OPRM1
entrez
4988
canonical
uniprot
P35372
canonical
ensembl
ENSG00000112038
resolver
ensp
ENSP00000229768
resolver
ensp
ENSP00000328264
resolver
ensp
ENSP00000338381
resolver
ensp
ENSP00000353598
resolver
ensp
ENSP00000394624
resolver
ensp
ENSP00000399359
resolver
ensp
ENSP00000403549
resolver
ensp
ENSP00000410497
resolver
ensp
ENSP00000411903
resolver
ensp
ENSP00000413752
resolver
ensp
ENSP00000429373
resolver
ensp
ENSP00000429719
resolver
ensp
ENSP00000430097
resolver
ensp
ENSP00000430260
resolver
ensp
ENSP00000430876
resolver
enst
ENST00000360422
resolver
genesymbol
OPRM1
resolver
genesymbol_syn
MOP
resolver
genesymbol_syn
MOR
resolver
genesymbol_syn
MOR1
resolver
genesymbol_syn
OPRM
resolver
hgnc
HGNC:8156
resolver
uniprot
A0A0A0MRG7
resolver
uniprot
A0A6H0WF09
resolver
uniprot
B0FXJ1
resolver
uniprot
B2R9S7
resolver
uniprot
B8K2Q5
resolver
uniprot
B8Q1L7
resolver
uniprot
B8Q1L8
resolver
uniprot
B8Q1L9
resolver
uniprot
E7EWZ3
resolver
uniprot
G8XRH4
resolver
uniprot
G8XRH5
resolver
uniprot
G8XRH6
resolver
uniprot
G8XRH8
resolver
uniprot
L0E130
resolver
uniprot
Q12930
resolver
uniprot
Q4VWM1
resolver
uniprot
Q4VWM2
resolver
uniprot
Q4VWM3
resolver
uniprot
Q4VWM4
resolver
uniprot
Q4VWM6
resolver
uniprot
Q4VWX6
resolver
uniprot
Q5TDA1
resolver
uniprot
Q6UPP1
resolver
uniprot
Q6UQ80
resolver
uniprot
Q7Z2D8
resolver
uniprot
Q86V80
resolver
uniprot
Q8IWW3
resolver
uniprot
Q8IWW4
resolver
uniprot
Q9UCZ4
resolver
uniprot
Q9UN57
resolver
uniprot_entry
A0A0A0MRG7_HUMAN
resolver
uniprot_entry
A0A6H0WF09_HUMAN
resolver
uniprot_entry
B8K2Q5_HUMAN
resolver
uniprot_entry
G8XRH4_HUMAN
resolver
uniprot_entry
G8XRH5_HUMAN
resolver
uniprot_entry
L0E130_HUMAN
resolver
uniprot_entry
OPRM_HUMAN
resolver
uniprot_sec
B0FXJ1
resolver
uniprot_sec
B2R9S7
resolver
uniprot_sec
B8Q1L7
resolver
uniprot_sec
B8Q1L8
resolver
uniprot_sec
B8Q1L9
resolver
uniprot_sec
E7EWZ3
resolver
uniprot_sec
G8XRH6
resolver
uniprot_sec
G8XRH8
resolver
uniprot_sec
Q12930
resolver
uniprot_sec
Q4VWM1
resolver
uniprot_sec
Q4VWM2
resolver
uniprot_sec
Q4VWM3
resolver
uniprot_sec
Q4VWM4
resolver
uniprot_sec
Q4VWM6
resolver
uniprot_sec
Q4VWX6
resolver
uniprot_sec
Q5TDA1
resolver
uniprot_sec
Q6UPP1
resolver
uniprot_sec
Q6UQ80
resolver
uniprot_sec
Q7Z2D8
resolver
uniprot_sec
Q86V80
resolver
uniprot_sec
Q8IWW3
resolver
uniprot_sec
Q8IWW4
resolver
uniprot_sec
Q9UCZ4
resolver
uniprot_sec
Q9UN57
resolver
amino_acid_sequence
MDSSAAPTNASNCTDALAYSSCSPAPSPGSWVNLSHLDGNLSDPCGPNRTDLGGRDSLCPPTGSPSMITAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIINVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALVTIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSNIEQQNSTRIRQNTRDHPSTANTVDRTNHQLENLEAETAPLP
uniprot
proteins
function
FUNCTION: Receptor for endogenous opioids such as beta-endorphin and endomorphin (PubMed:10529478, PubMed:12589820, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128). Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone (PubMed:10529478, PubMed:10836142, PubMed:12589820, PubMed:19300905, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128). Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (By similarity). 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 (PubMed:7905839). 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 extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15 (PubMed:12068084). 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 (By similarity). Also couples to adenylate cyclase stimulatory G alpha proteins (By similarity). The selective temporal coupling to G proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4 (By similarity). Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization (By similarity). Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G protein thus terminating signal transduction (By similarity). The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins (By similarity). 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 (By similarity). 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 (By similarity). Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G protein coupling (By similarity). Endogenous ligands induce rapid desensitization, endocytosis and recycling (By similarity). Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties (By similarity). {ECO:0000250|UniProtKB:P33535, ECO:0000269|PubMed:10529478, ECO:0000269|PubMed:12068084, ECO:0000269|PubMed:12589820, ECO:0000269|PubMed:7891175, ECO:0000269|PubMed:7905839, ECO:0000269|PubMed:7957926, ECO:0000269|PubMed:9689128, ECO:0000303|PubMed:10836142, ECO:0000303|PubMed:19300905}.; FUNCTION: [Isoform 12]: Couples to GNAS and is proposed to be involved in excitatory effects. {ECO:0000269|PubMed:20525224}.; FUNCTION: [Isoform 16]: Does not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity. {ECO:0000269|PubMed:16580639}.; FUNCTION: [Isoform 17]: Does not bind agonists but may act through oligomerization with binding-competent OPRM1 isoforms and reduce their ligand binding activity. {ECO:0000269|PubMed:16580639}.
uniprot
proteins
mass_dalton
44779
uniprot
proteins
mutagenesis
MUTAGEN 142; /note="C->A,S: Abolishes ligand binding; when associated with A-219 or S-219."; /evidence="ECO:0000269|PubMed:10529478"; MUTAGEN 219; /note="C->A,S: Abolishes ligand binding; when associated with A-142 or S-142."; /evidence="ECO:0000269|PubMed:10529478"; MUTAGEN 273; /note="K->A: Impairs interaction with calmodulin."; /evidence="ECO:0000269|PubMed:10419536, ECO:0000269|PubMed:10899953"; MUTAGEN 275; /note="R->A: Impairs interaction with calmodulin."; /evidence="ECO:0000269|PubMed:10899953
uniprot
proteins
post_translational_modification
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 does not seem 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}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10393893
uniprot
proteins
pubmed
10419536
uniprot
proteins
pubmed
10529478
uniprot
proteins
pubmed
10836142
uniprot
proteins
pubmed
10899953
uniprot
proteins
pubmed
12068084
uniprot
proteins
pubmed
12413885
uniprot
proteins
pubmed
12519790
uniprot
proteins
pubmed
12589820
uniprot
proteins
pubmed
12734358
uniprot
proteins
pubmed
12810704
uniprot
proteins
pubmed
14573758
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15778451
uniprot
proteins
pubmed
15893644
uniprot
proteins
pubmed
15967873
uniprot
proteins
pubmed
16542645
uniprot
proteins
pubmed
16580639
uniprot
proteins
pubmed
17224450
uniprot
proteins
pubmed
19077058
uniprot
proteins
pubmed
19103668
uniprot
proteins
pubmed
19300905
uniprot
proteins
pubmed
19788913
uniprot
proteins
pubmed
20214800
uniprot
proteins
pubmed
20525224
uniprot
proteins
pubmed
7488213
uniprot
proteins
pubmed
7891175
uniprot
proteins
pubmed
7905839
uniprot
proteins
pubmed
7957926
uniprot
proteins
pubmed
9399694
uniprot
proteins
pubmed
9689128
uniprot
proteins
sequence_length
400
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10529478, ECO:0000269|PubMed:12589820, ECO:0000269|PubMed:16580639, ECO:0000269|PubMed:7891175, ECO:0000269|PubMed:7905839, ECO:0000269|PubMed:7957926, ECO:0000269|PubMed:9689128}; Multi-pass membrane protein {ECO:0000269|PubMed:16580639}. 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}.; SUBCELLULAR LOCATION: [Isoform 12]: Cytoplasm {ECO:0000269|PubMed:20525224}.
uniprot
proteins
transmembrane_region
TRANSMEM 69..93; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 107..131; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 143..165; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 186..207; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 231..255; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 280..306; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 315..338; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P42866
uniprot
proteins