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P35372

- OPRM_HUMAN

UniProt

P35372 - OPRM_HUMAN

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Protein
Mu-type opioid receptor
Gene
OPRM1, MOR1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

GO - Molecular functioni

  1. G-protein alpha-subunit binding Source: UniProtKB
  2. G-protein coupled receptor activity Source: UniProtKB
  3. beta-endorphin 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. G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: ProtInc
  2. adenylate cyclase-activating dopamine receptor signaling pathway Source: Ensembl
  3. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: Ensembl
  4. behavioral response to ethanol Source: UniProtKB
  5. calcium ion transmembrane transport Source: GOC
  6. cellular response to stress Source: UniProtKB
  7. locomotory behavior Source: Ensembl
  8. negative regulation of Wnt protein secretion Source: UniProtKB
  9. negative regulation of adenylate cyclase activity Source: UniProtKB
  10. negative regulation of cAMP-mediated signaling Source: UniProtKB
  11. negative regulation of cell proliferation Source: ProtInc
  12. negative regulation of cytosolic calcium ion concentration Source: UniProtKB
  13. negative regulation of nitric oxide biosynthetic process Source: UniProtKB
  14. neuropeptide signaling pathway Source: GOC
  15. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  16. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  17. positive regulation of cAMP-mediated signaling Source: UniProtKB
  18. positive regulation of cytosolic calcium ion concentration 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
Complete GO annotation...

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; Multi-pass membrane protein 2 Publications
Isoform 12 : Cytoplasm 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6868Extracellular By similarity
Add
BLAST
Transmembranei69 – 9325Helical; Name=1; By similarity
Add
BLAST
Topological domaini94 – 10613Cytoplasmic By similarity
Add
BLAST
Transmembranei107 – 13125Helical; Name=2; By similarity
Add
BLAST
Topological domaini132 – 14211Extracellular By similarity
Add
BLAST
Transmembranei143 – 16523Helical; Name=3; By similarity
Add
BLAST
Topological domaini166 – 18520Cytoplasmic By similarity
Add
BLAST
Transmembranei186 – 20722Helical; Name=4; By similarity
Add
BLAST
Topological domaini208 – 23023Extracellular By similarity
Add
BLAST
Transmembranei231 – 25525Helical; Name=5; By similarity
Add
BLAST
Topological domaini256 – 28328Cytoplasmic By similarity
Add
BLAST
Transmembranei284 – 30724Helical; Name=6; By similarity
Add
BLAST
Topological domaini308 – 3147Extracellular By similarity
Transmembranei315 – 33824Helical; Name=7; By similarity
Add
BLAST
Topological domaini339 – 40062Cytoplasmic By similarity
Add
BLAST

GO - Cellular componenti

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

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 receptor
PRO_0000069972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi9 – 91N-linked (GlcNAc...) Reviewed prediction
Glycosylationi12 – 121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi33 – 331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi40 – 401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi48 – 481N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi142 ↔ 219 By similarity
Modified residuei168 – 1681Phosphotyrosine By similarity
Lipidationi353 – 3531S-palmitoyl cysteine Reviewed prediction
Modified residuei365 – 3651Phosphoserine By similarity
Modified residuei372 – 3721Phosphothreonine By similarity
Modified residuei377 – 3771Phosphoserine By 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.
Ubiquitinated. A basal ubiquitination seems not to be related to degradation. Ubiquitination is increased upon formation of OPRM1:OPRD1 oligomers leading to proteasomal degradation; the ubiquitination is diminished by RTP4 By similarity.

Keywords - PTMi

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

Proteomic databases

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.13 Publications

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.

Family & Domainsi

Sequence similaritiesi

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.

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.
VSP_042327Add
BLAST
Alternative sequencei1 – 9696MDSSA…MYVIV → MMRAKSISTKAGKPS in isoform 13.
VSP_042328Add
BLAST
Alternative sequencei1 – 11M → MCLHRRVPSEETYSLDRFAQ NPPLFPPPSLPASESRMAHA PLLQRCGAARTGFCKKQQEL WQRRKEAAEALGTRKVSVLL ATSHSGARPAVSTM in isoform 10.
VSP_037693
Alternative sequencei97 – 400304RYTKM…TAPLP → SSSWF in isoform 17.
VSP_042329Add
BLAST
Alternative sequencei98 – 400303YTKMK…TAPLP → YSWFVIGGPEGRRKQRRLGE DKRARGCGEKG in isoform 16.
VSP_042330Add
BLAST
Alternative sequencei98 – 18689YTKMK…TPRNA → FHRLYTNILSSNLVLGKPAE DLCFHLRLHYASAHHYRVLW TDDLAPQECPHALWLQRKGQ ESSKDHQDGAGGGGCVHRLL DSHSHLRHH in isoform 18.
VSP_047577Add
BLAST
Alternative sequencei187 – 400214Missing in isoform 18.
VSP_047578Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → S in isoform 11.
VSP_037694Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → NYYIIHRCCCNTPLISQKPV LLWFCD in isoform 14.
VSP_042331Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → VRSL in isoform 2 and isoform 15.
VSP_001896Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → CLPIPSLSCWALEQGCLVVY PGPLQGPLVRYDLPAILHSS CLRGNTAPSPSGGAFLLS in isoform 3.
VSP_037695Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → GPPAKFVADQLAGSS in isoform 4.
VSP_037696Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → PPLAVSMAQIFTRYPPPTHR EKTCNDYMKR in isoform 5.
VSP_037697Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → IRDPISNLPRVSVF in isoform 6.
VSP_037698Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → KIDLFQKSSLLNCEHTKG in isoform 7.
VSP_037699Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → RERRQKSDW in isoform 8.
VSP_037700Add
BLAST
Alternative sequencei389 – 40012LENLE…TAPLP → VELNLDCHCENAKPWPLSYN AGQSPFPFPGRV in isoform 9.
VSP_037701Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261P → L in BAG36624. 1 Publication
Sequence conflicti51 – 511D → N in AAA20580. 1 Publication
Sequence conflicti109 – 1091I → V in AAQ77391. 1 Publication
Sequence conflicti207 – 2071M → I in AAB60354. 1 Publication
Sequence conflicti234 – 2341L → V in AAA20580. 1 Publication
Isoform 3 (identifier: P35372-3)
Sequence conflicti402 – 4021Q → H in AAK74189. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 147 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

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