LipidDB ID

LipidDB-10116-01428

Entry Name

UniProt Accession

P33535; Q2TV20; Q2TV21; Q4VWM5; Q4VWM7; Q4VWX7; Q4VWX8; Q62846; Q64064; Q64120;

Theoretical PI

8.52

Molecular Weight

44493.99

Genbank Protein ID

BAA03852.1; AAA41643.1; AAA41630.1; AAA70049.1; AAA16075.1; AAA79180.1; AAQ77387.1; AAQ77388.1; AAP44725.1; AAP44726.1; AAQ77384.1; AAQ77386.1; AAB33530.2;

Genbank Nucleotide ID

D16349; L20684; L13069; U02083; L22455; U35424; AY309003; AY309004; AY225402; AY225403; AY309000; AY309002; S77863; S75669;

Protein Name

Mu-type opioid receptor

Protein Synonyms/Alias

M-OR-1; MOR-1; Opioid receptor B;

Gene Name

Oprm1

Gene Synonyms/Alias

Ror-b;

Created Date

01-FEB-1994

Organism

Rattus norvegicus (Rat)

NCBI Taxa ID

10116

Reference

[1] Zheng H, Pearsall EA, Hurst DP, Zhang Y, Chu J, Zhou Y, Reggio PH, Loh HH, LawPY. Palmitoylation and membrane cholesterol stabilize μ-opioid receptorhomodimerization and G protein coupling. BMC Cell Biol. 2012 Mar 19;13:6. doi:10.1186/1471-2121-13-6.[PMID:22429589]

Functional Description

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.

Sequence Annotation

Topological domain: 1 66 Extracellular.
Transmembrane: 67 91 Helical; Name=1.
Topological domain: 92 104 Cytoplasmic.
Transmembrane: 105 129 Helical; Name=2.
Topological domain: 130 140 Extracellular.
Transmembrane: 141 163 Helical; Name=3.
Topological domain: 164 183 Cytoplasmic.
Transmembrane: 184 205 Helical; Name=4.
Topological domain: 206 228 Extracellular.
Transmembrane: 229 253 Helical; Name=5.
Topological domain: 254 281 Cytoplasmic.
Transmembrane: 282 305 Helical; Name=6.
Topological domain: 306 312 Extracellular.
Transmembrane: 313 336 Helical; Name=7.
Topological domain: 337 398 Cytoplasmic.
Modified residue: 166 166 Phosphotyrosine.
Modified residue: 363 363 Phosphoserine.
Modified residue: 370 370 Phosphothreonine.
Modified residue: 375 375 Phosphoserine.
Modified residue: 394 394 Phosphothreonine.

Protein Length

398 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005737; C:cytoplasm; IDA:RGD
GO:0030425; C:dendrite; IDA:RGD
GO:0032839; C:dendrite cytoplasm; IDA:RGD
GO:0032590; C:dendrite membrane; IDA:RGD
GO:0005925; C:focal adhesion; IDA:RGD
GO:0005887; C:integral component of plasma membrane; TAS:RGD
GO:0016020; C:membrane; IDA:RGD
GO:0045121; C:membrane raft; IDA:RGD
GO:0043204; C:perikaryon; IDA:RGD
GO:0004979; F:beta-endorphin receptor activity; IEA:Ensembl
GO:0031005; F:filamin binding; IMP:RGD
GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB
GO:0031681; F:G-protein beta-subunit binding; IPI:RGD
GO:0004930; F:G-protein coupled receptor activity; IMP:UniProtKB
GO:0038047; F:morphine receptor activity; IMP:UniProtKB
GO:0019904; F:protein domain specific binding; IPI:RGD
GO:0005245; F:voltage-gated calcium channel activity; IMP:UniProtKB
GO:0002438; P:acute inflammatory response to antigenic stimulus; IEP:RGD
GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IEA:Ensembl
GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IDA:RGD
GO:0031635; P:adenylate cyclase-inhibiting opioid receptor signaling pathway; IDA:RGD
GO:0048149; P:behavioral response to ethanol; IEA:Ensembl
GO:0070588; P:calcium ion transmembrane transport; IMP:GOC
GO:0071315; P:cellular response to morphine; IDA:GOC
GO:0033554; P:cellular response to stress; IEA:Ensembl
GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:RGD
GO:0006955; P:immune response; TAS:RGD
GO:0007626; P:locomotory behavior; IEA:Ensembl
GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:UniProtKB
GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB
GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISS:UniProtKB
GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB
GO:0061358; P:negative regulation of Wnt protein secretion; ISS:UniProtKB
GO:0038003; P:opioid receptor signaling pathway; IDA:RGD
GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB
GO:0032100; P:positive regulation of appetite; IMP:RGD
GO:0043950; P:positive regulation of cAMP-mediated signaling; IEA:Ensembl
GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl
GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB
GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB
GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl
GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IDA:RGD
GO:2000310; P:regulation of N-methyl-D-aspartate selective glutamate receptor activity; IMP:UniProtKB
GO:0051930; P:regulation of sensory perception of pain; IDA:RGD
GO:0042220; P:response to cocaine; IEP:RGD
GO:0045471; P:response to ethanol; IDA:RGD
GO:0032094; P:response to food; IEP:RGD
GO:0070848; P:response to growth factor; IEP:RGD
GO:0032496; P:response to lipopolysaccharide; IEP:RGD
GO:0043278; P:response to morphine; IEP:RGD
GO:0019233; P:sensory perception of pain; ISS:UniProtKB
GO:0042060; P:wound healing; IEP:RGD

Interpro

InterPro; IPR000276; GPCR_Rhodpsn
InterPro; IPR017452; GPCR_Rhodpsn_7TM
InterPro; IPR000105; Mu_opioid_rcpt
InterPro; IPR001418; Opioid_rcpt

Pfam

Pfam; PF00001; 7tm_1;

SMART

PROSITE

PROSITE; PS00237; G_PROTEIN_RECEP_F1_1;
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2;

PRINTS

PRINTS; PR00237; GPCRRHODOPSN;
PRINTS; PR00537; MUOPIOIDR;
PRINTS; PR00384; OPIOIDR;