Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mu-type opioid receptor

Gene

Oprm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for endogenous opioids such as beta-endorphin and endomorphin. Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors. The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extend to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15. They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B. Also couples to adenylate cyclase stimulatory G alpha proteins. The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4. Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization. Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction. The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins. The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation. Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling. Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling. Endogenous ligands induce rapid desensitization, endocytosis and recycling. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties. Involved in neurogenesis.9 Publications

GO - Molecular functioni

  • beta-endorphin receptor activity Source: GO_Central
  • filamin binding Source: RGD
  • G-protein alpha-subunit binding Source: UniProtKB
  • G-protein beta-subunit binding Source: RGD
  • G-protein coupled receptor activity Source: UniProtKB
  • morphine receptor activity Source: UniProtKB
  • neuropeptide binding Source: GO_Central
  • protein C-terminus binding Source: RGD
  • protein domain specific binding Source: RGD
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  • acute inflammatory response to antigenic stimulus Source: RGD
  • adenylate cyclase-activating dopamine receptor signaling pathway Source: Ensembl
  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: RGD
  • adenylate cyclase-inhibiting opioid receptor signaling pathway Source: RGD
  • behavioral response to ethanol Source: Ensembl
  • cellular response to stress Source: Ensembl
  • eating behavior Source: RGD
  • estrous cycle Source: RGD
  • excitatory postsynaptic potential Source: RGD
  • G-protein coupled receptor signaling pathway Source: RGD
  • immune response Source: RGD
  • locomotory behavior Source: Ensembl
  • negative regulation of adenylate cyclase activity Source: UniProtKB
  • negative regulation of cAMP biosynthetic process Source: RGD
  • negative regulation of cAMP-mediated signaling Source: UniProtKB
  • negative regulation of cytosolic calcium ion concentration Source: UniProtKB
  • negative regulation of nitric oxide biosynthetic process Source: UniProtKB
  • negative regulation of Wnt protein secretion Source: UniProtKB
  • opioid receptor signaling pathway Source: RGD
  • phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • positive regulation of appetite Source: RGD
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of neurogenesis Source: UniProtKB
  • regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: UniProtKB
  • regulation of sensory perception of pain Source: RGD
  • response to cocaine Source: RGD
  • response to ethanol Source: RGD
  • response to food Source: RGD
  • response to growth factor Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to morphine Source: RGD
  • response to radiation Source: RGD
  • sensory perception of pain Source: UniProtKB
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-RNO-111885. Opioid Signalling.
R-RNO-202040. G-protein activation.
R-RNO-375276. Peptide ligand-binding receptors.
R-RNO-418594. 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):
Opioid receptor B
Gene namesi
Name:Oprm1
Synonyms:Ror-b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3234. Oprm1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 66ExtracellularBy similarityAdd BLAST66
Transmembranei67 – 91Helical; Name=1By similarityAdd BLAST25
Topological domaini92 – 104CytoplasmicBy similarityAdd BLAST13
Transmembranei105 – 129Helical; Name=2By similarityAdd BLAST25
Topological domaini130 – 140ExtracellularBy similarityAdd BLAST11
Transmembranei141 – 163Helical; Name=3By similarityAdd BLAST23
Topological domaini164 – 183CytoplasmicBy similarityAdd BLAST20
Transmembranei184 – 205Helical; Name=4By similarityAdd BLAST22
Topological domaini206 – 228ExtracellularBy similarityAdd BLAST23
Transmembranei229 – 253Helical; Name=5By similarityAdd BLAST25
Topological domaini254 – 281CytoplasmicBy similarityAdd BLAST28
Transmembranei282 – 305Helical; Name=6By similarityAdd BLAST24
Topological domaini306 – 312ExtracellularBy similarity7
Transmembranei313 – 336Helical; Name=7By similarityAdd BLAST24
Topological domaini337 – 398CytoplasmicBy similarityAdd BLAST62

GO - Cellular componenti

  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • dendrite cytoplasm Source: RGD
  • dendrite membrane Source: RGD
  • focal adhesion Source: RGD
  • integral component of plasma membrane Source: RGD
  • membrane Source: RGD
  • membrane raft Source: RGD
  • perikaryon Source: RGD
  • postsynapse Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi91Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-96, A-166 and A-336. 1 Publication1
Mutagenesisi96Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-166 and A-336. 1 Publication1
Mutagenesisi114D → A or N: Impairs agonist affinity, agonist-induced inhibition of adenylate cyclase and coupling to G-proteins. 2 Publications1
Mutagenesisi114D → E: No effect on inhibition of adenylate cyclase. 2 Publications1
Mutagenesisi147D → A: No effect on constitutive activation. Impairs agonist affinity and agonist-induced inhibition of adenylate cyclase. 2 Publications1
Mutagenesisi147D → E: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase. 2 Publications1
Mutagenesisi147D → N: No effect on constitutive activation. 2 Publications1
Mutagenesisi164D → E: Reduces basal activity. 1 Publication1
Mutagenesisi164D → H, M, Q or Y: Constitutive active. 1 Publication1
Mutagenesisi166Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-96 and A-336. 2 Publications1
Mutagenesisi166Y → F: Decrease in phosphorylation, no decrease in G-protein binding. 2 Publications1
Mutagenesisi180T → A: Impairs ARRB2- and GRK3-mediated receptor desensitization. 1 Publication1
Mutagenesisi275L → E: No effect on constitutive activation. Some constitutive activity; when associated with K-279. 1 Publication1
Mutagenesisi279T → D: Receptor inactivation. 2 Publications1
Mutagenesisi279T → K: Constitutive active. Some constitutive activity; when associated with E-275. 2 Publications1
Mutagenesisi297H → A: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase. 1 Publication1
Mutagenesisi336Y → A: Abolishes agonist-induced G-protein-independent receptor internalization; when associated with A-91, A-96 and A-166. 1 Publication1
Mutagenesisi346C → A: No change in palmitoylation. No change in palmitoylation; when associated with A-351. 1 Publication1
Mutagenesisi351C → A: No change in palmitoylation; when associated with A-346. 1 Publication1
Mutagenesisi363S → A: Abolishes basal phosphorylation; when associated with A-370. Abolishes basal and agonist-induced phosphorylation; when associated with A-370 and A-375. Accelerates agonist-induced receptor internalization. 2 Publications1
Mutagenesisi370T → A: Abolishes basal phosphorylation; when associated with A-363. Abolishes basal and agonist-induced phosphorylation; when associated with A-363 and A-375. Accelerates agonist-induced receptor internalization. 2 Publications1
Mutagenesisi375S → A: Reduces agonist-induced receptor internalization. Abolishes morphine-induced phosphorylation. Restores agonist-specific PRKCE activity. Abolishes basal and agonist-induced phosphorylation; when associated with A-363 and A-370. 3 Publications1
Mutagenesisi394T → A: Impairs phosphorylation and abolishes agonist-mediated acute receptor desensitization. 2 Publications1

Chemistry databases

ChEMBLiCHEMBL270.
GuidetoPHARMACOLOGYi319.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000699781 – 398Mu-type opioid receptorAdd BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi9N-linked (GlcNAc...)Sequence analysis1
Glycosylationi31N-linked (GlcNAc...)Sequence analysis1
Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
Glycosylationi46N-linked (GlcNAc...)Sequence analysis1
Glycosylationi53N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi140 ↔ 217PROSITE-ProRule annotation
Modified residuei166Phosphotyrosine1 Publication1
Lipidationi351S-palmitoyl cysteineSequence analysis1
Modified residuei363Phosphoserine1 Publication1
Modified residuei370Phosphothreonine1 Publication1
Modified residuei375Phosphoserine1 Publication1
Modified residuei394Phosphothreonine1 Publication1

Post-translational modificationi

Phosphorylated. Differentially phosphorylated in basal and agonist-induced conditions. Agonist-mediated phosphorylation modulates receptor internalization. Phosphorylated by GRK2 in a agonist-dependent manner. Phosphorylation at Tyr-166 requires receptor activation, is dependent on non-receptor protein tyrosine kinase Src and results in a decrease in agonist efficacy by reducing G-protein coupling efficiency. Phosphorylated on tyrosine residues; the phosphorylation is involved in agonist-induced G-protein-independent receptor down-regulation. Phosphorylation at Ser-375 is involved in G-protein-dependent but not beta-arrestin-dependent activation of the ERK pathway.5 Publications
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

PaxDbiP33535.

PTM databases

iPTMnetiP33535.
PhosphoSitePlusiP33535.
SwissPalmiP33535.

Expressioni

Tissue specificityi

Brain. Is expressed in the cerebral cortex, caudate putamen, nucleus accumbens, septal nuclei, thalamus, hippocampus, and habenula. Not detected in cerebellum.

Gene expression databases

BgeeiENSRNOG00000018191.
ExpressionAtlasiP33535. baseline and differential.
GenevisibleiP33535. RN.

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 (By similarity). Interacts with PLD2. Interacts with RANBP9 and WLS (By similarity). Interacts with GPM6A. Interacts with RTP4 (By similarity). Interacts with SYP and GNAS. Interacts with RGS9, RGS17 and RGS20 (By similarity). Interacts with RGS4. Interacts with PPP1R9B and HINT1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Gpm6aQ812E97EBI-4392569,EBI-6113756
Pld2P704983EBI-4392569,EBI-6140589
SypP078258EBI-4392569,EBI-976085
WlsQ6P6892EBI-4392569,EBI-6113235

GO - Molecular functioni

  • filamin binding Source: RGD
  • G-protein alpha-subunit binding Source: UniProtKB
  • G-protein beta-subunit binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein domain specific binding Source: RGD

Protein-protein interaction databases

IntActiP33535. 6 interactors.
STRINGi10116.ENSRNOP00000051290.

Chemistry databases

BindingDBiP33535.

Structurei

3D structure databases

ProteinModelPortaliP33535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP33535.
KOiK04215.
OMAiNSTRVRQ.
TreeFamiTF315737.

Family and domain databases

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 (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P33535-1) [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

        10         20         30         40         50
MDSSTGPGNT SDCSDPLAQA SCSPAPGSWL NLSHVDGNQS DPCGLNRTGL
60 70 80 90 100
GGNDSLCPQT GSPSMVTAIT IMALYSIVCV VGLFGNFLVM YVIVRYTKMK
110 120 130 140 150
TATNIYIFNL ALADALATST LPFQSVNYLM GTWPFGTILC KIVISIDYYN
160 170 180 190 200
MFTSIFTLCT MSVDRYIAVC HPVKALDFRT PRNAKIVNVC NWILSSAIGL
210 220 230 240 250
PVMFMATTKY RQGSIDCTLT FSHPTWYWEN LLKICVFIFA FIMPVLIITV
260 270 280 290 300
CYGLMILRLK SVRMLSGSKE KDRNLRRITR MVLVVVAVFI VCWTPIHIYV
310 320 330 340 350
IIKALITIPE TTFQTVSWHF CIALGYTNSC LNPVLYAFLD ENFKRCFREF
360 370 380 390
CIPTSSTIEQ QNSTRVRQNT REHPSTANTV DRTNHQLENL EAETAPLP
Length:398
Mass (Da):44,494
Last modified:February 1, 1994 - v1
Checksum:i9C916DE7C1C33743
GO
Isoform 2 (identifier: P33535-2) [UniParc]FASTAAdd to basket
Also known as: MOR1A

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

Show »
Length:390
Mass (Da):43,636
Checksum:i1880D1C9918035A4
GO
Isoform 3 (identifier: P33535-3) [UniParc]FASTAAdd to basket
Also known as: MOR1R

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

Show »
Length:390
Mass (Da):43,586
Checksum:i166612B3218035A4
GO
Isoform 4 (identifier: P33535-4) [UniParc]FASTAAdd to basket
Also known as: MOR1B

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

Show »
Length:391
Mass (Da):43,816
Checksum:i81767FCF38618035
GO
Isoform 5 (identifier: P33535-5) [UniParc]FASTAAdd to basket
Also known as: MOR1B2

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

Show »
Length:393
Mass (Da):43,986
Checksum:iA9819A64EBC80041
GO
Isoform 6 (identifier: P33535-6) [UniParc]FASTAAdd to basket
Also known as: MOR1C1

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

Show »
Length:451
Mass (Da):50,445
Checksum:iF1130789E14DF1F7
GO
Isoform 7 (identifier: P33535-7) [UniParc]FASTAAdd to basket
Also known as: MOR-1C2

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

Show »
Length:468
Mass (Da):52,410
Checksum:i55F763EE13B2B6D1
GO
Isoform 8 (identifier: P33535-8) [UniParc]FASTAAdd to basket
Also known as: rMOR-1D

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

Show »
Length:387
Mass (Da):43,317
Checksum:iBAF18035A454EB66
GO

Sequence cautioni

The sequence AAQ77387 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti237F → G in AAA79180 (PubMed:8189219).Curated1
Sequence conflicti238I → V in AAQ77386 (Ref. 7) Curated1
Sequence conflicti245V → I in AAA41630 (PubMed:8393525).Curated1
Sequence conflicti245V → I in AAA70049 (Ref. 4) Curated1
Sequence conflicti245V → I in S77863 (PubMed:7733926).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_041828387 – 398LENLE…TAPLP → VCAF in isoform 2. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041829387 – 398LENLE…TAPLP → GAEL in isoform 3. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041830387 – 398LENLE…TAPLP → KIVLF in isoform 4. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041831387 – 398LENLE…TAPLP → EPQSVET in isoform 5. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041832387 – 398LENLE…TAPLP → PALAVSVAQIFTGYPSPTHG EKPCKSYRDRPRPCGRTWSL KSRAESNVEHFHCGAALIYN NVNFI in isoform 6. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041833387 – 398LENLE…TAPLP → PALAVSVAQIFTGYPSPTHG EKPCKSYRDRPRPCGRTWSL KSRAESNVEHFHCGAALIYN NELKIGPVSWLQMPAHVLVR PW in isoform 7. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_041834387 – 398LENLE…TAPLP → T in isoform 8. 1 PublicationAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16349 mRNA. Translation: BAA03852.1.
L20684 mRNA. Translation: AAA41643.1.
L13069 mRNA. Translation: AAA41630.1.
U02083 mRNA. Translation: AAA70049.1.
L22455 mRNA. Translation: AAA16075.1.
U35424 mRNA. Translation: AAA79180.1.
AY309003 mRNA. Translation: AAQ77387.1. Frameshift.
AY309004 mRNA. Translation: AAQ77388.1.
AY225402 mRNA. Translation: AAP44725.1.
AY225403 mRNA. Translation: AAP44726.1.
AY309000 mRNA. Translation: AAQ77384.1.
AY309002 mRNA. Translation: AAQ77386.1.
S77863 mRNA. No translation available.
S75669 mRNA. Translation: AAB33530.2.
PIRiI56504.
I56517.
S69010.
RefSeqiNP_001033686.1. NM_001038597.2. [P33535-2]
NP_001033688.2. NM_001038599.2. [P33535-5]
NP_001033689.1. NM_001038600.2. [P33535-6]
NP_001033690.1. NM_001038601.2. [P33535-7]
NP_001291664.1. NM_001304735.1. [P33535-1]
NP_001291666.1. NM_001304737.1. [P33535-1]
NP_001291667.1. NM_001304738.1. [P33535-1]
NP_001291669.1. NM_001304740.1. [P33535-1]
NP_037203.1. NM_013071.2. [P33535-1]
UniGeneiRn.10118.

Genome annotation databases

EnsembliENSRNOT00000024682; ENSRNOP00000024682; ENSRNOG00000018191. [P33535-6]
ENSRNOT00000079628; ENSRNOP00000072626; ENSRNOG00000018191. [P33535-8]
ENSRNOT00000083308; ENSRNOP00000074079; ENSRNOG00000018191. [P33535-1]
ENSRNOT00000092034; ENSRNOP00000068988; ENSRNOG00000018191. [P33535-7]
GeneIDi25601.
KEGGirno:25601.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16349 mRNA. Translation: BAA03852.1.
L20684 mRNA. Translation: AAA41643.1.
L13069 mRNA. Translation: AAA41630.1.
U02083 mRNA. Translation: AAA70049.1.
L22455 mRNA. Translation: AAA16075.1.
U35424 mRNA. Translation: AAA79180.1.
AY309003 mRNA. Translation: AAQ77387.1. Frameshift.
AY309004 mRNA. Translation: AAQ77388.1.
AY225402 mRNA. Translation: AAP44725.1.
AY225403 mRNA. Translation: AAP44726.1.
AY309000 mRNA. Translation: AAQ77384.1.
AY309002 mRNA. Translation: AAQ77386.1.
S77863 mRNA. No translation available.
S75669 mRNA. Translation: AAB33530.2.
PIRiI56504.
I56517.
S69010.
RefSeqiNP_001033686.1. NM_001038597.2. [P33535-2]
NP_001033688.2. NM_001038599.2. [P33535-5]
NP_001033689.1. NM_001038600.2. [P33535-6]
NP_001033690.1. NM_001038601.2. [P33535-7]
NP_001291664.1. NM_001304735.1. [P33535-1]
NP_001291666.1. NM_001304737.1. [P33535-1]
NP_001291667.1. NM_001304738.1. [P33535-1]
NP_001291669.1. NM_001304740.1. [P33535-1]
NP_037203.1. NM_013071.2. [P33535-1]
UniGeneiRn.10118.

3D structure databases

ProteinModelPortaliP33535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP33535. 6 interactors.
STRINGi10116.ENSRNOP00000051290.

Chemistry databases

BindingDBiP33535.
ChEMBLiCHEMBL270.
GuidetoPHARMACOLOGYi319.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP33535.
PhosphoSitePlusiP33535.
SwissPalmiP33535.

Proteomic databases

PaxDbiP33535.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024682; ENSRNOP00000024682; ENSRNOG00000018191. [P33535-6]
ENSRNOT00000079628; ENSRNOP00000072626; ENSRNOG00000018191. [P33535-8]
ENSRNOT00000083308; ENSRNOP00000074079; ENSRNOG00000018191. [P33535-1]
ENSRNOT00000092034; ENSRNOP00000068988; ENSRNOG00000018191. [P33535-7]
GeneIDi25601.
KEGGirno:25601.

Organism-specific databases

CTDi4988.
RGDi3234. Oprm1.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118797.
HOGENOMiHOG000230486.
HOVERGENiHBG106919.
InParanoidiP33535.
KOiK04215.
OMAiNSTRVRQ.
TreeFamiTF315737.

Enzyme and pathway databases

ReactomeiR-RNO-111885. Opioid Signalling.
R-RNO-202040. G-protein activation.
R-RNO-375276. Peptide ligand-binding receptors.
R-RNO-418594. G alpha (i) signalling events.

Miscellaneous databases

PROiP33535.

Gene expression databases

BgeeiENSRNOG00000018191.
ExpressionAtlasiP33535. baseline and differential.
GenevisibleiP33535. RN.

Family and domain databases

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]
ProtoNetiSearch...

Entry informationi

Entry nameiOPRM_RAT
AccessioniPrimary (citable) accession number: P33535
Secondary accession number(s): Q2TV20
, Q2TV21, Q4VWM5, Q4VWM7, Q4VWX7, Q4VWX8, Q62846, Q64064, Q64120
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.