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P35372

- OPRM_HUMAN

UniProt

P35372 - OPRM_HUMAN

Protein

Mu-type opioid receptor

Gene

OPRM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Receptor for endogenous opioids such as beta-endorphin and endomorphin. Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone. Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors. The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser 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 whereas morphine induces only low desensitization and endocytosis. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis. Isoform 12 couples to GNAS and is proposed to be involved in excitatory effects. Isoform 16 and isoform 17 do not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity.

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_14819. Peptide ligand-binding receptors.
    REACT_15295. Opioid Signalling.
    REACT_15457. G-protein activation.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mu-type opioid receptor
    Short name:
    M-OR-1
    Short name:
    MOR-1
    Alternative name(s):
    Mu opiate receptor
    Mu opioid receptor
    Short name:
    MOP
    Short name:
    hMOP
    Gene namesi
    Name:OPRM1
    Synonyms:MOR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8156. OPRM1.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Isoform 12 : Cytoplasm 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: ProtInc
    2. Golgi apparatus Source: ProtInc
    3. integral component of plasma membrane Source: ProtInc
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi142 – 1421C → A or S: Abolishes ligand binding; when associated with A-219 or S-219. 1 Publication
    Mutagenesisi219 – 2191C → A or S: Abolishes ligand binding; when associated with A-142 or S-142. 1 Publication
    Mutagenesisi273 – 2731K → A: Impairs interaction with calmodulin. 2 Publications
    Mutagenesisi275 – 2751R → A: Impairs interaction with calmodulin. 1 Publication

    Organism-specific databases

    PharmGKBiPA31945.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 400400Mu-type opioid receptorPRO_0000069972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi9 – 91N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi12 – 121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi142 ↔ 219PROSITE-ProRule annotation
    Modified residuei168 – 1681PhosphotyrosineBy similarity
    Lipidationi353 – 3531S-palmitoyl cysteineSequence Analysis
    Modified residuei365 – 3651PhosphoserineBy similarity
    Modified residuei372 – 3721PhosphothreonineBy similarity
    Modified residuei377 – 3771PhosphoserineBy 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-168 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-377 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway By similarity.By similarity
    Ubiquitinated. A basal ubiquitination seems not to be related to degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1 oligomers leading to proteasomal degradation; the ubiquitination is diminished by RTP4 By similarity.By similarity

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiP35372.
    PRIDEiP35372.

    PTM databases

    PhosphoSiteiP35372.

    Expressioni

    Tissue specificityi

    Expressed in brain. Isoform 16 and isoform 17 are detected in brain.1 Publication

    Gene expression databases

    ArrayExpressiP35372.
    BgeeiP35372.
    CleanExiHS_OPRM1.
    GenevestigatoriP35372.

    Organism-specific databases

    HPAiHPA014509.

    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. Interacts with GPM6A, RTP4, SYP, GNAS, RGS9, RGS17, RGS20, RGS4, PPP1R9B and HINT1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AUP1Q9Y6794EBI-2624570,EBI-1058701
    COPS5Q929055EBI-2624570,EBI-594661
    DOK4Q8TEW64EBI-2624570,EBI-6918542
    FLNAP213335EBI-2624570,EBI-350432
    GJA4P352122EBI-2624570,EBI-6918707
    RANBP9Q96S595EBI-2624570,EBI-636085
    SIAH1Q8IUQ44EBI-2624570,EBI-747107
    SIAH2O432553EBI-2624570,EBI-948141
    VAPAQ9P0L03EBI-2624570,EBI-1059156
    WLSQ5T9L310EBI-2624570,EBI-2868748
    ZYXQ159422EBI-2624570,EBI-444225

    Protein-protein interaction databases

    BioGridi111033. 7 interactions.
    IntActiP35372. 15 interactions.
    MINTiMINT-100121.

    Structurei

    3D structure databases

    DisProtiDP00272.
    ProteinModelPortaliP35372.
    SMRiP35372. Positions 63-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6868ExtracellularBy similarityAdd
    BLAST
    Topological domaini94 – 10613CytoplasmicBy similarityAdd
    BLAST
    Topological domaini132 – 14211ExtracellularBy similarityAdd
    BLAST
    Topological domaini166 – 18520CytoplasmicBy similarityAdd
    BLAST
    Topological domaini208 – 23023ExtracellularBy similarityAdd
    BLAST
    Topological domaini256 – 28328CytoplasmicBy similarityAdd
    BLAST
    Topological domaini308 – 3147ExtracellularBy similarity
    Topological domaini339 – 40062CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei69 – 9325Helical; Name=1By similarityAdd
    BLAST
    Transmembranei107 – 13125Helical; Name=2By similarityAdd
    BLAST
    Transmembranei143 – 16523Helical; Name=3By similarityAdd
    BLAST
    Transmembranei186 – 20722Helical; Name=4By similarityAdd
    BLAST
    Transmembranei231 – 25525Helical; Name=5By similarityAdd
    BLAST
    Transmembranei284 – 30724Helical; Name=6By similarityAdd
    BLAST
    Transmembranei315 – 33824Helical; Name=7By similarityAdd
    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.
    HOGENOMiHOG000230486.
    HOVERGENiHBG106919.
    InParanoidiP35372.
    KOiK04215.
    OMAiNSTRVRQ.
    PhylomeDBiP35372.
    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 (18)i

    Sequence statusi: Complete.

    This entry describes 18 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P35372-1) [UniParc]FASTAAdd to Basket

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

    « Hide

    MDSSAAPTNA SNCTDALAYS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT    50
    DLGGRDSLCP PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK 100
    MKTATNIYIF NLALADALAT STLPFQSVNY LMGTWPFGTI LCKIVISIDY 150
    YNMFTSIFTL CTMSVDRYIA VCHPVKALDF RTPRNAKIIN VCNWILSSAI 200
    GLPVMFMATT KYRQGSIDCT LTFSHPTWYW ENLLKICVFI FAFIMPVLII 250
    TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIVCWTPIHI 300
    YVIIKALVTI PETTFQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR 350
    EFCIPTSSNI EQQNSTRIRQ NTRDHPSTAN TVDRTNHQLE NLEAETAPLP 400
    Length:400
    Mass (Da):44,779
    Last modified:July 15, 1998 - v2
    Checksum:i1DABEBEC9AFF6F66
    GO
    Isoform 2 (identifier: P35372-2) [UniParc]FASTAAdd to Basket

    Also known as: MOR1A, MOR-1A

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → VRSL

    Show »
    Length:392
    Mass (Da):43,957
    Checksum:i14184C69F06AFCBE
    GO
    Isoform 3 (identifier: P35372-3) [UniParc]FASTAAdd to Basket

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

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → CLPIPSLSCWALEQGCLVVYPGPLQGPLVRYDLPAILHSSCLRGNTAPSPSGGAFLLS

    Show »
    Length:446
    Mass (Da):49,520
    Checksum:i42DC76968E6352A8
    GO
    Isoform 4 (identifier: P35372-4) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1B3

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → GPPAKFVADQLAGSS

    Show »
    Length:403
    Mass (Da):44,928
    Checksum:iB3FFA10F7B1C5311
    GO
    Isoform 5 (identifier: P35372-5) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1C, MOR-1O

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → PPLAVSMAQIFTRYPPPTHREKTCNDYMKR

    Show »
    Length:418
    Mass (Da):47,032
    Checksum:i51B9E7B131122196
    GO
    Isoform 6 (identifier: P35372-6) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1V, MOR-1Y, MOR-1Y2, MOR-1Y3

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → IRDPISNLPRVSVF

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:402
    Mass (Da):45,096
    Checksum:i5BC8380AB8196D70
    GO
    Isoform 7 (identifier: P35372-7) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1B1

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → KIDLFQKSSLLNCEHTKG

    Show »
    Length:406
    Mass (Da):45,544
    Checksum:i1A0330578A82B183
    GO
    Isoform 8 (identifier: P35372-8) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1B2

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → RERRQKSDW

    Show »
    Length:397
    Mass (Da):44,743
    Checksum:i3BC7E1C19B9739E3
    GO
    Isoform 9 (identifier: P35372-9) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1B5

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → VELNLDCHCENAKPWPLSYNAGQSPFPFPGRV

    Show »
    Length:420
    Mass (Da):47,070
    Checksum:i63301322222198DE
    GO
    Isoform 10 (identifier: P35372-10) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1i

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MCLHRRVPSE...SGARPAVSTM

    Show »
    Length:493
    Mass (Da):55,045
    Checksum:i14A90F782A013067
    GO
    Isoform 11 (identifier: P35372-11) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1B4

    The sequence of this isoform differs from the canonical sequence as follows:
         389-400: LENLEAETAPLP → S

    Show »
    Length:389
    Mass (Da):43,588
    Checksum:i7E806AFCBE572CD5
    GO
    Isoform 12 (identifier: P35372-12) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1G1, MOR-1K

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.

    Show »
    Length:300
    Mass (Da):34,393
    Checksum:i03FE8402349A629C
    GO
    Isoform 13 (identifier: P35372-13) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1G2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-96: MDSSAAPTNA...GNFLVMYVIV → MMRAKSISTKAGKPS

    Show »
    Length:319
    Mass (Da):36,516
    Checksum:i6373C1D800FF5E53
    GO
    Isoform 14 (identifier: P35372-14) [UniParc]FASTAAdd to Basket

    Also known as: Mu3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.
         389-400: LENLEAETAPLP → NYYIIHRCCCNTPLISQKPVLLWFCD

    Show »
    Length:314
    Mass (Da):36,240
    Checksum:i7346DB61E594896E
    GO
    Isoform 15 (identifier: P35372-15) [UniParc]FASTAAdd to Basket

    Also known as: MOR-1W

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.
         389-400: LENLEAETAPLP → VRSL

    Show »
    Length:292
    Mass (Da):33,570
    Checksum:i62A80E8005705E4C
    GO
    Isoform 16 (identifier: P35372-16) [UniParc]FASTAAdd to Basket

    Also known as: SV1

    The sequence of this isoform differs from the canonical sequence as follows:
         98-400: YTKMKTATNI...NLEAETAPLP → YSWFVIGGPEGRRKQRRLGEDKRARGCGEKG

    Show »
    Length:128
    Mass (Da):13,544
    Checksum:i1E780EE294726795
    GO
    Isoform 17 (identifier: P35372-17) [UniParc]FASTAAdd to Basket

    Also known as: SV2

    The sequence of this isoform differs from the canonical sequence as follows:
         97-400: RYTKMKTATN...NLEAETAPLP → SSSWF

    Show »
    Length:101
    Mass (Da):10,451
    Checksum:iE6590D98EDF64171
    GO
    Isoform 18 (identifier: P35372-18) [UniParc]FASTAAdd to Basket

    Also known as: hMOR-1Z

    The sequence of this isoform differs from the canonical sequence as follows:
         98-186: YTKMKTATNI...ALDFRTPRNA → FHRLYTNILS...LDSHSHLRHH
         187-400: Missing.

    Show »
    Length:186
    Mass (Da):20,188
    Checksum:i2A80DD5FADA6B83B
    GO

    Sequence cautioni

    Isoform 9 : The sequence AAQ77392.1 differs from that shown. Reason: a polymorphism leading to premature termination of translation (position: 411:Q->Stop)
    The sequence CAI20458.1 differs from that shown. Reason: Erroneous initiation.
    The sequence EAW47705.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261P → L in BAG36624. (PubMed:14702039)Curated
    Sequence conflicti51 – 511D → N in AAA20580. (PubMed:7905839)Curated
    Sequence conflicti109 – 1091I → V in AAQ77391. (PubMed:15893644)Curated
    Sequence conflicti207 – 2071M → I in AAB60354. (PubMed:7957926)Curated
    Sequence conflicti234 – 2341L → V in AAA20580. (PubMed:7905839)Curated
    Isoform 3 (identifier: P35372-3)
    Sequence conflicti402 – 4021Q → H in AAK74189. (PubMed:12589820)Curated

    Polymorphismi

    Variant Asp-40 does not show altered binding affinities for most opioid peptides and alkaloids tested, but it binds beta-endorphin, an endogenous opioid that activates the mu opioid receptor, approximately 3 times more tightly than the most common allelic form.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61A → V.4 Publications
    Corresponds to variant rs1799972 [ dbSNP | Ensembl ].
    VAR_009525
    Natural varianti40 – 401N → D in 10% of the population. 4 Publications
    Corresponds to variant rs1799971 [ dbSNP | Ensembl ].
    VAR_009524
    Natural varianti63 – 631G → V.
    Corresponds to variant rs9282817 [ dbSNP | Ensembl ].
    VAR_049426
    Natural varianti66 – 661S → F.
    Corresponds to variant rs9282819 [ dbSNP | Ensembl ].
    VAR_049427
    Natural varianti147 – 1471S → C Rare polymorphism. 2 Publications
    Corresponds to variant rs17174794 [ dbSNP | Ensembl ].
    VAR_009526
    Natural varianti152 – 1521N → D.1 Publication
    Corresponds to variant rs17174801 [ dbSNP | Ensembl ].
    VAR_019252
    Natural varianti260 – 2601R → H Rare polymorphism. 1 Publication
    Corresponds to variant rs1799974 [ dbSNP | Ensembl ].
    VAR_009527
    Natural varianti265 – 2651R → C.1 Publication
    Corresponds to variant rs17174822 [ dbSNP | Ensembl ].
    VAR_019253
    Natural varianti274 – 2741D → N.1 Publication
    Corresponds to variant rs17174829 [ dbSNP | Ensembl ].
    VAR_019254

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 100100Missing in isoform 12, isoform 14 and isoform 15. 4 PublicationsVSP_042327Add
    BLAST
    Alternative sequencei1 – 9696MDSSA…MYVIV → MMRAKSISTKAGKPS in isoform 13. 1 PublicationVSP_042328Add
    BLAST
    Alternative sequencei1 – 11M → MCLHRRVPSEETYSLDRFAQ NPPLFPPPSLPASESRMAHA PLLQRCGAARTGFCKKQQEL WQRRKEAAEALGTRKVSVLL ATSHSGARPAVSTM in isoform 10. 2 PublicationsVSP_037693
    Alternative sequencei97 – 400304RYTKM…TAPLP → SSSWF in isoform 17. CuratedVSP_042329Add
    BLAST
    Alternative sequencei98 – 400303YTKMK…TAPLP → YSWFVIGGPEGRRKQRRLGE DKRARGCGEKG in isoform 16. CuratedVSP_042330Add
    BLAST
    Alternative sequencei98 – 18689YTKMK…TPRNA → FHRLYTNILSSNLVLGKPAE DLCFHLRLHYASAHHYRVLW TDDLAPQECPHALWLQRKGQ ESSKDHQDGAGGGGCVHRLL DSHSHLRHH in isoform 18. 1 PublicationVSP_047577Add
    BLAST
    Alternative sequencei187 – 400214Missing in isoform 18. 1 PublicationVSP_047578Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → S in isoform 11. 1 PublicationVSP_037694Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → NYYIIHRCCCNTPLISQKPV LLWFCD in isoform 14. 1 PublicationVSP_042331Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → VRSL in isoform 2 and isoform 15. 3 PublicationsVSP_001896Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → CLPIPSLSCWALEQGCLVVY PGPLQGPLVRYDLPAILHSS CLRGNTAPSPSGGAFLLS in isoform 3. 1 PublicationVSP_037695Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → GPPAKFVADQLAGSS in isoform 4. 1 PublicationVSP_037696Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → PPLAVSMAQIFTRYPPPTHR EKTCNDYMKR in isoform 5. 1 PublicationVSP_037697Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → IRDPISNLPRVSVF in isoform 6. 3 PublicationsVSP_037698Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → KIDLFQKSSLLNCEHTKG in isoform 7. 1 PublicationVSP_037699Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → RERRQKSDW in isoform 8. 1 PublicationVSP_037700Add
    BLAST
    Alternative sequencei389 – 40012LENLE…TAPLP → VELNLDCHCENAKPWPLSYN AGQSPFPFPGRV in isoform 9. 1 PublicationVSP_037701Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25119 mRNA. Translation: AAA20580.1.
    U12569 mRNA. Translation: AAB60354.1.
    L29301 mRNA. Translation: AAA73958.1.
    AY036622 mRNA. Translation: AAK74189.1.
    AY036623 mRNA. Translation: AAK74190.1.
    AY195733 mRNA. Translation: AAO21305.1.
    AY225404 mRNA. Translation: AAP44727.1.
    AY309001 mRNA. Translation: AAQ77385.1.
    AY309005 mRNA. Translation: AAQ77389.1.
    AY309006 mRNA. Translation: AAQ77390.1.
    AY309007 mRNA. Translation: AAQ77391.1.
    AY309008 mRNA. Translation: AAQ77392.1.
    AY309009 mRNA. Translation: AAQ77393.1.
    EU340241 mRNA. Translation: ACA49726.1.
    EU340242 mRNA. Translation: ACA49727.1.
    EU340243 mRNA. Translation: ACA49728.1.
    AY364230 mRNA. Translation: AAR12887.1.
    AY364890 mRNA. Translation: AAR11568.1.
    HQ699462 mRNA. Translation: AET97615.1.
    EU360599 mRNA. Translation: ABY61366.1.
    EU362990 mRNA. Translation: ABY66530.1.
    AK313901 mRNA. Translation: BAG36624.1.
    AY521028 mRNA. Translation: AAS00462.1.
    AY587764 Genomic DNA. Translation: AAS83107.1.
    FJ041292 mRNA. Translation: ACM90350.1.
    FJ041293 mRNA. Translation: ACM90351.1.
    FJ041294 mRNA. Translation: ACM90352.1.
    AL132774, AL136444 Genomic DNA. Translation: CAI20458.1. Different initiation.
    AL445220 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW47705.1. Different initiation.
    BC074927 mRNA. Translation: AAH74927.1.
    AY292290 Genomic DNA. Translation: AAP44409.1.
    AY292291 Genomic DNA. Translation: AAP44410.1.
    AF153500 Genomic DNA. Translation: AAD44318.1.
    CCDSiCCDS43517.1. [P35372-5]
    CCDS43518.1. [P35372-3]
    CCDS47503.1. [P35372-10]
    CCDS47504.1. [P35372-7]
    CCDS47505.1. [P35372-8]
    CCDS47506.1. [P35372-4]
    CCDS47507.1. [P35372-9]
    CCDS47508.1. [P35372-2]
    CCDS55068.1. [P35372-13]
    CCDS55069.1. [P35372-11]
    CCDS55070.1. [P35372-1]
    CCDS55071.1. [P35372-12]
    PIRiI56553.
    S65693.
    RefSeqiNP_000905.3. NM_000914.4. [P35372-1]
    NP_001008503.2. NM_001008503.2. [P35372-5]
    NP_001008504.2. NM_001008504.3. [P35372-2]
    NP_001008505.2. NM_001008505.2. [P35372-3]
    NP_001138751.1. NM_001145279.3. [P35372-10]
    NP_001138752.1. NM_001145280.3. [P35372-12]
    NP_001138753.1. NM_001145281.2. [P35372-13]
    NP_001138754.1. NM_001145282.2. [P35372-7]
    NP_001138755.1. NM_001145283.2. [P35372-8]
    NP_001138756.1. NM_001145284.3. [P35372-4]
    NP_001138757.1. NM_001145285.2. [P35372-11]
    NP_001138758.1. NM_001145286.2. [P35372-9]
    NP_001138759.1. NM_001145287.2. [P35372-12]
    NP_001272452.1. NM_001285523.1.
    NP_001272453.1. NM_001285524.1. [P35372-10]
    NP_001272455.1. NM_001285526.1. [P35372-12]
    NP_001272456.1. NM_001285527.1. [P35372-15]
    NP_001272457.1. NM_001285528.1. [P35372-14]
    XP_006715559.1. XM_006715496.1. [P35372-10]
    UniGeneiHs.2353.

    Genome annotation databases

    EnsembliENST00000229768; ENSP00000229768; ENSG00000112038. [P35372-3]
    ENST00000330432; ENSP00000328264; ENSG00000112038. [P35372-1]
    ENST00000337049; ENSP00000338381; ENSG00000112038. [P35372-5]
    ENST00000360422; ENSP00000353598; ENSG00000112038. [P35372-6]
    ENST00000414028; ENSP00000399359; ENSG00000112038. [P35372-4]
    ENST00000419506; ENSP00000403549; ENSG00000112038. [P35372-9]
    ENST00000428397; ENSP00000411903; ENSG00000112038. [P35372-2]
    ENST00000434900; ENSP00000394624; ENSG00000112038. [P35372-10]
    ENST00000435918; ENSP00000413752; ENSG00000112038. [P35372-8]
    ENST00000452687; ENSP00000410497; ENSG00000112038. [P35372-7]
    ENST00000518759; ENSP00000430260; ENSG00000112038. [P35372-13]
    ENST00000519083; ENSP00000431048; ENSG00000112038. [P35372-6]
    ENST00000520708; ENSP00000430876; ENSG00000112038. [P35372-12]
    ENST00000522236; ENSP00000429373; ENSG00000112038. [P35372-12]
    ENST00000522555; ENSP00000429719; ENSG00000112038. [P35372-12]
    ENST00000522739; ENSP00000428018; ENSG00000112038. [P35372-6]
    ENST00000524150; ENSP00000430575; ENSG00000112038. [P35372-18]
    ENST00000524163; ENSP00000430097; ENSG00000112038. [P35372-11]
    GeneIDi4988.
    KEGGihsa:4988.
    UCSCiuc003qpn.2. human. [P35372-2]
    uc003qpo.1. human. [P35372-3]
    uc003qpq.1. human. [P35372-7]
    uc003qpr.2. human. [P35372-1]
    uc003qpt.1. human. [P35372-5]
    uc003qpu.2. human. [P35372-15]
    uc011efb.2. human. [P35372-10]
    uc011efc.1. human. [P35372-13]
    uc011eff.1. human. [P35372-9]
    uc011efg.1. human. [P35372-11]
    uc011efh.1. human. [P35372-8]
    uc011efi.2. human. [P35372-4]

    Polymorphism databases

    DMDMi2851402.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Mu opioid receptor entry

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25119 mRNA. Translation: AAA20580.1 .
    U12569 mRNA. Translation: AAB60354.1 .
    L29301 mRNA. Translation: AAA73958.1 .
    AY036622 mRNA. Translation: AAK74189.1 .
    AY036623 mRNA. Translation: AAK74190.1 .
    AY195733 mRNA. Translation: AAO21305.1 .
    AY225404 mRNA. Translation: AAP44727.1 .
    AY309001 mRNA. Translation: AAQ77385.1 .
    AY309005 mRNA. Translation: AAQ77389.1 .
    AY309006 mRNA. Translation: AAQ77390.1 .
    AY309007 mRNA. Translation: AAQ77391.1 .
    AY309008 mRNA. Translation: AAQ77392.1 .
    AY309009 mRNA. Translation: AAQ77393.1 .
    EU340241 mRNA. Translation: ACA49726.1 .
    EU340242 mRNA. Translation: ACA49727.1 .
    EU340243 mRNA. Translation: ACA49728.1 .
    AY364230 mRNA. Translation: AAR12887.1 .
    AY364890 mRNA. Translation: AAR11568.1 .
    HQ699462 mRNA. Translation: AET97615.1 .
    EU360599 mRNA. Translation: ABY61366.1 .
    EU362990 mRNA. Translation: ABY66530.1 .
    AK313901 mRNA. Translation: BAG36624.1 .
    AY521028 mRNA. Translation: AAS00462.1 .
    AY587764 Genomic DNA. Translation: AAS83107.1 .
    FJ041292 mRNA. Translation: ACM90350.1 .
    FJ041293 mRNA. Translation: ACM90351.1 .
    FJ041294 mRNA. Translation: ACM90352.1 .
    AL132774 , AL136444 Genomic DNA. Translation: CAI20458.1 . Different initiation.
    AL445220 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW47705.1 . Different initiation.
    BC074927 mRNA. Translation: AAH74927.1 .
    AY292290 Genomic DNA. Translation: AAP44409.1 .
    AY292291 Genomic DNA. Translation: AAP44410.1 .
    AF153500 Genomic DNA. Translation: AAD44318.1 .
    CCDSi CCDS43517.1. [P35372-5 ]
    CCDS43518.1. [P35372-3 ]
    CCDS47503.1. [P35372-10 ]
    CCDS47504.1. [P35372-7 ]
    CCDS47505.1. [P35372-8 ]
    CCDS47506.1. [P35372-4 ]
    CCDS47507.1. [P35372-9 ]
    CCDS47508.1. [P35372-2 ]
    CCDS55068.1. [P35372-13 ]
    CCDS55069.1. [P35372-11 ]
    CCDS55070.1. [P35372-1 ]
    CCDS55071.1. [P35372-12 ]
    PIRi I56553.
    S65693.
    RefSeqi NP_000905.3. NM_000914.4. [P35372-1 ]
    NP_001008503.2. NM_001008503.2. [P35372-5 ]
    NP_001008504.2. NM_001008504.3. [P35372-2 ]
    NP_001008505.2. NM_001008505.2. [P35372-3 ]
    NP_001138751.1. NM_001145279.3. [P35372-10 ]
    NP_001138752.1. NM_001145280.3. [P35372-12 ]
    NP_001138753.1. NM_001145281.2. [P35372-13 ]
    NP_001138754.1. NM_001145282.2. [P35372-7 ]
    NP_001138755.1. NM_001145283.2. [P35372-8 ]
    NP_001138756.1. NM_001145284.3. [P35372-4 ]
    NP_001138757.1. NM_001145285.2. [P35372-11 ]
    NP_001138758.1. NM_001145286.2. [P35372-9 ]
    NP_001138759.1. NM_001145287.2. [P35372-12 ]
    NP_001272452.1. NM_001285523.1.
    NP_001272453.1. NM_001285524.1. [P35372-10 ]
    NP_001272455.1. NM_001285526.1. [P35372-12 ]
    NP_001272456.1. NM_001285527.1. [P35372-15 ]
    NP_001272457.1. NM_001285528.1. [P35372-14 ]
    XP_006715559.1. XM_006715496.1. [P35372-10 ]
    UniGenei Hs.2353.

    3D structure databases

    DisProti DP00272.
    ProteinModelPortali P35372.
    SMRi P35372. Positions 63-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111033. 7 interactions.
    IntActi P35372. 15 interactions.
    MINTi MINT-100121.

    Chemistry

    BindingDBi P35372.
    ChEMBLi CHEMBL233.
    DrugBanki DB00802. Alfentanil.
    DB00913. Anileridine.
    DB00921. Buprenorphine.
    DB00611. Butorphanol.
    DB00318. Codeine.
    DB01209. Dezocine.
    DB01081. Diphenoxylate.
    DB00813. Fentanyl.
    DB00956. Hydrocodone.
    DB00327. Hydromorphone.
    DB00504. Levallorphan.
    DB01227. Levomethadyl Acetate.
    DB00854. Levorphanol.
    DB00836. Loperamide.
    DB00333. Methadone.
    DB01433. Methadyl Acetate.
    DB00295. Morphine.
    DB00844. Nalbuphine.
    DB01183. Naloxone.
    DB00704. Naltrexone.
    DB00497. Oxycodone.
    DB01192. Oxymorphone.
    DB00652. Pentazocine.
    DB00647. Propoxyphene.
    DB00899. Remifentanil.
    DB00708. Sufentanil.
    DB00193. Tramadol.
    GuidetoPHARMACOLOGYi 319.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P35372.

    Polymorphism databases

    DMDMi 2851402.

    Proteomic databases

    PaxDbi P35372.
    PRIDEi P35372.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229768 ; ENSP00000229768 ; ENSG00000112038 . [P35372-3 ]
    ENST00000330432 ; ENSP00000328264 ; ENSG00000112038 . [P35372-1 ]
    ENST00000337049 ; ENSP00000338381 ; ENSG00000112038 . [P35372-5 ]
    ENST00000360422 ; ENSP00000353598 ; ENSG00000112038 . [P35372-6 ]
    ENST00000414028 ; ENSP00000399359 ; ENSG00000112038 . [P35372-4 ]
    ENST00000419506 ; ENSP00000403549 ; ENSG00000112038 . [P35372-9 ]
    ENST00000428397 ; ENSP00000411903 ; ENSG00000112038 . [P35372-2 ]
    ENST00000434900 ; ENSP00000394624 ; ENSG00000112038 . [P35372-10 ]
    ENST00000435918 ; ENSP00000413752 ; ENSG00000112038 . [P35372-8 ]
    ENST00000452687 ; ENSP00000410497 ; ENSG00000112038 . [P35372-7 ]
    ENST00000518759 ; ENSP00000430260 ; ENSG00000112038 . [P35372-13 ]
    ENST00000519083 ; ENSP00000431048 ; ENSG00000112038 . [P35372-6 ]
    ENST00000520708 ; ENSP00000430876 ; ENSG00000112038 . [P35372-12 ]
    ENST00000522236 ; ENSP00000429373 ; ENSG00000112038 . [P35372-12 ]
    ENST00000522555 ; ENSP00000429719 ; ENSG00000112038 . [P35372-12 ]
    ENST00000522739 ; ENSP00000428018 ; ENSG00000112038 . [P35372-6 ]
    ENST00000524150 ; ENSP00000430575 ; ENSG00000112038 . [P35372-18 ]
    ENST00000524163 ; ENSP00000430097 ; ENSG00000112038 . [P35372-11 ]
    GeneIDi 4988.
    KEGGi hsa:4988.
    UCSCi uc003qpn.2. human. [P35372-2 ]
    uc003qpo.1. human. [P35372-3 ]
    uc003qpq.1. human. [P35372-7 ]
    uc003qpr.2. human. [P35372-1 ]
    uc003qpt.1. human. [P35372-5 ]
    uc003qpu.2. human. [P35372-15 ]
    uc011efb.2. human. [P35372-10 ]
    uc011efc.1. human. [P35372-13 ]
    uc011eff.1. human. [P35372-9 ]
    uc011efg.1. human. [P35372-11 ]
    uc011efh.1. human. [P35372-8 ]
    uc011efi.2. human. [P35372-4 ]

    Organism-specific databases

    CTDi 4988.
    GeneCardsi GC06P154391.
    HGNCi HGNC:8156. OPRM1.
    HPAi HPA014509.
    MIMi 600018. gene.
    neXtProti NX_P35372.
    PharmGKBi PA31945.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279457.
    HOGENOMi HOG000230486.
    HOVERGENi HBG106919.
    InParanoidi P35372.
    KOi K04215.
    OMAi NSTRVRQ.
    PhylomeDBi P35372.
    TreeFami TF315737.

    Enzyme and pathway databases

    Reactomei REACT_14819. Peptide ligand-binding receptors.
    REACT_15295. Opioid Signalling.
    REACT_15457. G-protein activation.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    GeneWikii %CE%9C-opioid_receptor.
    GenomeRNAii 4988.
    NextBioi 19206.
    PROi P35372.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35372.
    Bgeei P35372.
    CleanExi HS_OPRM1.
    Genevestigatori P35372.

    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. "Human mu opiate receptor. cDNA and genomic clones, pharmacologic characterization and chromosomal assignment."
      Wang J.-B., Johnson P.S., Persico A.M., Hawkins A.L., Griffin C.A., Uhl G.R.
      FEBS Lett. 338:217-222(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Expression of two variants of the human mu opioid receptor mRNA in SK-N-SH cells and human brain."
      Bare L.A., Mansson E., Yang D.
      FEBS Lett. 354:213-216(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ASP-40.
      Tissue: Brain.
    3. "The human mu opioid receptor: modulation of functional desensitization by calcium/calmodulin-dependent protein kinase and protein kinase C."
      Mestek A. Jr., Hurley J.H., Bye L.S., Campbell A.D., Chen Y., Tian M., Liu J., Schulman H., Yu L.
      J. Neurosci. 15:2396-2406(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Identification and characterization of two new human mu opioid receptor splice variants, hMOR-1O and hMOR-1X."
      Pan Y.X., Xu J., Mahurter L., Xu M., Gilbert A.K., Pasternak G.W.
      Biochem. Biophys. Res. Commun. 301:1057-1061(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5).
    5. "Molecular identification and functional expression of mu 3, a novel alternatively spliced variant of the human mu opiate receptor gene."
      Cadet P., Mantione K.J., Stefano G.B.
      J. Immunol. 170:5118-5123(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14).
    6. "Identification and characterization of six new alternatively spliced variants of the human mu opioid receptor gene, Oprm."
      Pan L., Xu J., Yu R., Xu M.-M., Pan Y.-X., Pasternak G.W.
      Neuroscience 133:209-220(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 6; 7; 8; 9 AND 11).
    7. "Isolation and characterization of new exon 11-associated N-terminal splice variants of the human mu opioid receptor gene."
      Xu J., Xu M., Hurd Y.L., Pasternak G.W., Pan Y.X.
      J. Neurochem. 108:962-972(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10; 12 AND 13).
    8. "Novel variants of the human mu opioid receptor are generated by alternative splicing and transcription from different positions in the OPRM1 gene."
      Baar C., Kvam T.-M., Rakvag T.T., Kaasa S., Skorpen F.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 15).
      Tissue: Brain.
    9. "Isolation and expression of alternatively spliced variants encoding proteins with single transmembrane domain in mu opioid receptor genes."
      Xu J., Pasternak G.W., Pan Y.
      Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 18).
    10. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
      Tissue: Brain.
    11. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    12. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Kopatz S.A., Aronstam R.S., Sharma S.V.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    13. NIEHS SNPs program
      Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-6; ASP-40; CYS-147; ASP-152; CYS-265 AND ASN-274.
    14. "Isolation and characterization of two alternatively spliced variants from the human mu opioid receptor, OPRM1, gene."
      Xu J., Xu M., Pasternak G.W., Pan Y.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 10).
    15. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    16. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    17. "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 1).
    18. "An homozygous Ala 6 Val (GCC->GTC) mutation was detected on human mu opioid receptor gene of an African American individual with sickle cell anemia."
      Metha S., Glendenning M., Kutlar A., Kutlar F.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20, VARIANT VAL-6.
      Tissue: Blood.
    19. "The mu opiate receptor as a candidate gene for pain: polymorphisms, variations in expression, nociception, and opiate responses."
      Uhl G.R., Sora I., Wang Z.
      Proc. Natl. Acad. Sci. U.S.A. 96:7752-7755(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
    20. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 229-374.
    21. "ADP-ribosylation factor-dependent phospholipase D2 activation is required for agonist-induced mu-opioid receptor endocytosis."
      Koch T., Brandenburg L.O., Schulz S., Liang Y., Klein J., Hollt V.
      J. Biol. Chem. 278:9979-9985(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLD2.
    22. "Mutation of human mu opioid receptor extracellular 'disulfide cysteine' residues alters ligand binding but does not prevent receptor targeting to the cell plasma membrane."
      Zhang P., Johnson P.S., Zollner C., Wang W., Wang Z., Montes A.E., Seidleck B.K., Blaschak C.J., Surratt C.K.
      Brain Res. Mol. Brain Res. 72:195-204(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-142 AND CYS-219.
    23. "Calmodulin binding to G protein-coupling domain of opioid receptors."
      Wang D., Sadee W., Quillan J.M.
      J. Biol. Chem. 274:22081-22088(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF LYS-273.
    24. "Molecular mechanisms and regulation of opioid receptor signaling."
      Law P.Y., Wong Y.H., Loh H.H.
      Annu. Rev. Pharmacol. Toxicol. 40:389-430(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    25. "Calmodulin regulation of basal and agonist-stimulated G protein coupling by the mu-opioid receptor (OP(3)) in morphine-pretreated cell."
      Wang D., Surratt C.K., Sadee W.
      J. Neurochem. 75:763-771(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CALMODULIN, MUTAGENESIS OF LYS-273 AND ARG-275.
    26. "Interactions of opioid and chemokine receptors: oligomerization of mu, kappa, and delta with CCR5 on immune cells."
      Suzuki S., Chuang L.F., Yau P., Doi R.H., Chuang R.Y.
      Exp. Cell Res. 280:192-200(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH CCR5.
    27. "Agonists activate Gi1 alpha or Gi2 alpha fused to the human mu opioid receptor differently."
      Massotte D., Brillet K., Kieffer B., Milligan G.
      J. Neurochem. 81:1372-1382(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COUPLING TO GNAI1 AND GNAI2.
    28. "Selective interactions between helix VIII of the human mu-opioid receptors and the C terminus of periplakin disrupt G protein activation."
      Feng G.J., Kellett E., Scorer C.A., Wilde J., White J.H., Milligan G.
      J. Biol. Chem. 278:33400-33407(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPL.
    29. "Interaction between the mu opioid receptor and filamin A is involved in receptor regulation and trafficking."
      Onoprishvili I., Andria M.L., Kramer H.K., Ancevska-Taneva N., Hiller J.M., Simon E.J.
      Mol. Pharmacol. 64:1092-1100(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLNA.
    30. "Opioid receptor homo- and heterodimerization in living cells by quantitative bioluminescence resonance energy transfer."
      Wang D., Sun X., Bohn L.M., Sadee W.
      Mol. Pharmacol. 67:2173-2184(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMOOLIGOMERIZATION, RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH OPRD1 AND OPRK1.
    31. "Functional complementation and the analysis of opioid receptor homodimerization."
      Pascal G., Milligan G.
      Mol. Pharmacol. 68:905-915(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMOOLIGOMERIZATION.
    32. "The opioid ligand binding of human mu-opioid receptor is modulated by novel splice variants of the receptor."
      Choi H.S., Kim C.S., Hwang C.K., Song K.Y., Wang W., Qiu Y., Law P.Y., Wei L.N., Loh H.H.
      Biochem. Biophys. Res. Commun. 343:1132-1140(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 16 AND 17), FUNCTION (ISOFORMS 16 AND 17), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT.
    33. "A member of the heat shock protein 40 family, hlj1, binds to the carboxyl tail of the human mu opioid receptor."
      Ancevska-Taneva N., Onoprishvili I., Andria M.L., Hiller J.M., Simon E.J.
      Brain Res. 1081:28-33(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJB4.
    34. "Physical association between neuropeptide FF and micro-opioid receptors as a possible molecular basis for anti-opioid activity."
      Roumy M., Lorenzo C., Mazeres S., Bouchet S., Zajac J.M., Mollereau C.
      J. Biol. Chem. 282:8332-8342(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECEPTOR HETEROOLIGOMERIZATION, INTERACTION WITH NPFFR2.
    35. "Membrane functional organisation and dynamic of mu-opioid receptors."
      Lopez A., Salome L.
      Cell. Mol. Life Sci. 66:2093-2108(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    36. "Regulation of mu opioid receptor internalization by the scaffold protein RanBPM."
      Talbot J.N., Skifter D.A., Bianchi E., Monaghan D.T., Toews M.L., Murrin L.C.
      Neurosci. Lett. 466:154-158(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP9.
    37. "Interaction of the mu-opioid receptor with GPR177 (Wntless) inhibits Wnt secretion: potential implications for opioid dependence."
      Jin J., Kittanakom S., Wong V., Reyes B.A., Van Bockstaele E.J., Stagljar I., Berrettini W., Levenson R.
      BMC Neurosci. 11:33-33(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WLS.
    38. "A novel alternatively spliced isoform of the mu-opioid receptor: functional antagonism."
      Gris P., Gauthier J., Cheng P., Gibson D.G., Gris D., Laur O., Pierson J., Wentworth S., Nackley A.G., Maixner W., Diatchenko L.
      Mol. Pain 6:33-33(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 12), SUBCELLULAR LOCATION (ISOFORM 12).
    39. "Mu opioid receptor gene variants: lack of association with alcohol dependence."
      Bergen A.W., Kokoszka J., Peterson R., Long J.C., Virkkunen M., Linnoila M., Goldman D.
      Mol. Psychiatry 2:490-494(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-6; ASP-40 AND CYS-147.
    40. "Single-nucleotide polymorphism in the human mu opioid receptor gene alters beta-endorphin binding and activity: possible implications for opiate addiction."
      Bond C., LaForge K.S., Tian M., Melia D., Zhang S., Borg L., Gong J., Schluger J., Strong J.A., Leal S.M., Tischfield J.A., Kreek M.J., Yu L.
      Proc. Natl. Acad. Sci. U.S.A. 95:9608-9613(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-6; ASP-40 AND HIS-260.

    Entry informationi

    Entry nameiOPRM_HUMAN
    AccessioniPrimary (citable) accession number: P35372
    Secondary accession number(s): B0FXJ1
    , B2R9S7, B8Q1L7, B8Q1L8, B8Q1L9, E7EWZ3, G8XRH6, G8XRH8, Q12930, Q4VWM1, Q4VWM2, Q4VWM3, Q4VWM4, Q4VWM6, Q4VWX6, Q5TDA1, Q6UPP1, Q6UQ80, Q7Z2D8, Q86V80, Q8IWW3, Q8IWW4, Q9UCZ4, Q9UN57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    OPRM1 is the main physiological target for most clinically important opioid analgesics. OPRM1-mediated inhibition of voltage-gated calcium channels on central presynaptic terminals of primary afferent nociceptors is thought to be one of the primary mechanisms mediating analgesia at the spinal level. Opioid-induced hyperalgesic responses are observed following both acute and chronic dosing associated with cellular excitation.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3