LipidDB ID

LipidDB-10090-00020

Entry Name

UniProt Accession

P42866; A1XGX3; A1XGX4; A1YAC3; A1YAC4; A5H7G2; Q4U2P4; Q4U2Q6; Q548C6; Q60768; Q6YC50; Q8CAN5; Q8CGW2; Q8CH73; Q8CH74; Q8CH75; Q8VBU3; Q8VBU6; Q8VBX8; Q8VI69; Q8VI70; Q8VI71; Q8VIN3; Q8VIN4; Q8VIN5; Q8VIN6; Q8VIP0; Q8VIP1; Q9JIY1; Q9R0D1; Q9R1L9; Q9R1M0;

Theoretical PI

8.62

Molecular Weight

44420.98

Genbank Protein ID

AAB60673.1; AAB60673.1; AAB60673.1; AAB60673.1; AAA81170.1; AAA86878.1; AAD54415.1; AAD51861.1; AAD51862.1; AAL55581.1; AAF79213.1; BAB63338.1; AAL34927.1; AAL34400.1; AAL34394.1; AAL34507.1; AAL34508.1; AAL34509.1; AAK74188.1; AAO18365.1; AAL55582.1; AAL55583.1; AAO13792.1; AAO13793.1; AAO13794.1; BAC29982.1; ABC94862.1; ABC94863.1; ABI95796.1; ABI95797.2; ABN45760.1; ABN45761.1; ABN45762.1; ABN45763.1; EDL03560.1; EDL03561.1; EDL03562.1; AAI19546.1;

Genbank Nucleotide ID

U10561; U10558; U10559; U10560; U26915; U19380; AF062753; AF074973; AF074974; AF167565; AF167568; AB047546; AF062755; AF260311; AF074972; AF400246; AF400247; AF400248; AY036621; AY160190; AF167566; AF167567; AF346812; AF346813; AF346814; AK038389; DQ363376; DQ363377; DQ868787; DQ868788; EF105311; EF105312; EF105313; EF105314; CH466562; CH466562; CH466562; AC153981; AC155718; AC164171; BC119545;

Protein Name

Mu-type opioid receptor

Protein Synonyms/Alias

M-OR-1; MOR-1;

Gene Name

Oprm1

Gene Synonyms/Alias

Mor; Oprm;

Created Date

01-NOV-1995

Organism

Mus musculus (Mouse)

NCBI Taxa ID

10090

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. Isoform 9 is involved in morphine-induced scratching and seems to cross-activate GRPR in response to morphine.

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.

Protein Length

398 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IDA:MGI
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0004979; F:beta-endorphin receptor activity; IEA:Ensembl
GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB
GO:0004930; F:G-protein coupled receptor activity; ISS:UniProtKB
GO:0038047; F:morphine receptor activity; ISS:UniProtKB
GO:0004985; F:opioid receptor activity; IDA:MGI
GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB
GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:MGI
GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IDA:MGI
GO:0048149; P:behavioral response to ethanol; IEA:Ensembl
GO:0070588; P:calcium ion transmembrane transport; ISS:GOC
GO:0033554; P:cellular response to stress; IEA:Ensembl
GO:0007626; P:locomotory behavior; IMP:MGI
GO:0007194; P:negative regulation of adenylate cyclase activity; ISS: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:GOC
GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB
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; ISS:UniProtKB
GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB
GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl
GO:2000310; P:regulation of N-methyl-D-aspartate selective glutamate receptor activity; ISS:UniProtKB
GO:0019233; P:sensory perception of pain; IMP:UniProtKB

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;