Sctr
entrez
319229
canonical
uniprot
Q5FWI2
canonical
ensembl
ENSMUSG00000026387
resolver
ensp
ENSMUSP00000072660
resolver
ensp
ENSMUSP00000139932
resolver
ensp
ENSMUSP00000219038
resolver
ensp
ENSMUSP00000219040
resolver
ensp
ENSMUSP00000219045
resolver
ensp
ENSMUSP00000219050
resolver
enst
ENSMUST00000072886
resolver
enst
ENSMUST00000189037
resolver
genesymbol
Sctr
resolver
uniprot
H7BX37
resolver
uniprot
Q80T66
resolver
uniprot_entry
H7BX37_MOUSE
resolver
uniprot_entry
SCTR_MOUSE
resolver
uniprot_sec
Q80T66
resolver
amino_acid_sequence
MLSTMSPRLSLLLLWLLLLINAAHPVGALPRLCDVRRVLLEERAECLRELSEEKKALGPKTASGCERFWDNMSCWPSSALAQTVEVPCPKFLRMFSGRNGSLFRNCTKDGWSETFPRPDLACGVNMNGSFNERRHAYLLKLKVMYTVGYSSSLAMLLVALSILCSFRRLHCTRNYIHMHLFVSFILRALSNFIKDAVLFPADDVTYCDAHRAGCKLVMIFFQYCIMANYAWLLVEGLYLHTLLAISFFSERKCLQAFVLFGWGSPAIFVALWAVTRHFLEDFGCWDINSNASIWWVIRGPVILSIVINFIFFINILRILMRKLRTQETRGNETHHYKRLAKSTLLLIPLFGIHYIVFAFSPEGAMEVQLFFELALGSFQGLVVAVLYCFLNGELEVQKKWRQWHLQEFPLRPVALSNSFSNATNGPTHSTKAGTSEQSRSIPGANVI
uniprot
proteins
function
FUNCTION: G protein-coupled receptor activated by secretin (SCT), which is involved in different processes such as regulation of the pH of the duodenal content, food intake and water homeostasis (PubMed:20927047, PubMed:24273196, PubMed:30449620). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and activates cAMP-dependent pathway (PubMed:30449620). Upon binding to secretin, regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation (PubMed:30449620). Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation (PubMed:30449620). Also able to stimulate lipolysis in white adipocytes (PubMed:24273196). Also plays an important role in cellular osmoregulation by regulating renal water reabsorption (PubMed:17283064). Also plays a role in the central nervous system: required for synaptic plasticity (PubMed:17008357). {ECO:0000250|UniProtKB:P11384, ECO:0000269|PubMed:17008357, ECO:0000269|PubMed:17283064, ECO:0000269|PubMed:20927047, ECO:0000269|PubMed:24273196, ECO:0000269|PubMed:30449620}.
uniprot
proteins
mass_dalton
50932
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Ser and Thr residues at the cytoplasmic C-terminus by G protein-coupled receptor kinases (GRKs). {ECO:0000250|UniProtKB:P23811}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
12679517
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17008357
uniprot
proteins
pubmed
17283064
uniprot
proteins
pubmed
20927047
uniprot
proteins
pubmed
24273196
uniprot
proteins
pubmed
24769669
uniprot
proteins
pubmed
30449620
uniprot
proteins
sequence_length
447
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17283064}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47872}. Basolateral cell membrane {ECO:0000269|PubMed:17283064}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47872}. Note=In the renal medulla, localized on the basolateral membranes of cells in the collecting ducts. {ECO:0000269|PubMed:17283064}.
uniprot
proteins
transmembrane_region
TRANSMEM 141..166; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 174..194; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 216..238; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 254..275; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 291..314; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 340..355; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 367..390; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P47872
uniprot
proteins