     387-398: LENLEAETAPLP → PTLAVSVAQIFTGYPSPTHVEKPCKSCMDRGMRNLLPDDGPRQESGEGQLGR
Isoform 16 (identifier: P42866-16)

Also known as: MOR-1N;

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MDSSAGPGNI...GNFLVMYVIV → MMEAFSKSAFQKLRQRDGNQEGKSYL
     387-398: LENLEAETAPLP → RNEEPSS
Isoform 17 (identifier: P42866-17)

Also known as: MOR-1U;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → PTLAVSVAQI...QESGEGQLGR
Isoform 18 (identifier: P42866-18)

Also known as: MOR-1V;

The sequence of this isoform differs from the canonical sequence as follows:
     387-398: LENLEAETAPLP → KQEKTKTKSAWEIWEQKEHTLLLGETHLTIQHLS
Isoform 19 (identifier: P42866-19)

Also known as: MOR-1W;

The sequence of this isoform differs from the canonical sequence as follows:
     388-398: ENLEAETAPLP → AFGCCNEHHDQR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Mu-type opioid receptor
PRO_0000069975

Regions

Topological domain1 – 6666Extracellular Ref.32
Transmembrane67 – 9125Helical; Name=1
Topological domain92 – 10413Cytoplasmic Ref.32
Transmembrane105 – 12925Helical; Name=2
Topological domain130 – 14011Extracellular Ref.32
Transmembrane141 – 16323Helical; Name=3
Topological domain164 – 18320Cytoplasmic Ref.32
Transmembrane184 – 20522Helical; Name=4
Topological domain206 – 22823Extracellular Ref.32
Transmembrane229 – 25325Helical; Name=5
Topological domain254 – 28128Cytoplasmic Ref.32
Transmembrane282 – 30524Helical; Name=6
Topological domain306 – 3127Extracellular Ref.32
Transmembrane313 – 33624Helical; Name=7
Topological domain337 – 39862Cytoplasmic Ref.32

Amino acid modifications

Modified residue1661Phosphotyrosine By similarity
Modified residue3631Phosphoserine By similarity
Modified residue3701Phosphothreonine By similarity
Modified residue3751Phosphoserine By similarity
Lipidation3511S-palmitoyl cysteine Potential
Glycosylation91N-linked (GlcNAc...) Potential
Glycosylation311N-linked (GlcNAc...) Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation461N-linked (GlcNAc...) Potential
Disulfide bond140 ↔ 217 Ref.32

Natural variations

Alternative sequence1 – 9494MDSSA…MYVIV → MMEAFSKSAFQKLRQRDGNQ EGKSYL in isoform 14, isoform 15 and isoform 16.
VSP_042332
Alternative sequence387 – 39812LENLE…TAPLP → KKKLDSQRGCVQHPV in isoform 10.
VSP_042333
Alternative sequence387 – 39812LENLE…TAPLP → APCACVPGANRGQTKASDLL DLELETVGSHQADAETNPGP YEGSKCAEPLAISLVPLY in isoform 11.
VSP_042334
Alternative sequence387 – 39812LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDR in isoform 12.
VSP_042335
Alternative sequence387 – 39812LENLE…TAPLP → IMKFEAIYPKLSFKSWALKY FTFIREKKRNTKAGALPTCH AGSPSQAHRGVAAWLLPLRH MGPSYPS in isoform 13.
VSP_042336
Alternative sequence387 – 39812LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDSVDCYNRKQQT GSLRKNKKKKKRRKNKQNIL EAGISRGMRNLLPDDGPRQE SGEGQLGR in isoform 17.
VSP_042337
Alternative sequence387 – 39812LENLE…TAPLP → KQEKTKTKSAWEIWEQKEHT LLLGETHLTIQHLS in isoform 18.
VSP_042338
Alternative sequence387 – 39812LENLE…TAPLP → VCAF in isoform 2.
VSP_042339
Alternative sequence387 – 39812LENLE…TAPLP → KIDLF in isoform 3.
VSP_042340
Alternative sequence387 – 39812LENLE…TAPLP → KLLMWRAMPTFKRHLAIMLS LDN in isoform 4.
VSP_042341
Alternative sequence387 – 39812LENLE…TAPLP → TSLTLQ in isoform 5.
VSP_042342
Alternative sequence387 – 39812LENLE…TAPLP → AHQKPQECLKCRCLSLTILV ICLHFQHQQFFIMIKKNVS in isoform 6.
VSP_042343
Alternative sequence387 – 39812LENLE…TAPLP → CV in isoform 7.
VSP_042344
Alternative sequence387 – 39812LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDRGMRNLLPDDG PRQESGEGQLGR in isoform 8 and isoform 15.
VSP_042345
Alternative sequence387 – 39812LENLE…TAPLP → RNEEPSS in isoform 9 and isoform 16.
VSP_042346
Alternative sequence388 – 39811ENLEAETAPLP → AFGCCNEHHDQR in isoform 19.
VSP_042347

Experimental info

Mutagenesis3871L → A: Abolishes receptor recycling; when associated with A-390. Ref.22
Mutagenesis3901L → A: Abolishes receptor recycling; when associated with A-387. Ref.22
Sequence conflict221C → W in AAA86878. Ref.3

Secondary structure

.......................... 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MOR-1) (MOR-H) (MOR-1J) (MOR-1T) [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DFE1C758E2DA197E

FASTA39844,421
        10         20         30         40         50         60 
MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL GGSHSLCPQT 

        70         80         90        100        110        120 
GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK TATNIYIFNL ALADALATST 

       130        140        150        160        170        180 
LPFQSVNYLM GTWPFGNILC KIVISIDYYN MFTSIFTLCT MSVDRYIAVC HPVKALDFRT 

       190        200        210        220        230        240 
PRNAKIVNVC NWILSSAIGL PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA 

       250        260        270        280        290        300 
FIMPVLIITV CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 

       310        320        330        340        350        360 
IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF CIPTSSTIEQ 

       370        380        390 
QNSARIRQNT REHPSTANTV DRTNHQLENL EAETAPLP 

« Hide

Isoform 2 (MOR-1A) [UniParc].

Checksum: 6B5B6A686C255294
Show »

FASTA39043,563
Isoform 3 (MOR-1B1) [UniParc].

Checksum: AC05BC14999C2552
Show »

FASTA39143,759
Isoform 4 (MOR-1B2) [UniParc].

Checksum: 2DC2D18223481EA6
Show »

FASTA40945,911
Isoform 5 (MOR-1B3) (MOR-1Q) [UniParc].

Checksum: 0272F331816B0C25
Show »

FASTA39243,786
Isoform 6 (MOR-1B4) (MOR-1R) [UniParc].

Checksum: F4DF1831F0FFE9D8
Show »

FASTA42547,752
Isoform 7 (MOR-1B5) (MOR-1P) [UniParc].

Checksum: B6041C2552940375
Show »

FASTA38843,345
Isoform 8 (MOR-1C) [UniParc].

Checksum: C3EEFA233DC7B6AF
Show »

FASTA43848,753
Isoform 9 (MOR-1D) [UniParc].

Checksum: 44A102A98DA09EAC
Show »

FASTA39343,942
Isoform 10 (MOR-1E) (MOR-1Eiii) (MOR-1Eiv) [UniParc].

Checksum: 2C72C33B40623D9C
Show »

FASTA40144,848
Isoform 11 (MOR-1F) [UniParc].

Checksum: B813B308EBDBC7E2
Show »

FASTA44449,094
Isoform 12 (MOR-1O) [UniParc].

Checksum: 287DCE930F4215FA
Show »

FASTA41646,388
Isoform 13 (MOR-1P) (MOR-1R) [UniParc].

Checksum: 7C97FCCB51A405A0
Show »

FASTA45350,715
Isoform 14 (MOR-1G) [UniParc].

Checksum: EFE198DA945CFD69
Show »

FASTA33037,958
Isoform 15 (MOR-1M) [UniParc].

Checksum: 3982458B31042392
Show »

FASTA37042,290
Isoform 16 (MOR-1N) [UniParc].

Checksum: E245158D1F8F8102
Show »

FASTA32537,479
Isoform 17 (MOR-1U) [UniParc].

Checksum: 0CEE0C00E6885C99
Show »

FASTA47452,982
Isoform 18 (MOR-1V) [UniParc].

Checksum: 2D5D6A022EFDAEFD
Show »

FASTA42047,197
Isoform 19 (MOR-1W) [UniParc].

Checksum: 6009B17CC0C8654A
Show »

FASTA39944,654

References

« Hide 'large scale' references
[1]"Genomic structure analysis of promoter sequence of a mouse mu opioid receptor gene."
Min B.H., Augustin L.B., Felsheim R.F., Fuchs J.A., Loh H.H.
Proc. Natl. Acad. Sci. U.S.A. 91:9081-9085(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6.
Tissue: Liver.
[2]"Antisense mapping the MOR-1 opioid receptor: evidence for alternative splicing and a novel morphine-6 beta-glucuronide receptor."
Rossi G.C., Pan Y.X., Brown G.P., Pasternak G.W.
FEBS Lett. 369:192-196(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Characterization of the murine mu opioid receptor gene."
Kaufman D.L., Keith D.E., Anton B., Tian J., Magendzo K., Newman D., Tran T., Lee D.S., Wen C., Xia Y., Lusis A.J., Evans C.J.
J. Biol. Chem. 270:15877-15883(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
Strain: BALB/c.
Tissue: Brain.
[4]"Identification and characterization of three new alternatively spliced mu-opioid receptor isoforms."
Pan Y.X., Xu J., Bolan E., Abbadie C., Chang A., Zuckerman A., Rossi G., Pasternak G.W.
Mol. Pharmacol. 56:396-403(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8; 9 AND 10).
Strain: C57BL/6.
[5]"Identification and characterization of a mouse spliced mu-opioid receptor isoform (MOR-1A)."
Pan Y.-X., Xu J., Chang A., Pasternak G.W.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: CD-1.
[6]"Isolation and expression of a novel alternatively spliced mu opioid receptor isoform, MOR-1F."
Pan Y.X., Xu J., Bolan E., Chang A., Mahurter L., Rossi G., Pasternak G.W.
FEBS Lett. 466:337-340(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11).
Strain: CD-1.
[7]"The untranslated region of (mu)-opioid receptor mRNA contributes to reduced opioid sensitivity in CXBK mice."
Ikeda K., Kobayashi T., Ichikawa T., Kumanishi T., Niki H., Yano R.
J. Neurosci. 21:1334-1339(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: C57BL/6By x BALB/cBy.
Tissue: Brain.
[8]"Generation of the mu opioid receptor (MOR-1) protein by three new splice variants of the Oprm gene."
Pan Y.X., Xu J., Mahurter L., Bolan E., Xu M., Pasternak G.W.
Proc. Natl. Acad. Sci. U.S.A. 98:14084-14089(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 14; 15 AND 16).
Strain: C57BL/6By x BALB/cBy.
[9]"Identification and characterization of a novel splice variant from mouse mu opioid receptor gene (Oprm)."
Pan Y., Xu J., Xu M., Pasternak G.W.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
[10]"Identification and characterization of a new isoform from mouse mu opioid receptor gene Oprm."
Xu J., Pasternak G.W.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
Strain: CD-1.
[11]"Identification of four novel exon 5 splice variants of the mouse mu-opioid receptor gene: functional consequences of C-terminal splicing."
Pan Y.X., Xu J., Bolan E., Moskowitz H.S., Xu M., Pasternak G.W.
Mol. Pharmacol. 68:866-875(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7).
Strain: CD-1.
[12]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
[13]"Identification of five mouse mu-opioid receptor (MOR) gene (Oprm1) splice variants containing a newly identified alternatively spliced exon."
Doyle G.A., Sheng X.R., Lin S.S., Press D.M., Grice D.E., Buono R.J., Ferraro T.N., Berrettini W.H.
Gene 395:98-107(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 10; 17; 18 AND 19).
Strain: C57BL/6.
Tissue: Brain.
[14]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[16]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
[17]"Opiate receptor knockout mice define mu receptor roles in endogenous nociceptive responses and morphine-induced analgesia."
Sora I., Takahashi N., Funada M., Ujike H., Revay R.S., Donovan D.M., Miner L.L., Uhl G.R.
Proc. Natl. Acad. Sci. U.S.A. 94:1544-1549(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Influence of Gz and Gi2 transducer proteins in the affinity of opioid agonists to mu receptors."
Garzon J., Castro M., Sanchez-Blazquez P.
Eur. J. Neurosci. 10:2557-2564(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: COUPLING TO GNAZ.
[19]"Oligomerization of mu- and delta-opioid receptors. Generation of novel functional properties."
George S.R., Fan T., Xie Z., Tse R., Tam V., Varghese G., O'Dowd B.F.
J. Biol. Chem. 275:26128-26135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR HETEROOLIGOMERIZATION, FUNCTION, INTERACTION WITH OPRD1.
[20]"Dimerization of morphine and orphanin FQ/nociceptin receptors: generation of a novel opioid receptor subtype."
Pan Y.X., Bolan E., Pasternak G.W.
Biochem. Biophys. Res. Commun. 297:659-663(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRL1.
[21]"Opioid agonists have different efficacy profiles for G protein activation, rapid desensitization, and endocytosis of mu-opioid receptors."
Borgland S.L., Connor M., Osborne P.B., Furness J.B., Christie M.J.
J. Biol. Chem. 278:18776-18784(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR DESENSITIZATION, SUBCELLULAR LOCATION, RECEPTOR INTERNALIZATION.
[22]"A novel endocytic recycling signal that distinguishes the membrane trafficking of naturally occurring opioid receptors."
Tanowitz M., von Zastrow M.
J. Biol. Chem. 278:45978-45986(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR RECYCLING, MUTAGENESIS OF LEU-387 AND LEU-390.
[23]"Genetic analysis of the murine mu opioid receptor: increased complexity of Oprm gene splicing."
Kvam T.M., Baar C., Rakvag T.T., Kaasa S., Krokan H.E., Skorpen F.
J. Mol. Med. 82:250-255(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[24]"The RGSZ2 protein exists in a complex with mu-opioid receptors and regulates the desensitizing capacity of Gz proteins."
Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Sanchez-Blazquez P.
Neuropsychopharmacology 30:1632-1648(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RGS17 AND RGS20.
[25]"mu opioid and CB1 cannabinoid receptor interactions: reciprocal inhibition of receptor signaling and neuritogenesis."
Rios C., Gomes I., Devi L.A.
Br. J. Pharmacol. 148:387-395(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[26]"RGS9-2 is a negative modulator of mu-opioid receptor function."
Psifogeorgou K., Papakosta P., Russo S.J., Neve R.L., Kardassis D., Gold S.J., Zachariou V.
J. Neurochem. 103:617-625(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RGS9.
[27]"Multiple actions of spinophilin regulate mu opioid receptor function."
Charlton J.J., Allen P.B., Psifogeorgou K., Chakravarty S., Gomes I., Neve R.L., Devi L.A., Greengard P., Nestler E.J., Zachariou V.
Neuron 58:238-247(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R9B.
[28]"Cell surface targeting of mu-delta opioid receptor heterodimers by RTP4."
Decaillot F.M., Rozenfeld R., Gupta A., Devi L.A.
Proc. Natl. Acad. Sci. U.S.A. 105:16045-16050(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRD1 AND RTP4.
[29]"Unidirectional cross-activation of GRPR by MOR1D uncouples itch and analgesia induced by opioids."
Liu X.Y., Liu Z.C., Sun Y.G., Ross M., Kim S., Tsai F.F., Li Q.F., Jeffry J., Kim J.Y., Loh H.H., Chen Z.F.
Cell 147:447-458(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 9), INTERACTION WITH GRPR.
[30]"The histidine triad nucleotide-binding protein 1 supports mu-opioid receptor-glutamate NMDA receptor cross-regulation."
Rodriguez-Munoz M., Sanchez-Blazquez P., Vicente-Sanchez A., Bailon C., Martin-Aznar B., Garzon J.
Cell. Mol. Life Sci. 68:2933-2949(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HINT1.
[31]"Heteromerization of the mu- and delta-opioid receptors produces ligand-biased antagonism and alters mu-receptor trafficking."
Milan-Lobo L., Whistler J.L.
J. Pharmacol. Exp. Ther. 337:868-875(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: RECEPTOR HETEROOLIGOMERIZATION, FUNCTION, INTERACTION WITH OPRD1.
[32]"Crystal structure of the micro-opioid receptor bound to a morphinan antagonist."
Manglik A., Kruse A.C., Kobilka T.S., Thian F.S., Mathiesen J.M., Sunahara R.K., Pardo L., Weis W.I., Kobilka B.K., Granier S.
Nature 485:321-326(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 52-360 IN COMPLEX WITH MORPHINAN ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10561 expand/collapse EMBL AC list , U10558, U10559, U10560 Genomic DNA. Translation: AAB60673.1.
U26915 mRNA. Translation: AAA81170.1.
U19380 mRNA. Translation: AAA86878.1.
AF062753 mRNA. Translation: AAD54415.1.
AF074973 mRNA. Translation: AAD51861.1.
AF074974 mRNA. Translation: AAD51862.1.
AF167565 mRNA. Translation: AAL55581.1.
AF167568 mRNA. Translation: AAF79213.1.
AB047546 mRNA. Translation: BAB63338.1.
AF062755 mRNA. Translation: AAL34927.1.
AF260311 mRNA. Translation: AAL34400.1.
AF074972 mRNA. Translation: AAL34394.1.
AF400246 mRNA. Translation: AAL34507.1.
AF400247 mRNA. Translation: AAL34508.1.
AF400248 mRNA. Translation: AAL34509.1.
AY036621 mRNA. Translation: AAK74188.1.
AY160190 mRNA. Translation: AAO18365.1.
AF167566 mRNA. Translation: AAL55582.1.
AF167567 mRNA. Translation: AAL55583.1.
AF346812 mRNA. Translation: AAO13792.1.
AF346813 mRNA. Translation: AAO13793.1.
AF346814 mRNA. Translation: AAO13794.1.
AK038389 mRNA. Translation: BAC29982.1.
DQ363376 mRNA. Translation: ABC94862.1.
DQ363377 mRNA. Translation: ABC94863.1.
DQ868787 mRNA. Translation: ABI95796.1.
DQ868788 mRNA. Translation: ABI95797.2.
EF105311 mRNA. Translation: ABN45760.1.
EF105312 mRNA. Translation: ABN45761.1.
EF105313 mRNA. Translation: ABN45762.1.
EF105314 mRNA. Translation: ABN45763.1.
CH466562 Genomic DNA. Translation: EDL03560.1.
CH466562 Genomic DNA. Translation: EDL03561.1.
CH466562 Genomic DNA. Translation: EDL03562.1.
AC153981 Genomic DNA. No translation available.
AC155718 Genomic DNA. No translation available.
AC164171 Genomic DNA. No translation available.
BC119545 mRNA. Translation: AAI19546.1.
CCDSCCDS56687.1. [P42866-8]
PIRA57510.
RefSeqNP_001034741.1. NM_001039652.1. [P42866-8]
XP_006512501.1. XM_006512438.1. [P42866-1]
UniGeneMm.439715.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DKLX-ray2.80A52-360[»]
ProteinModelPortalP42866.
SMRP42866. Positions 61-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46148N.
IntActP42866. 7 interactions.
MINTMINT-8298941.
STRING10090.ENSMUSP00000101239.

Chemistry

BindingDBP42866.
ChEMBLCHEMBL2095192.
GuidetoPHARMACOLOGY319.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP42866.

Proteomic databases

PaxDbP42866.
PRIDEP42866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000783; ENSMUSP00000000783; ENSMUSG00000000766. [P42866-6]
ENSMUST00000052751; ENSMUSP00000060329; ENSMUSG00000000766. [P42866-9]
ENSMUST00000056385; ENSMUSP00000060590; ENSMUSG00000000766. [P42866-1]
ENSMUST00000063036; ENSMUSP00000053498; ENSMUSG00000000766. [P42866-16]
ENSMUST00000078634; ENSMUSP00000077704; ENSMUSG00000000766.
ENSMUST00000092729; ENSMUSP00000090405; ENSMUSG00000000766. [P42866-7]
ENSMUST00000092731; ENSMUSP00000090407; ENSMUSG00000000766. [P42866-5]
ENSMUST00000092734; ENSMUSP00000090410; ENSMUSG00000000766. [P42866-1]
ENSMUST00000105602; ENSMUSP00000101227; ENSMUSG00000000766. [P42866-2]
ENSMUST00000105605; ENSMUSP00000101230; ENSMUSG00000000766. [P42866-3]
ENSMUST00000105607; ENSMUSP00000101232; ENSMUSG00000000766. [P42866-1]
ENSMUST00000105611; ENSMUSP00000101236; ENSMUSG00000000766. [P42866-8]
ENSMUST00000105615; ENSMUSP00000101240; ENSMUSG00000000766. [P42866-15]
ENSMUST00000135502; ENSMUSP00000135143; ENSMUSG00000000766. [P42866-12]
ENSMUST00000144264; ENSMUSP00000115836; ENSMUSG00000000766. [P42866-19]
ENSMUST00000147171; ENSMUSP00000117950; ENSMUSG00000000766. [P42866-14]
ENSMUST00000154906; ENSMUSP00000114342; ENSMUSG00000000766. [P42866-4]
GeneID18390.
KEGGmmu:18390.
UCSCuc007eff.1. mouse. [P42866-9]
uc007efl.1. mouse. [P42866-17]
uc007efn.1. mouse. [P42866-8]
uc007efp.1. mouse. [P42866-15]
uc007efq.1. mouse. [P42866-16]
uc007eft.1. mouse. [P42866-12]
uc007efw.2. mouse. [P42866-1]
uc007egc.1. mouse. [P42866-14]
uc007ege.1. mouse. [P42866-3]
uc007egf.1. mouse. [P42866-2]

Organism-specific databases

CTD4988.
MGIMGI:97441. Oprm1.

Phylogenomic databases

eggNOGNOG279457.
GeneTreeENSGT00630000089574.
HOGENOMHOG000230486.
HOVERGENHBG106919.
KOK04215.
OMARARCNIS.
OrthoDBEOG7BKCVQ.
TreeFamTF315737.

Gene expression databases

ArrayExpressP42866.
BgeeP42866.
CleanExMM_OPRM1.
GenevestigatorP42866.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000105. Mu_opioid_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00537. MUOPIOIDR.
PR00384. OPIOIDR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio293988.
PROP42866.
SOURCESearch...

Entry information

Entry nameOPRM_MOUSE
AccessionPrimary (citable) accession number: P42866
Secondary accession number(s): A1XGX3 expand/collapse secondary AC list , A1XGX4, A1YAC3, A1YAC4, A5H7G2, Q4U2P4, Q4U2Q6, Q548C6, Q60768, Q6YC50, Q8CAN5, Q8CGW2, Q8CH73, Q8CH74, Q8CH75, Q8VBU3, Q8VBU6, Q8VBX8, Q8VI69, Q8VI70, Q8VI71, Q8VIN3, Q8VIN4, Q8VIN5, Q8VIN6, Q8VIP0, Q8VIP1, Q9JIY1, Q9R0D1, Q9R1L9, Q9R1M0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries