OXTR
entrez
5021
canonical
uniprot
P30559
canonical
ensembl
ENSG00000180914
resolver
ensp
ENSP00000324270
resolver
ensp
ENSP00000564748
resolver
ensp
ENSP00000564749
resolver
ensp
ENSP00000564750
resolver
ensp
ENSP00000564751
resolver
enst
ENST00000316793
resolver
enst
ENST00000894689
resolver
enst
ENST00000894690
resolver
enst
ENST00000894691
resolver
enst
ENST00000894692
resolver
genesymbol
OXTR
resolver
hgnc
HGNC:8529
resolver
uniprot
B2R9L7
resolver
uniprot
Q15071
resolver
uniprot_entry
B2R9L7_HUMAN
resolver
uniprot_entry
OXYR_HUMAN
resolver
uniprot_sec
Q15071
resolver
activity_regulation
ACTIVITY REGULATION: Directly inhibited by progesterone, which prevents oxytocin-binding (By similarity). Cholesterol and magnesium act as allosteric activators (PubMed:32832646, PubMed:35241813). {ECO:0000250|UniProtKB:P70536, ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813}.
uniprot
proteins
amino_acid_sequence
MEGALAANWSAEAANASAAPPGAEGNRTAGPPRRNEALARVEVAVLCLILLLALSGNACVLLALRTTRQKHSRLFFFMKHLSIADLVVAVFQVLPQLLWDITFRFYGPDLLCRLVKYLQVVGMFASTYLLLLMSLDRCLAICQPLRSLRRRTDRLAVLATWLGCLVASAPQVHIFSLREVADGVFDCWAVFIQPWGPKAYITWITLAVYIVPVIVLAACYGLISFKIWQNLRLKTAAAAAAEAPEGAAAGDGGRVALARVSSVKLISKAKIRTVKMTFIIVLAFIVCWTPFFFVQMWSVWDANAPKEASAFIIVMLLASLNSCCNPWIYMLFTGHLFHELVQRFLCCSASYLKGRRLGETSASKKSNSSSFVLSHRSSSQRSCSQPSTA
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for oxytocin (OXT), a neuropeptide hormone released by the posterior pituitary gland that plays a key role in social behavior and other biological processes, such as milk ejection (PubMed:11923477, PubMed:22069312, PubMed:32832646, PubMed:35104164, PubMed:35241813, PubMed:35851571). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as phospholipase C (PubMed:22069312, PubMed:32832646, PubMed:35104164, PubMed:35241813, PubMed:35851571). OXTR is mainly coupled to G(q) G proteins and mediates production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) second messengers that modulate the activity of phosphatidylinositol 3-kinase and promote the release of Ca(2+) ions from intracellular stores, respectively (PubMed:11923477, PubMed:22069312, PubMed:32832646, PubMed:35104164, PubMed:35241813, PubMed:35851571). In presence of high levels of oxytocin, also coupled to G(i) G proteins, mediating inhibition of adenylate cyclase activity (PubMed:22069312, PubMed:35241813, PubMed:35851571). Central release of oxytocin plays essential roles in social behavior, such as maternal care, social cognition and affiliative behaviors, triggering signaling that modulates neural circuits by altering ion channel activity, changing intrinsic neuronal properties and modifying synaptic transmission (both excitatory and inhibitory) (PubMed:19934046, PubMed:20647384, PubMed:21896752, PubMed:22123970, PubMed:24367110). Peripheral release of oxytocin (secretion into the bloodstream) promotes various processes, such as parturition, lactation or osteoblast differentiation (PubMed:6278592). OXTR-mediated signaling promotes milk ejection by triggering and strengthening contraction of the smooth muscle of mammary gland (By similarity). {ECO:0000250|UniProtKB:P97926, ECO:0000269|PubMed:11923477, ECO:0000269|PubMed:19934046, ECO:0000269|PubMed:20647384, ECO:0000269|PubMed:21896752, ECO:0000269|PubMed:22069312, ECO:0000269|PubMed:22123970, ECO:0000269|PubMed:24367110, ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35104164, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, ECO:0000269|PubMed:6278592}.
uniprot
proteins
mass_dalton
42772
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="R->A: Decreased activation by oxytocin."; /evidence="ECO:0000269|PubMed:35241813"; MUTAGEN 42; /note="E->A: Decreased activation by magnesium."; /evidence="ECO:0000269|PubMed:32832646"; MUTAGEN 100; /note="D->A: Decreased activation by magnesium."; /evidence="ECO:0000269|PubMed:32832646"; MUTAGEN 100; /note="D->K: Activated both in presence of absence of magnesium."; /evidence="ECO:0000269|PubMed:35241813"; MUTAGEN 103; /note="F->A: Decreased activation by oxytocin."; /evidence="ECO:0000269|PubMed:35241813"; MUTAGEN 116; /note="K->A: Decreased activation by oxytocin."; /evidence="ECO:0000269|PubMed:32832646"; MUTAGEN 119; /note="Q->A: Decreased activation by oxytocin."; /evidence="ECO:0000269|PubMed:32832646"; MUTAGEN 171; /note="Q->A,N: Decreased activation by oxytocin."; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35851571"; MUTAGEN 200; /note="Y->A: Decreased aallosteric activation by cholesterol."; /evidence="ECO:0000269|PubMed:32832646"; MUTAGEN 201; /note="I->A: Decreased activation by oxytocin."; /evidence="ECO:0000269|PubMed:35851571"; MUTAGEN 203; /note="W->A: Decreased activation by cholesterol."; /evidence="ECO:0000269|PubMed:32832646"; MUTAGEN 204; /note="I->A: Decreased activation by oxytocin."; /evidence="ECO:0000269|PubMed:35851571"; MUTAGEN 261; /note="S->A: Abolished phosphorylation by PRKD1."; /evidence="ECO:0000269|PubMed:35104164"; MUTAGEN 261; /note="S->E: Mimics phosphorylation; increased G(q)-dependent signaling."; /evidence="ECO:0000269|PubMed:35104164"; MUTAGEN 268; /note="K->A: Does not impair G(q)-dependent signaling."; /evidence="ECO:0000269|PubMed:11923477"; MUTAGEN 270; /note="K->A: Abolished G(q)-dependent signaling."; /evidence="ECO:0000269|PubMed:11923477"; MUTAGEN 291; /note="F->A: Decreased activation by oxytocin."; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35851571
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-261 by PRKD1 promotes association with G(q) G protein and downstream signaling, enhancing long-term social memory (PubMed:35104164). Phosphorylated by GRK2, GRK3 and/or GRK6 following prolonged stimulation by oxytocin, promoting association with beta-arrestin (ARRB1 or ARRB2), leading to receptor desensitization and negative regulation of G protein-coupled receptor signaling (PubMed:11279203, PubMed:14976224, PubMed:16179383, PubMed:19423652). {ECO:0000269|PubMed:11279203, ECO:0000269|PubMed:14976224, ECO:0000269|PubMed:16179383, ECO:0000269|PubMed:19423652, ECO:0000269|PubMed:35104164}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
protein_family
Vasopressin/oxytocin receptor subfamily
uniprot
proteins
pubmed
11279203
uniprot
proteins
pubmed
11923477
uniprot
proteins
pubmed
1313946
uniprot
proteins
pubmed
14976224
uniprot
proteins
pubmed
16179383
uniprot
proteins
pubmed
19423652
uniprot
proteins
pubmed
19934046
uniprot
proteins
pubmed
20647384
uniprot
proteins
pubmed
21896752
uniprot
proteins
pubmed
22069312
uniprot
proteins
pubmed
22123970
uniprot
proteins
pubmed
24367110
uniprot
proteins
pubmed
32832646
uniprot
proteins
pubmed
35104164
uniprot
proteins
pubmed
35241813
uniprot
proteins
pubmed
35851571
uniprot
proteins
pubmed
6278592
uniprot
proteins
pubmed
7798245
uniprot
proteins
sequence_length
389
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16179383, ECO:0000269|PubMed:22069312}; Multi-pass membrane protein {ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571}.
uniprot
proteins
transmembrane_region
TRANSMEM 36..58; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, ECO:0007744|PDB:6TPK, ECO:0007744|PDB:7QVM, ECO:0007744|PDB:7RYC"; TRANSMEM 77..102; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, ECO:0007744|PDB:6TPK, ECO:0007744|PDB:7QVM, ECO:0007744|PDB:7RYC"; TRANSMEM 109..139; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, ECO:0007744|PDB:6TPK, ECO:0007744|PDB:7QVM, ECO:0007744|PDB:7RYC"; TRANSMEM 154..174; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, ECO:0007744|PDB:6TPK, ECO:0007744|PDB:7QVM, ECO:0007744|PDB:7RYC"; TRANSMEM 200..225; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, ECO:0007744|PDB:6TPK, ECO:0007744|PDB:7QVM, ECO:0007744|PDB:7RYC"; TRANSMEM 273..296; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, ECO:0007744|PDB:6TPK, ECO:0007744|PDB:7QVM, ECO:0007744|PDB:7RYC"; TRANSMEM 309..329; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:32832646, ECO:0000269|PubMed:35241813, ECO:0000269|PubMed:35851571, ECO:0007744|PDB:6TPK, ECO:0007744|PDB:7QVM, ECO:0007744|PDB:7RYC
uniprot
proteins