OPRL1
entrez
4987
canonical
uniprot
P41146
canonical
ensembl
ENSG00000125510
resolver
ensp
ENSP00000336764
resolver
ensp
ENSP00000336843
resolver
ensp
ENSP00000347848
resolver
ensp
ENSP00000500894
resolver
ensp
ENSP00000549309
resolver
ensp
ENSP00000612780
resolver
ensp
ENSP00000612782
resolver
enst
ENST00000672146
resolver
genesymbol
OPRL1
resolver
genesymbol_syn
OOR
resolver
genesymbol_syn
ORL1
resolver
hgnc
HGNC:8155
resolver
uniprot
A0A5F9ZI64
resolver
uniprot
Q8IXB0
resolver
uniprot
Q8TD34
resolver
uniprot
Q8WYH9
resolver
uniprot
Q9H4K4
resolver
uniprot_entry
A0A5F9ZI64_HUMAN
resolver
uniprot_entry
OPRX_HUMAN
resolver
uniprot_entry
Q8IXB0_HUMAN
resolver
uniprot_sec
Q8TD34
resolver
uniprot_sec
Q8WYH9
resolver
uniprot_sec
Q9H4K4
resolver
amino_acid_sequence
MEPLFPAPFWEVIYGSHLQGNLSLLSPNHSLLPPHLLLNASHGAFLPLGLKVTIVGLYLAVCVGGLLGNCLVMYVILRHTKMKTATNIYIFNLALADTLVLLTLPFQGTDILLGFWPFGNALCKTVIAIDYYNMFTSTFTLTAMSVDRYVAICHPIRALDVRTSSKAQAVNVAIWALASVVGVPVAIMGSAQVEDEEIECLVEIPTPQDYWGPVFAICIFLFSFIVPVLVISVCYSLMIRRLRGVRLLSGSREKDRNLRRITRLVLVVVAVFVGCWTPVQVFVLAQGLGVQPSSETAVAILRFCTALGYVNSCLNPILYAFLDENFKACFRKFCCASALRRDVQVSDRVRSIAKDVALACKTSETVPRPA
uniprot
proteins
function
FUNCTION: G protein-coupled opioid receptor that functions as a receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin. {ECO:0000269|PubMed:11238602, ECO:0000269|PubMed:12568343, ECO:0000269|PubMed:22596163, ECO:0000269|PubMed:23086955, ECO:0000269|PubMed:8137918}.
uniprot
proteins
mass_dalton
40693
uniprot
proteins
mutagenesis
MUTAGEN 107; /note="Q->A: Impairs G protein-mediated inhibition of adenylate cyclase."; /evidence="ECO:0000269|PubMed:22596163"; MUTAGEN 110; /note="D->A: Abolishes G protein-mediated inhibition of adenylate cyclase. No effect on antagonist-mediated inhibition of G protein-mediated signaling."; /evidence="ECO:0000269|PubMed:22596163"; MUTAGEN 130; /note="D->A: Abolishes G protein-mediated inhibition of adenylate cyclase. Abolishes antagonist-mediated inhibition of G protein-mediated signaling."; /evidence="ECO:0000269|PubMed:22596163"; MUTAGEN 131; /note="Y->A: Impairs G protein-mediated inhibition of adenylate cyclase."; /evidence="ECO:0000269|PubMed:22596163"; MUTAGEN 280; /note="Q->A: Impairs G protein-mediated inhibition of adenylate cyclase."; /evidence="ECO:0000269|PubMed:22596163"; MUTAGEN 309; /note="Y->A: Mildly impairs G protein-mediated inhibition of adenylate cyclase. Abolishes antagonist-mediated inhibition of G protein-mediated signaling."; /evidence="ECO:0000269|PubMed:22596163"; MUTAGEN 337; /note="S->A: No effect on ligand-mediated internalization; when associated with A-346 and A-351."; /evidence="ECO:0000269|PubMed:23086955"; MUTAGEN 346; /note="S->A: No effect on ligand-mediated internalization; when associated with A-337 and A-351."; /evidence="ECO:0000269|PubMed:23086955"; MUTAGEN 351; /note="S->A: No effect on ligand-mediated internalization; when associated with A-337 and A-346."; /evidence="ECO:0000269|PubMed:23086955"; MUTAGEN 363; /note="S->A: Impairs ligand-mediated internalization."; /evidence="ECO:0000269|PubMed:23086955
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-363 requires GRK3. {ECO:0000269|PubMed:23086955}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
11238602
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12568343
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22596163
uniprot
proteins
pubmed
23086955
uniprot
proteins
pubmed
7500847
uniprot
proteins
pubmed
8137918
uniprot
proteins
sequence_length
370
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle. Note=Ligand binding leads to receptor internalization into cytoplasmic vesicles, decreasing the amount of available receptor at the cell surface. Internalization requires phosphorylation at Ser-363. Can recycle to the cell membrane.
uniprot
proteins
transmembrane_region
TRANSMEM 49..74; /note="Helical; Name=1"; TRANSMEM 88..109; /note="Helical; Name=2"; TRANSMEM 125..146; /note="Helical; Name=3"; TRANSMEM 166..188; /note="Helical; Name=4"; TRANSMEM 212..236; /note="Helical; Name=5"; TRANSMEM 265..285; /note="Helical; Name=6"; TRANSMEM 301..322; /note="Helical; Name=7
uniprot
proteins