Oprm1
entrez
25601
canonical
uniprot
P33535
canonical
ensembl
ENSRNOG00000018191
resolver
ensp
ENSRNOP00000024682
resolver
ensp
ENSRNOP00000074079
resolver
ensp
ENSRNOP00000082784
resolver
ensp
ENSRNOP00000085499
resolver
enst
ENSRNOT00000083308
resolver
enst
ENSRNOT00000092578
resolver
genesymbol
Oprm1
resolver
genesymbol_syn
Ror-b
resolver
uniprot
A0A8I5ZVK2
resolver
uniprot
A0A8L2R8W0
resolver
uniprot
Q2TV20
resolver
uniprot
Q2TV21
resolver
uniprot
Q4VWM5
resolver
uniprot
Q4VWM7
resolver
uniprot
Q4VWX7
resolver
uniprot
Q4VWX8
resolver
uniprot
Q62846
resolver
uniprot
Q64064
resolver
uniprot
Q64120
resolver
uniprot_entry
A0A8I5ZVK2_RAT
resolver
uniprot_entry
A0A8L2R8W0_RAT
resolver
uniprot_entry
OPRM_RAT
resolver
uniprot_sec
Q2TV20
resolver
uniprot_sec
Q2TV21
resolver
uniprot_sec
Q4VWM5
resolver
uniprot_sec
Q4VWM7
resolver
uniprot_sec
Q4VWX7
resolver
uniprot_sec
Q4VWX8
resolver
uniprot_sec
Q62846
resolver
uniprot_sec
Q64064
resolver
uniprot_sec
Q64120
resolver
amino_acid_sequence
MDSSTGPGNTSDCSDPLAQASCSPAPGSWLNLSHVDGNQSDPCGLNRTGLGGNDSLCPQTGSPSMVTAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGTILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIVNVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALITIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSTIEQQNSTRVRQNTREHPSTANTVDRTNHQLENLEAETAPLP
uniprot
proteins
function
FUNCTION: Receptor for endogenous opioids such as beta-endorphin and endomorphin (PubMed:11060299, PubMed:15944153, PubMed:16682964, PubMed:17384143, PubMed:17947509, PubMed:1846076, PubMed:18558479, PubMed:21292762, PubMed:7595566, PubMed:7678862, PubMed:8051154, PubMed:8240812, PubMed:8393525, PubMed:9224819, PubMed:9572309). Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone (PubMed:11060299, PubMed:15944153, PubMed:16682964, PubMed:17384143, PubMed:17947509, PubMed:1846076, PubMed:18558479, PubMed:21292762, PubMed:7595566, PubMed:7678862, PubMed:8051154, PubMed:8240812, PubMed:8393525, PubMed:9224819, PubMed:9572309). Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (PubMed:8624732). 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:16682964, PubMed:9224819). 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:9224819, PubMed:9572309). 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 (PubMed:15944153, PubMed:21292762, PubMed:7595566, PubMed:9572309). Also couples to adenylate cyclase stimulatory G alpha proteins (PubMed:7595566). 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 (PubMed:11060299, PubMed:17384143, PubMed:17947509, PubMed:18558479). 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 (PubMed:11278523, PubMed:11896051, PubMed:15944153). 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 (PubMed:11060299, PubMed:17384143, PubMed:17947509, PubMed:18558479). Endogenous ligands induce rapid desensitization, endocytosis and recycling. Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties (PubMed:16682964, PubMed:17384143). {ECO:0000269|PubMed:11060299, ECO:0000269|PubMed:11278523, ECO:0000269|PubMed:11896051, ECO:0000269|PubMed:15944153, ECO:0000269|PubMed:16682964, ECO:0000269|PubMed:17384143, ECO:0000269|PubMed:17947509, ECO:0000269|PubMed:1846076, ECO:0000269|PubMed:18558479, ECO:0000269|PubMed:21292762, ECO:0000269|PubMed:7595566, ECO:0000269|PubMed:7678862, ECO:0000269|PubMed:8051154, ECO:0000269|PubMed:8240812, ECO:0000269|PubMed:8393525, ECO:0000269|PubMed:8624732, ECO:0000269|PubMed:9224819, ECO:0000269|PubMed:9572309}.
uniprot
proteins
mass_dalton
44494
uniprot
proteins
mutagenesis
MUTAGEN 91; /note="Y->A: Abolishes agonist-induced G protein-independent receptor internalization; when associated with A-96, A-166 and A-336."; /evidence="ECO:0000269|PubMed:10488100"; MUTAGEN 96; /note="Y->A: Abolishes agonist-induced G protein-independent receptor internalization; when associated with A-91, A-166 and A-336."; /evidence="ECO:0000269|PubMed:10488100"; MUTAGEN 114; /note="D->A,N: Impairs agonist affinity, agonist-induced inhibition of adenylate cyclase and coupling to G-proteins."; /evidence="ECO:0000269|PubMed:8051154, ECO:0000269|PubMed:9224819"; MUTAGEN 114; /note="D->E: No effect on inhibition of adenylate cyclase."; /evidence="ECO:0000269|PubMed:8051154, ECO:0000269|PubMed:9224819"; MUTAGEN 147; /note="D->A: No effect on constitutive activation. Impairs agonist affinity and agonist-induced inhibition of adenylate cyclase."; /evidence="ECO:0000269|PubMed:11580279, ECO:0000269|PubMed:8051154"; MUTAGEN 147; /note="D->E: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase."; /evidence="ECO:0000269|PubMed:11580279, ECO:0000269|PubMed:8051154"; MUTAGEN 147; /note="D->N: No effect on constitutive activation."; /evidence="ECO:0000269|PubMed:11580279, ECO:0000269|PubMed:8051154"; MUTAGEN 164; /note="D->E: Reduces basal activity."; /evidence="ECO:0000269|PubMed:11580279"; MUTAGEN 164; /note="D->H,M,Q,Y: Constitutive active."; /evidence="ECO:0000269|PubMed:11580279"; MUTAGEN 166; /note="Y->A: Abolishes agonist-induced G protein-independent receptor internalization; when associated with A-91, A-96 and A-336."; /evidence="ECO:0000269|PubMed:10488100, ECO:0000269|PubMed:19959593"; MUTAGEN 166; /note="Y->F: Decrease in phosphorylation, no decrease in G-protein binding."; /evidence="ECO:0000269|PubMed:10488100, ECO:0000269|PubMed:19959593"; MUTAGEN 180; /note="T->A: Impairs ARRB2- and GRK3-mediated receptor desensitization."; /evidence="ECO:0000269|PubMed:11060299"; MUTAGEN 275; /note="L->E: No effect on constitutive activation. Some constitutive activity; when associated with K-279."; /evidence="ECO:0000269|PubMed:12356297"; MUTAGEN 279; /note="T->D: Receptor inactivation."; /evidence="ECO:0000269|PubMed:11695897, ECO:0000269|PubMed:12356297"; MUTAGEN 279; /note="T->K: Constitutive active. Some constitutive activity; when associated with E-275."; /evidence="ECO:0000269|PubMed:11695897, ECO:0000269|PubMed:12356297"; MUTAGEN 297; /note="H->A: Impairs agonist affinity and increases agonist-induced inhibition of adenylate cyclase."; /evidence="ECO:0000269|PubMed:8051154"; MUTAGEN 336; /note="Y->A: Abolishes agonist-induced G protein-independent receptor internalization; when associated with A-91, A-96 and A-166."; /evidence="ECO:0000269|PubMed:10488100"; MUTAGEN 346; /note="C->A: No change in palmitoylation. No change in palmitoylation; when associated with A-351."; /evidence="ECO:0000269|PubMed:9877183"; MUTAGEN 351; /note="C->A: No change in palmitoylation; when associated with A-346."; /evidence="ECO:0000269|PubMed:9877183"; MUTAGEN 363; /note="S->A: Abolishes basal phosphorylation; when associated with A-370. Abolishes basal and agonist-induced phosphorylation; when associated with A-370 and A-375. Accelerates agonist-induced receptor internalization."; /evidence="ECO:0000269|PubMed:11278523, ECO:0000269|PubMed:18558479"; MUTAGEN 370; /note="T->A: Abolishes basal phosphorylation; when associated with A-363. Abolishes basal and agonist-induced phosphorylation; when associated with A-363 and A-375. Accelerates agonist-induced receptor internalization."; /evidence="ECO:0000269|PubMed:11278523, ECO:0000269|PubMed:18558479"; MUTAGEN 375; /note="S->A: Reduces agonist-induced receptor internalization. Abolishes morphine-induced phosphorylation. Restores agonist-specific PRKCE activity. Abolishes basal and agonist-induced phosphorylation; when associated with A-363 and A-370."; /evidence="ECO:0000269|PubMed:11278523, ECO:0000269|PubMed:18558479, ECO:0000269|PubMed:21292762"; MUTAGEN 394; /note="T->A: Impairs phosphorylation and abolishes agonist-mediated acute receptor desensitization."; /evidence="ECO:0000269|PubMed:10488100, ECO:0000269|PubMed:10820022
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:0000269|PubMed:10488100, ECO:0000269|PubMed:10744734, ECO:0000269|PubMed:10820022, ECO:0000269|PubMed:11278523, ECO:0000269|PubMed:19959593}.; 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
10488100
uniprot
proteins
pubmed
10744734
uniprot
proteins
pubmed
10820022
uniprot
proteins
pubmed
10842167
uniprot
proteins
pubmed
11060299
uniprot
proteins
pubmed
11278523
uniprot
proteins
pubmed
11580279
uniprot
proteins
pubmed
11695897
uniprot
proteins
pubmed
11896051
uniprot
proteins
pubmed
12356297
uniprot
proteins
pubmed
12519790
uniprot
proteins
pubmed
14645661
uniprot
proteins
pubmed
14729105
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15525342
uniprot
proteins
pubmed
15857684
uniprot
proteins
pubmed
15944153
uniprot
proteins
pubmed
16682964
uniprot
proteins
pubmed
17005904
uniprot
proteins
pubmed
17384143
uniprot
proteins
pubmed
17548356
uniprot
proteins
pubmed
17947509
uniprot
proteins
pubmed
1846076
uniprot
proteins
pubmed
18558479
uniprot
proteins
pubmed
19324084
uniprot
proteins
pubmed
19959593
uniprot
proteins
pubmed
21292762
uniprot
proteins
pubmed
7532594
uniprot
proteins
pubmed
7595566
uniprot
proteins
pubmed
7678862
uniprot
proteins
pubmed
7733926
uniprot
proteins
pubmed
8051154
uniprot
proteins
pubmed
8189219
uniprot
proteins
pubmed
8234282
uniprot
proteins
pubmed
8240812
uniprot
proteins
pubmed
8393525
uniprot
proteins
pubmed
8394245
uniprot
proteins
pubmed
8624732
uniprot
proteins
pubmed
9224819
uniprot
proteins
pubmed
9572309
uniprot
proteins
pubmed
9877183
uniprot
proteins
sequence_length
398
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8240812, ECO:0000269|PubMed:8393525}; 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}.
uniprot
proteins
transmembrane_region
TRANSMEM 67..91; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 105..129; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 141..163; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 184..205; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 229..253; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 278..304; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P42866"; TRANSMEM 313..336; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P42866
uniprot
proteins