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P42866

- OPRM_MOUSE

UniProt

P42866 - OPRM_MOUSE

Protein

Mu-type opioid receptor

Gene

Oprm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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. protein binding Source: IntAct
    7. 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 behavior Source: Ensembl
    20. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: UniProtKB
    21. sensory perception of pain Source: UniProtKB

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_205726. G-protein activation.

    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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: MGI
    3. plasma membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiP42866.
    BgeeiP42866.
    CleanExiMM_OPRM1.
    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 – 9530
    Helixi102 – 13029
    Helixi138 – 17033
    Helixi172 – 1787
    Helixi181 – 20424
    Beta strandi209 – 2113
    Beta strandi214 – 2163
    Beta strandi222 – 2243
    Helixi225 – 23915
    Helixi242 – 25817
    Helixi273 – 30533
    Helixi312 – 33928
    Helixi341 – 35111

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6666Extracellular1 PublicationAdd
    BLAST
    Topological domaini92 – 10413Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini130 – 14011Extracellular1 PublicationAdd
    BLAST
    Topological domaini164 – 18320Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini206 – 22823Extracellular1 PublicationAdd
    BLAST
    Topological domaini254 – 28128Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini306 – 3127Extracellular1 Publication
    Topological domaini337 – 39862Cytoplasmic1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei67 – 9125Helical; Name=1Add
    BLAST
    Transmembranei105 – 12925Helical; Name=2Add
    BLAST
    Transmembranei141 – 16323Helical; Name=3Add
    BLAST
    Transmembranei184 – 20522Helical; Name=4Add
    BLAST
    Transmembranei229 – 25325Helical; Name=5Add
    BLAST
    Transmembranei282 – 30524Helical; Name=6Add
    BLAST
    Transmembranei313 – 33624Helical; Name=7Add
    BLAST

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG279457.
    GeneTreeiENSGT00630000089574.
    HOGENOMiHOG000230486.
    HOVERGENiHBG106919.
    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

    MDSSAGPGNI SDCSDPLAPA SCSPAPGSWL NLSHVDGNQS DPCGPNRTGL    50
    GGSHSLCPQT GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK 100
    TATNIYIFNL ALADALATST LPFQSVNYLM GTWPFGNILC KIVISIDYYN 150
    MFTSIFTLCT MSVDRYIAVC HPVKALDFRT PRNAKIVNVC NWILSSAIGL 200
    PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA FIMPVLIITV 250
    CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV 300
    IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF 350
    CIPTSSTIEQ QNSARIRQNT REHPSTANTV DRTNHQLENL EAETAPLP 398
    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:
    EMBL
    GenBank
    DDBJ
    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_001039652.1. [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:
    EMBL
    GenBank
    DDBJ
    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_001039652.1. [P42866-8 ]
    XP_006512501.1. XM_006512438.1. [P42866-1 ]
    UniGenei Mm.439715.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 ENSGT00630000089574.
    HOGENOMi HOG000230486.
    HOVERGENi HBG106919.
    KOi K04215.
    OMAi RARCNIS.
    OrthoDBi EOG7BKCVQ.
    TreeFami TF315737.

    Enzyme and pathway databases

    Reactomei REACT_205726. G-protein activation.

    Miscellaneous databases

    NextBioi 293988.
    PROi P42866.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42866.
    Bgeei P42866.
    CleanExi MM_OPRM1.
    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

    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: October 1, 2014
    This is version 127 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