SCTR_RABIT
ID SCTR_RABIT Reviewed; 445 AA.
AC O46502;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Secretin receptor;
DE Short=SCT-R;
DE Flags: Precursor;
GN Name=SCTR;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9700755; DOI=10.1016/s0196-9781(98)00040-0;
RA Svoboda M., Tastenoy M., de Neef P., Delporte C., Waelbroeck M.,
RA Robberecht P.;
RT "Molecular cloning and in vitro properties of the recombinant rabbit
RT secretin receptor.";
RL Peptides 19:1055-1062(1998).
CC -!- FUNCTION: Receptor for secretin (SCT), which is involved in different
CC processes such as regulation of the pH of the duodenal content, food
CC intake and water homeostasis. The activity of this receptor is mediated
CC by G proteins which activate adenylyl cyclase (By similarity). Upon
CC binding to secretin, regulates the pH of the duodenum by (1) inhibiting
CC the secretion of gastric acid from the parietal cells of the stomach
CC and (2) stimulating the production of bicarbonate (NaHCO(3)) from the
CC ductal cells of the pancreas (By similarity). In addition to regulating
CC the pH of the duodenal content, plays a central role in diet induced
CC thermogenesis: acts as a non-sympathetic brown fat (BAT) activator
CC mediating prandial thermogenesis, which consequentially induces
CC satiation. Mechanistically, secretin released by the gut after a meal
CC binds to secretin receptor (SCTR) in brown adipocytes, activating brown
CC fat thermogenesis by stimulating lipolysis, which is sensed in the
CC brain and promotes satiation. Also able to stimulate lipolysis in white
CC adipocytes. Also plays an important role in cellular osmoregulation by
CC regulating renal water reabsorption. Also plays a role in the central
CC nervous system: required for synaptic plasticity (By similarity).
CC {ECO:0000250|UniProtKB:P11384, ECO:0000250|UniProtKB:Q5FWI2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P23811};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylated on Ser and Thr residues at the cytoplasmic C-
CC terminus by G protein-coupled receptor kinases (GRKs).
CC {ECO:0000250|UniProtKB:P23811}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; AF025411; AAC32767.1; -; mRNA.
DR RefSeq; NP_001075497.1; NM_001082028.1.
DR AlphaFoldDB; O46502; -.
DR SMR; O46502; -.
DR STRING; 9986.ENSOCUP00000006668; -.
DR PRIDE; O46502; -.
DR GeneID; 100008671; -.
DR KEGG; ocu:100008671; -.
DR CTD; 6344; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; O46502; -.
DR OrthoDB; 651627at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009992; P:cellular water homeostasis; ISS:UniProtKB.
DR GO; GO:0002024; P:diet induced thermogenesis; ISS:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0032098; P:regulation of appetite; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0031667; P:response to nutrient levels; ISS:UniProtKB.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR002144; GPCR_2_secretin_rcpt.
DR PANTHER; PTHR45620:SF13; PTHR45620:SF13; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR00490; SECRETINR.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..445
FT /note="Secretin receptor"
FT /id="PRO_0000012853"
FT TOPO_DOM 22..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..163
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..190
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..236
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..272
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..313
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..358
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..365
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..388
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 50495 MW; 31C4169CB099F194 CRC64;
MCPRPGPPLG LWLLLGFACA AHLVGAPPRL CDVLWVLQEE RDQCLQELER ERLGEEQPVP
GCQGLWDNVS CWPSSAPGRM VELECPRFLR MLTNSNGSLF RNCTQDGWTE TFPRPDLACG
VSMNDSSHER QHAYLLKLKV MYTVGYSSSL VMLLVALGIL CAFRRLHCTR NYIHMHLFLS
FILRALSNFI KDAVLFSSDD AIHCDAHRVG CKLVMVFFQY CIMANYAWLL VEGLYLHSLL
VVSFFSERKC LQGFVVLGWG SPAMFVTSWA VTRHFLEDSG CWDINANAAI WWVIRGPVIL
SILINFILFI NILRILTRKL RTQETRGQDM NHYKRLARST LLLIPLFGVH YIVFVFSPEG
AMEIQLFFEL ALGSFQGLVV AVLYCFLNGE VQLEVQKKWQ QWHLWEPPLC PVALSSSFSN
GTSSLNSTKA CPSGRSRDTC KVSII
