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Mu-type opioid receptor (M-OR-1) (MOR-1)

 OPRM_MACFA              Reviewed;         400 AA.
Q95M54;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
28-MAR-2018, entry version 83.
RecName: Full=Mu-type opioid receptor;
Short=M-OR-1;
Short=MOR-1;
Name=OPRM1; Synonyms=MOR1;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=14699447; DOI=10.1038/sj.mp.4001378;
Miller G.M., Bendor J., Tiefenbacher S., Yang H., Novak M.A.,
Madras B.K.;
"A mu-opioid receptor single nucleotide polymorphism in rhesus monkey:
association with stress response and aggression.";
Mol. Psychiatry 9:99-108(2004).
-!- FUNCTION: 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, 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.
{ECO:0000250|UniProtKB:P33535, ECO:0000250|UniProtKB:P35372,
ECO:0000250|UniProtKB:P42866}.
-!- SUBUNIT: Forms homooligomers and heterooligomers with other GPCRs,
such as OPRD1, OPRK1, OPRL1, NPFFR2, ADRA2A, SSTR2, CNR1 and CCR5
(probably in dimeric forms). Interacts with heterotrimeric G
proteins; interaction with a heterotrimeric complex containing
GNAI1, GNB1 and GNG2 stabilizes the active conformation of the
receptor and increases its affinity for endomorphin-2, the
synthetic opioid peptide DAMGO and for morphinan agonists (By
similarity). Interacts with PPL; the interaction disrupts agonist-
mediated G-protein activation. Interacts (via C-terminus) with
DNAJB4 (via C-terminus). Interacts with calmodulin; the
interaction inhibits the constitutive activity of OPRM1; it
abolishes basal and attenuates agonist-stimulated G-protein
coupling. Interacts with FLNA, PLD2, RANBP9 and WLS and GPM6A (By
similarity). Interacts with RTP4 (By similarity). Interacts with
SYP and GNAS (By similarity). Interacts with RGS9, RGS17, RGS20,
RGS4, PPP1R9B and HINT1. {ECO:0000250|UniProtKB:P33535,
ECO:0000250|UniProtKB:P35372, ECO:0000250|UniProtKB:P42866}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P42866}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P42866}. Cell projection, axon
{ECO:0000250|UniProtKB:P97266}. Perikaryon
{ECO:0000250|UniProtKB:P97266}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P97266}. Endosome
{ECO:0000250|UniProtKB:P97266}. Note=Is rapidly internalized after
agonist binding. {ECO:0000250|UniProtKB:P97266}.
-!- PTM: 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-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).
{ECO:0000250|UniProtKB:P33535}.
-!- PTM: 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.
{ECO:0000250|UniProtKB:P42866}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; AY038989; AAK71884.1; -; mRNA.
RefSeq; NP_001274559.1; NM_001287630.1.
RefSeq; XP_015304310.1; XM_015448824.1.
UniGene; Mfa.9401; -.
ProteinModelPortal; Q95M54; -.
SMR; Q95M54; -.
Ensembl; ENSMFAT00000024546; ENSMFAP00000005866; ENSMFAG00000002542.
GeneID; 102123390; -.
KEGG; mcf:102123390; -.
CTD; 4988; -.
GeneTree; ENSGT00760000118797; -.
HOVERGEN; HBG106919; -.
KO; K04215; -.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0004979; F:beta-endorphin receptor activity; IEA:InterPro.
GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; ISS:UniProtKB.
GO; GO:0038047; F:morphine receptor activity; ISS:UniProtKB.
GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISS:UniProtKB.
GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0061358; P:negative regulation of Wnt protein secretion; ISS:UniProtKB.
GO; GO:0038003; P:opioid receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; ISS:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
CDD; cd15090; 7tmA_Mu_opioid_R; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR000105; Mu_opioid_rcpt.
InterPro; IPR001418; Opioid_rcpt.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR00537; MUOPIOIDR.
PRINTS; PR00384; OPIOIDR.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Cell membrane; Cell projection; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Receptor; Transducer; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 400 Mu-type opioid receptor.
/FTId=PRO_0000069973.
TOPO_DOM 1 68 Extracellular.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 69 93 Helical; Name=1.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 94 106 Cytoplasmic.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 107 131 Helical; Name=2.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 132 142 Extracellular.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 143 165 Helical; Name=3.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 166 185 Cytoplasmic.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 186 207 Helical; Name=4.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 208 230 Extracellular.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 231 255 Helical; Name=5.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 256 279 Cytoplasmic.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 280 306 Helical; Name=6.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 307 314 Extracellular.
{ECO:0000250|UniProtKB:P42866}.
TRANSMEM 315 338 Helical; Name=7.
{ECO:0000250|UniProtKB:P42866}.
TOPO_DOM 339 400 Cytoplasmic.
{ECO:0000250|UniProtKB:P42866}.
MOTIF 334 338 NPxxY; plays a role in stabilizing the
activated conformation of the receptor.
{ECO:0000250|UniProtKB:P42866}.
MOD_RES 168 168 Phosphotyrosine.
{ECO:0000250|UniProtKB:P33535}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000250|UniProtKB:P42866}.
MOD_RES 372 372 Phosphothreonine.
{ECO:0000250|UniProtKB:P33535}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000250|UniProtKB:P33535}.
MOD_RES 396 396 Phosphothreonine.
{ECO:0000250|UniProtKB:P33535}.
LIPID 353 353 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 9 9 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 12 12 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 142 219 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 400 AA; 44775 MW; 811811F36A2DC84C CRC64;
MDSSAVPTNA SNCTDALAHS SCSPAPSPGS WVNLSHLDGN LSDPCGPNRT DLGGRDSLCP
PTGSPSMITA ITIMALYSIV CVVGLFGNFL VMYVIVRYTK MKTATNIYIF NLALADALVT
STLPFQSVNY LMGTWPFGTI LCKIVISIDY YNMFTSIFTL CTMSVDRYIA VCHPVKALDF
RTPRNAKIIN VCNWILSSAI GLPVMFMATT KYRQGSIDCT LTFSHPSWYW ENLLKICVFI
FAFIMPVLII TVCYGLMILR LKSVRMLSGS KEKDRNLRRI TRMVLVVVAV FIICWTPIHI
YVIIKALVTI PETTLQTVSW HFCIALGYTN SCLNPVLYAF LDENFKRCFR EFCIPTSSNI
EQQNSTRIRQ NTRDHPSTAN TVDRTNHQLE NLEAETAPLP


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