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P42866

- OPRM_MOUSE

UniProt

P42866 - OPRM_MOUSE

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Protein

Mu-type opioid receptor

Gene

Oprm1

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

Functioni

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.6 Publications

GO - Molecular functioni

  1. beta-endorphin receptor activity Source: Ensembl
  2. G-protein alpha-subunit binding Source: UniProtKB
  3. G-protein coupled receptor activity Source: UniProtKB
  4. morphine receptor activity Source: UniProtKB
  5. opioid receptor activity Source: MGI
  6. voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  1. adenylate cyclase-activating dopamine receptor signaling pathway Source: MGI
  2. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: MGI
  3. behavioral response to ethanol Source: Ensembl
  4. calcium ion transmembrane transport Source: GOC
  5. cellular response to stress Source: Ensembl
  6. locomotory behavior Source: MGI
  7. negative regulation of adenylate cyclase activity Source: UniProtKB
  8. negative regulation of cAMP-mediated signaling Source: UniProtKB
  9. negative regulation of cytosolic calcium ion concentration Source: UniProtKB
  10. negative regulation of nitric oxide biosynthetic process Source: UniProtKB
  11. negative regulation of Wnt protein secretion Source: UniProtKB
  12. opioid receptor signaling pathway Source: GOC
  13. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  14. positive regulation of cAMP-mediated signaling Source: Ensembl
  15. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  16. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  17. positive regulation of neurogenesis Source: UniProtKB
  18. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  19. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: UniProtKB
  20. sensory perception of pain Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_205726. G-protein activation.
REACT_235286. Peptide ligand-binding receptors.
REACT_242845. Opioid Signalling.
REACT_250376. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Mu-type opioid receptor
Short name:
M-OR-1
Short name:
MOR-1
Gene namesi
Name:Oprm1
Synonyms:Mor, Oprm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:97441. Oprm1.

Subcellular locationi

Cell membrane 3 Publications; Multi-pass membrane protein 3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6666Extracellular1 PublicationAdd
BLAST
Transmembranei67 – 9125Helical; Name=1Add
BLAST
Topological domaini92 – 10413Cytoplasmic1 PublicationAdd
BLAST
Transmembranei105 – 12925Helical; Name=2Add
BLAST
Topological domaini130 – 14011Extracellular1 PublicationAdd
BLAST
Transmembranei141 – 16323Helical; Name=3Add
BLAST
Topological domaini164 – 18320Cytoplasmic1 PublicationAdd
BLAST
Transmembranei184 – 20522Helical; Name=4Add
BLAST
Topological domaini206 – 22823Extracellular1 PublicationAdd
BLAST
Transmembranei229 – 25325Helical; Name=5Add
BLAST
Topological domaini254 – 28128Cytoplasmic1 PublicationAdd
BLAST
Transmembranei282 – 30524Helical; Name=6Add
BLAST
Topological domaini306 – 3127Extracellular1 Publication
Transmembranei313 – 33624Helical; Name=7Add
BLAST
Topological domaini337 – 39862Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: MGI
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

During adult neurogenesis in hippocampus, increased numbers of granule cells maturing into neurons, larger granule cell layers and increased numbers of granule cells.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi387 – 3871L → A: Abolishes receptor recycling; when associated with A-390. 1 Publication
Mutagenesisi390 – 3901L → A: Abolishes receptor recycling; when associated with A-387. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Mu-type opioid receptorPRO_0000069975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi9 – 91N-linked (GlcNAc...)Sequence Analysis
Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi140 ↔ 2171 PublicationPROSITE-ProRule annotation
Modified residuei166 – 1661PhosphotyrosineBy similarity
Lipidationi351 – 3511S-palmitoyl cysteineSequence Analysis
Modified residuei363 – 3631PhosphoserineBy similarity
Modified residuei370 – 3701PhosphothreonineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity

Post-translational modificationi

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 RTP4.1 Publication

Keywords - PTMi

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

Proteomic databases

PaxDbiP42866.
PRIDEiP42866.

PTM databases

PhosphoSiteiP42866.

Expressioni

Gene expression databases

BgeeiP42866.
CleanExiMM_OPRM1.
ExpressionAtlasiP42866. differential.
GenevestigatoriP42866.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GNASP63092-22EBI-5282656,EBI-7607528From a different organism.
GrprP217294EBI-6049667,EBI-6049651

Protein-protein interaction databases

DIPiDIP-46148N.
IntActiP42866. 7 interactions.
MINTiMINT-8298941.
STRINGi10090.ENSMUSP00000101239.

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi66 – 9530Combined sources
Helixi102 – 13029Combined sources
Helixi138 – 17033Combined sources
Helixi172 – 1787Combined sources
Helixi181 – 20424Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi222 – 2243Combined sources
Helixi225 – 23915Combined sources
Helixi242 – 25817Combined sources
Helixi273 – 30533Combined sources
Helixi312 – 33928Combined sources
Helixi341 – 35111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DKLX-ray2.80A52-360[»]
ProteinModelPortaliP42866.
SMRiP42866. Positions 61-352.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG279457.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP42866.
KOiK04215.
OMAiRARCNIS.
OrthoDBiEOG7BKCVQ.
TreeFamiTF315737.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000105. Mu_opioid_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR00537. MUOPIOIDR.
PR00384. OPIOIDR.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequences (19)i

Sequence statusi: Complete.

This entry describes 19 isoformsi produced by alternative splicing. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL
60 70 80 90 100
GGSHSLCPQT GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK
110 120 130 140 150
TATNIYIFNL ALADALATST LPFQSVNYLM GTWPFGNILC 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 QNSARIRQNT REHPSTANTV DRTNHQLENL EAETAPLP
Length:398
Mass (Da):44,421
Last modified:November 1, 1995 - v1
Checksum:iDFE1C758E2DA197E
GO
Isoform 2 (identifier: P42866-2) [UniParc]FASTAAdd to Basket

Also known as: MOR-1A

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

Show »
Length:390
Mass (Da):43,563
Checksum:i6B5B6A686C255294
GO
Isoform 3 (identifier: P42866-3) [UniParc]FASTAAdd to Basket

Also known as: MOR-1B1

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

Show »
Length:391
Mass (Da):43,759
Checksum:iAC05BC14999C2552
GO
Isoform 4 (identifier: P42866-4) [UniParc]FASTAAdd to Basket

Also known as: MOR-1B2

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

Show »
Length:409
Mass (Da):45,911
Checksum:i2DC2D18223481EA6
GO
Isoform 5 (identifier: P42866-5) [UniParc]FASTAAdd to Basket

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

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

Show »
Length:392
Mass (Da):43,786
Checksum:i0272F331816B0C25
GO
Isoform 6 (identifier: P42866-6) [UniParc]FASTAAdd to Basket

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

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

Show »
Length:425
Mass (Da):47,752
Checksum:iF4DF1831F0FFE9D8
GO
Isoform 7 (identifier: P42866-7) [UniParc]FASTAAdd to Basket

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

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

Show »
Length:388
Mass (Da):43,345
Checksum:iB6041C2552940375
GO
Isoform 8 (identifier: P42866-8) [UniParc]FASTAAdd to Basket

Also known as: MOR-1C

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

Show »
Length:438
Mass (Da):48,753
Checksum:iC3EEFA233DC7B6AF
GO
Isoform 9 (identifier: P42866-9) [UniParc]FASTAAdd to Basket

Also known as: MOR-1D

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

Show »
Length:393
Mass (Da):43,942
Checksum:i44A102A98DA09EAC
GO
Isoform 10 (identifier: P42866-10) [UniParc]FASTAAdd to Basket

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

Show »
Length:401
Mass (Da):44,848
Checksum:i2C72C33B40623D9C
GO
Isoform 11 (identifier: P42866-11) [UniParc]FASTAAdd to Basket

Also known as: MOR-1F

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

Show »
Length:444
Mass (Da):49,094
Checksum:iB813B308EBDBC7E2
GO
Isoform 12 (identifier: P42866-12) [UniParc]FASTAAdd to Basket

Also known as: MOR-1O

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

Show »
Length:416
Mass (Da):46,388
Checksum:i287DCE930F4215FA
GO
Isoform 13 (identifier: P42866-13) [UniParc]FASTAAdd to Basket

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

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

Show »
Length:453
Mass (Da):50,715
Checksum:i7C97FCCB51A405A0
GO
Isoform 14 (identifier: P42866-14) [UniParc]FASTAAdd to Basket

Also known as: MOR-1G

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MDSSAGPGNI...GNFLVMYVIV → MMEAFSKSAFQKLRQRDGNQEGKSYL

Show »
Length:330
Mass (Da):37,958
Checksum:iEFE198DA945CFD69
GO
Isoform 15 (identifier: P42866-15) [UniParc]FASTAAdd to Basket

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

Show »
Length:370
Mass (Da):42,290
Checksum:i3982458B31042392
GO
Isoform 16 (identifier: P42866-16) [UniParc]FASTAAdd to Basket

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

Show »
Length:325
Mass (Da):37,479
Checksum:iE245158D1F8F8102
GO
Isoform 17 (identifier: P42866-17) [UniParc]FASTAAdd to Basket

Also known as: MOR-1U

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

Show »
Length:474
Mass (Da):52,982
Checksum:i0CEE0C00E6885C99
GO
Isoform 18 (identifier: P42866-18) [UniParc]FASTAAdd to Basket

Also known as: MOR-1V

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

Show »
Length:420
Mass (Da):47,197
Checksum:i2D5D6A022EFDAEFD
GO
Isoform 19 (identifier: P42866-19) [UniParc]FASTAAdd to Basket

Also known as: MOR-1W

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

Show »
Length:399
Mass (Da):44,654
Checksum:i6009B17CC0C8654A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221C → W in AAA86878. (PubMed:7797593)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9494MDSSA…MYVIV → MMEAFSKSAFQKLRQRDGNQ EGKSYL in isoform 14, isoform 15 and isoform 16. 1 PublicationVSP_042332Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → KKKLDSQRGCVQHPV in isoform 10. 2 PublicationsVSP_042333Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → APCACVPGANRGQTKASDLL DLELETVGSHQADAETNPGP YEGSKCAEPLAISLVPLY in isoform 11. 1 PublicationVSP_042334Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDR in isoform 12. 1 PublicationVSP_042335Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → IMKFEAIYPKLSFKSWALKY FTFIREKKRNTKAGALPTCH AGSPSQAHRGVAAWLLPLRH MGPSYPS in isoform 13. 1 PublicationVSP_042336Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDSVDCYNRKQQT GSLRKNKKKKKRRKNKQNIL EAGISRGMRNLLPDDGPRQE SGEGQLGR in isoform 17. 1 PublicationVSP_042337Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → KQEKTKTKSAWEIWEQKEHT LLLGETHLTIQHLS in isoform 18. 1 PublicationVSP_042338Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → VCAF in isoform 2. 1 PublicationVSP_042339Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → KIDLF in isoform 3. 1 PublicationVSP_042340Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → KLLMWRAMPTFKRHLAIMLS LDN in isoform 4. 1 PublicationVSP_042341Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → TSLTLQ in isoform 5. 1 PublicationVSP_042342Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → AHQKPQECLKCRCLSLTILV ICLHFQHQQFFIMIKKNVS in isoform 6. 1 PublicationVSP_042343Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → CV in isoform 7. 1 PublicationVSP_042344Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → PTLAVSVAQIFTGYPSPTHV EKPCKSCMDRGMRNLLPDDG PRQESGEGQLGR in isoform 8 and isoform 15. 4 PublicationsVSP_042345Add
BLAST
Alternative sequencei387 – 39812LENLE…TAPLP → RNEEPSS in isoform 9 and isoform 16. 2 PublicationsVSP_042346Add
BLAST
Alternative sequencei388 – 39811ENLEAETAPLP → AFGCCNEHHDQR in isoform 19. 1 PublicationVSP_042347Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10561
, 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.
CCDSiCCDS56687.1. [P42866-8]
PIRiA57510.
RefSeqiNP_001034741.1. NM_001039652.2. [P42866-8]
XP_006512501.1. XM_006512438.1. [P42866-1]
UniGeneiMm.439715.

Genome annotation databases

EnsembliENSMUST00000000783; 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]
GeneIDi18390.
KEGGimmu:18390.
UCSCiuc007eff.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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10561
, 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 .
CCDSi CCDS56687.1. [P42866-8 ]
PIRi A57510.
RefSeqi NP_001034741.1. NM_001039652.2. [P42866-8 ]
XP_006512501.1. XM_006512438.1. [P42866-1 ]
UniGenei Mm.439715.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4DKL X-ray 2.80 A 52-360 [» ]
ProteinModelPortali P42866.
SMRi P42866. Positions 61-352.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-46148N.
IntActi P42866. 7 interactions.
MINTi MINT-8298941.
STRINGi 10090.ENSMUSP00000101239.

Chemistry

BindingDBi P42866.
ChEMBLi CHEMBL2095192.
GuidetoPHARMACOLOGYi 319.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei P42866.

Proteomic databases

PaxDbi P42866.
PRIDEi P42866.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000783 ; 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 ]
GeneIDi 18390.
KEGGi mmu:18390.
UCSCi uc007eff.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

CTDi 4988.
MGIi MGI:97441. Oprm1.

Phylogenomic databases

eggNOGi NOG279457.
GeneTreei ENSGT00760000118797.
HOGENOMi HOG000230486.
HOVERGENi HBG106919.
InParanoidi P42866.
KOi K04215.
OMAi RARCNIS.
OrthoDBi EOG7BKCVQ.
TreeFami TF315737.

Enzyme and pathway databases

Reactomei REACT_205726. G-protein activation.
REACT_235286. Peptide ligand-binding receptors.
REACT_242845. Opioid Signalling.
REACT_250376. G alpha (i) signalling events.

Miscellaneous databases

NextBioi 293988.
PROi P42866.
SOURCEi Search...

Gene expression databases

Bgeei P42866.
CleanExi MM_OPRM1.
ExpressionAtlasi P42866. differential.
Genevestigatori P42866.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
InterProi IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR000105. Mu_opioid_rcpt.
IPR001418. Opioid_rcpt.
[Graphical view ]
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00237. GPCRRHODOPSN.
PR00537. MUOPIOIDR.
PR00384. OPIOIDR.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. Cited for: INTERACTION WITH RGS9.
  27. 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.

Entry informationi

Entry nameiOPRM_MOUSE
AccessioniPrimary (citable) accession number: P42866
Secondary accession number(s): A1XGX3
, 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 historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3