Oprm1
entrez
18390
canonical
uniprot
P42866
canonical
ensembl
ENSMUSG00000000766
resolver
ensp
ENSMUSP00000000783
resolver
ensp
ENSMUSP00000053498
resolver
ensp
ENSMUSP00000060329
resolver
ensp
ENSMUSP00000077704
resolver
ensp
ENSMUSP00000101226
resolver
ensp
ENSMUSP00000101227
resolver
ensp
ENSMUSP00000101230
resolver
ensp
ENSMUSP00000101232
resolver
ensp
ENSMUSP00000101236
resolver
ensp
ENSMUSP00000101240
resolver
ensp
ENSMUSP00000114342
resolver
ensp
ENSMUSP00000117950
resolver
ensp
ENSMUSP00000120187
resolver
enst
ENSMUST00000078634
resolver
enst
ENSMUST00000105601
resolver
enst
ENSMUST00000123861
resolver
genesymbol
Oprm1
resolver
genesymbol_syn
Mor
resolver
genesymbol_syn
Oprm
resolver
uniprot
A0A0R4J0Z2
resolver
uniprot
A1KZZ4
resolver
uniprot
A1XGX3
resolver
uniprot
A1XGX4
resolver
uniprot
A1YAC3
resolver
uniprot
A1YAC4
resolver
uniprot
A5H7G2
resolver
uniprot
F7CYI1
resolver
uniprot
Q4U2P4
resolver
uniprot
Q4U2Q6
resolver
uniprot
Q548C6
resolver
uniprot
Q60768
resolver
uniprot
Q6YC50
resolver
uniprot
Q8CAN5
resolver
uniprot
Q8CGW2
resolver
uniprot
Q8CH73
resolver
uniprot
Q8CH74
resolver
uniprot
Q8CH75
resolver
uniprot
Q8VBU3
resolver
uniprot
Q8VBU6
resolver
uniprot
Q8VBX8
resolver
uniprot
Q8VI69
resolver
uniprot
Q8VI70
resolver
uniprot
Q8VI71
resolver
uniprot
Q8VIN3
resolver
uniprot
Q8VIN4
resolver
uniprot
Q8VIN5
resolver
uniprot
Q8VIN6
resolver
uniprot
Q8VIP0
resolver
uniprot
Q8VIP1
resolver
uniprot
Q9JIY1
resolver
uniprot
Q9R0D1
resolver
uniprot
Q9R1L9
resolver
uniprot
Q9R1M0
resolver
uniprot_entry
A0A0R4J0Z2_MOUSE
resolver
uniprot_entry
A1KZZ4_MOUSE
resolver
uniprot_entry
F7CYI1_MOUSE
resolver
uniprot_entry
OPRM_MOUSE
resolver
uniprot_sec
A1XGX3
resolver
uniprot_sec
A1XGX4
resolver
uniprot_sec
A1YAC3
resolver
uniprot_sec
A1YAC4
resolver
uniprot_sec
A5H7G2
resolver
uniprot_sec
Q4U2P4
resolver
uniprot_sec
Q4U2Q6
resolver
uniprot_sec
Q548C6
resolver
uniprot_sec
Q60768
resolver
uniprot_sec
Q6YC50
resolver
uniprot_sec
Q8CAN5
resolver
uniprot_sec
Q8CGW2
resolver
uniprot_sec
Q8CH73
resolver
uniprot_sec
Q8CH74
resolver
uniprot_sec
Q8CH75
resolver
uniprot_sec
Q8VBU3
resolver
uniprot_sec
Q8VBU6
resolver
uniprot_sec
Q8VBX8
resolver
uniprot_sec
Q8VI69
resolver
uniprot_sec
Q8VI70
resolver
uniprot_sec
Q8VI71
resolver
uniprot_sec
Q8VIN3
resolver
uniprot_sec
Q8VIN4
resolver
uniprot_sec
Q8VIN5
resolver
uniprot_sec
Q8VIN6
resolver
uniprot_sec
Q8VIP0
resolver
uniprot_sec
Q8VIP1
resolver
uniprot_sec
Q9JIY1
resolver
uniprot_sec
Q9R0D1
resolver
uniprot_sec
Q9R1L9
resolver
uniprot_sec
Q9R1M0
resolver
amino_acid_sequence
MDSSAGPGNISDCSDPLAPASCSPAPGSWLNLSHVDGNQSDPCGPNRTGLGGSHSLCPQTGSPSMVTAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGNILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIVNVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALITIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSTIEQQNSARIRQNTREHPSTANTVDRTNHQLENLEAETAPLP
uniprot
proteins
function
FUNCTION: Receptor for endogenous opioids such as beta-endorphin and endomorphin (PubMed:10842167, PubMed:16682964, PubMed:21422164, PubMed:22437502, PubMed:26245379, PubMed:7797593, PubMed:9037090). Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone (PubMed:16682964, PubMed:7797593, PubMed:9037090). Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (PubMed:35201898, PubMed:6933569). 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:10842167, PubMed:21422164, PubMed:22437502). 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:26245379, PubMed:9767386). 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 (PubMed:15827571, PubMed:17725581). 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 (PubMed:12642578). 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. 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:10842167, ECO:0000269|PubMed:12642578, ECO:0000269|PubMed:15827571, ECO:0000269|PubMed:16682964, ECO:0000269|PubMed:17725581, ECO:0000269|PubMed:21422164, ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379, ECO:0000269|PubMed:35201898, ECO:0000269|PubMed:6933569, ECO:0000269|PubMed:7797593, ECO:0000269|PubMed:9037090, ECO:0000269|PubMed:9767386}.; FUNCTION: [Isoform 9]: Isoform 9 is involved in morphine-induced scratching and seems to cross-activate GRPR in response to morphine. {ECO:0000269|PubMed:22000021}.
uniprot
proteins
mass_dalton
44421
uniprot
proteins
mutagenesis
MUTAGEN 387; /note="L->A: Abolishes receptor recycling; when associated with A-390."; /evidence="ECO:0000269|PubMed:12939277"; MUTAGEN 390; /note="L->A: Abolishes receptor recycling; when associated with A-387."; /evidence="ECO:0000269|PubMed:12939277
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-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. {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:0000269|PubMed:18836069}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10419560
uniprot
proteins
pubmed
10682855
uniprot
proteins
pubmed
10842167
uniprot
proteins
pubmed
11160404
uniprot
proteins
pubmed
11717463
uniprot
proteins
pubmed
12270145
uniprot
proteins
pubmed
12642578
uniprot
proteins
pubmed
12939277
uniprot
proteins
pubmed
14991152
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15827571
uniprot
proteins
pubmed
15939800
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16682964
uniprot
proteins
pubmed
17398041
uniprot
proteins
pubmed
17725581
uniprot
proteins
pubmed
18439408
uniprot
proteins
pubmed
18836069
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21153910
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21422164
uniprot
proteins
pubmed
22000021
uniprot
proteins
pubmed
22437502
uniprot
proteins
pubmed
26245379
uniprot
proteins
pubmed
28350844
uniprot
proteins
pubmed
35201898
uniprot
proteins
pubmed
6933569
uniprot
proteins
pubmed
7649256
uniprot
proteins
pubmed
7797593
uniprot
proteins
pubmed
8090773
uniprot
proteins
pubmed
9037090
uniprot
proteins
pubmed
9767386
uniprot
proteins
sequence_length
398
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12642578, ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:7797593}; Multi-pass membrane protein {ECO:0000269|PubMed:12642578, ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379, ECO:0000269|PubMed:7797593}. 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}.
uniprot
proteins
transmembrane_region
TRANSMEM 67..91; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379"; TRANSMEM 105..129; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379"; TRANSMEM 141..163; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379"; TRANSMEM 184..205; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379"; TRANSMEM 229..253; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379"; TRANSMEM 278..304; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379"; TRANSMEM 313..336; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:22437502, ECO:0000269|PubMed:26245379
uniprot
proteins