Sctr
entrez
81779
canonical
uniprot
P23811
canonical
ensembl
ENSRNOG00000049766
resolver
ensembl
ENSRNOG00055012884
resolver
ensembl
ENSRNOG00060005612
resolver
ensembl
ENSRNOG00065009515
resolver
ensp
ENSRNOP00000064579
resolver
ensp
ENSRNOP00000077594
resolver
ensp
ENSRNOP00000103353
resolver
ensp
ENSRNOP00055017922
resolver
ensp
ENSRNOP00060007027
resolver
ensp
ENSRNOP00065011446
resolver
enst
ENSRNOT00000119961
resolver
enst
ENSRNOT00000143096
resolver
enst
ENSRNOT00055022080
resolver
enst
ENSRNOT00060009352
resolver
enst
ENSRNOT00065015246
resolver
genesymbol
Sctr
resolver
uniprot
A0A8I5YBX3
resolver
uniprot
A0ABK0LJ14
resolver
uniprot_entry
A0A8I5YBX3_RAT
resolver
uniprot_entry
A0ABK0LJ14_RAT
resolver
uniprot_entry
SCTR_RAT
resolver
amino_acid_sequence
MLSTMRPRLSLLLLRLLLLTKAAHTVGVPPRLCDVRRVLLEERAHCLQQLSKEKKGALGPETASGCEGLWDNMSCWPSSAPARTVEVQCPKFLLMLSNKNGSLFRNCTQDGWSETFPRPDLACGVNINNSFNERRHAYLLKLKVMYTVGYSSSLAMLLVALSILCSFRRLHCTRNYIHMHLFVSFILRALSNFIKDAVLFSSDDVTYCDAHKVGCKLVMIFFQYCIMANYAWLLVEGLYLHTLLAISFFSERKYLQAFVLLGWGSPAIFVALWAITRHFLENTGCWDINANASVWWVIRGPVILSILINFIFFINILRILMRKLRTQETRGSETNHYKRLAKSTLLLIPLFGIHYIVFAFSPEDAMEVQLFFELALGSFQGLVVAVLYCFLNGEVQLEVQKKWRQWHLQEFPLRPVAFNNSFSNATNGPTHSTKASTEQSRSIPRASII
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:12403838, PubMed:25332973). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and activates cAMP-dependent pathway (PubMed:12403838, PubMed:9506976). 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. 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. Also able to stimulate lipolysis in white adipocytes. Also plays an important role in cellular osmoregulation by regulating renal water reabsorption. Also plays a role in the central nervous system: required for synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:P11384, ECO:0000250|UniProtKB:Q5FWI2, ECO:0000269|PubMed:12403838, ECO:0000269|PubMed:9506976, ECO:0000303|PubMed:25332973}.
uniprot
proteins
mass_dalton
51234
uniprot
proteins
mutagenesis
MUTAGEN 36; /note="R->A: Strong reduction in secretin (SCT)-binding."; /evidence="ECO:0000269|PubMed:12403838"; MUTAGEN 37; /note="R->A: Reduction in secretin (SCT)-binding."; /evidence="ECO:0000269|PubMed:12403838
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:0000269|PubMed:7476911, ECO:0000269|PubMed:9506976}.; PTM: N-glycosylated. {ECO:0000269|PubMed:7476911}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
12403838
uniprot
proteins
pubmed
15276242
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1646711
uniprot
proteins
pubmed
25332973
uniprot
proteins
pubmed
7476911
uniprot
proteins
pubmed
9506976
uniprot
proteins
sequence_length
449
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7476911, ECO:0000269|PubMed:9506976}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47872}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q5FWI2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47872}.
uniprot
proteins
transmembrane_region
TRANSMEM 142..167; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 175..195; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 217..239; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 255..276; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 292..315; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 341..356; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P47872"; TRANSMEM 368..391; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P47872
uniprot
proteins