SECR_RABIT
ID SECR_RABIT Reviewed; 27 AA.
AC P32647;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Secretin {ECO:0000303|PubMed:2342988};
GN Name=SCT {ECO:0000250|UniProtKB:P09683};
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 PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND AMIDATION AT LEU-27.
RC TISSUE=Small intestine;
RX PubMed=2342988; DOI=10.1016/0196-9781(90)90120-t;
RA Gossen D., Buscail L., Cauvin A., Gourlet P., de Neef P., Rathe J.,
RA Robberecht P., Vandermeers-Piret M.C., Vandermeers A., Christophe J.;
RT "Amino acid sequence of VIP, PHI and secretin from the rabbit small
RT intestine.";
RL Peptides 11:123-128(1990).
CC -!- FUNCTION: Hormone involved in different processes, such as regulation
CC of the pH of the duodenal content, food intake and water homeostasis.
CC Exerts its biological effects by binding to secretin receptor (SCTR), a
CC G-protein coupled receptor expressed in the basolateral domain of
CC several cells. Acts as a key gastrointestinal hormone by regulating the
CC pH of the duodenal content. Secreted by S cells of the duodenum in the
CC crypts of Lieberkuehn and regulates the pH of the duodenum by (1)
CC inhibiting the secretion of gastric acid from the parietal cells of the
CC stomach and (2) stimulating the production of bicarbonate (NaHCO(3))
CC from the ductal cells of the pancreas (By similarity). Production of
CC bicarbonate is essential to neutralize the pH and ensure no damage is
CC done to the small intestine by the gastric acid. In addition to
CC regulating the pH of the duodenal content, plays a central role in diet
CC induced thermogenesis: acts as a non-sympathetic brown fat (BAT)
CC activator mediating prandial thermogenesis, which consequentially
CC induces satiation. Mechanistically, secretin released by the gut after
CC a meal binds to secretin receptor (SCTR) in brown adipocytes,
CC activating brown fat thermogenesis by stimulating lipolysis, which is
CC sensed in the brain and promotes satiation. Also able to stimulate
CC lipolysis in white adipocytes (By similarity). Also plays an important
CC role in cellular osmoregulation: released into the systemic circulation
CC in response to hyperosmolality and acts at different levels in the
CC hypothalamus, pituitary and kidney to regulate water homeostasis (By
CC similarity). Also plays a role in the central nervous system, possibly
CC by acting as a neuropeptide hormone: required for hippocampal synaptic
CC function and neural progenitor cells maintenance (By similarity).
CC {ECO:0000250|UniProtKB:P11384, ECO:0000250|UniProtKB:Q08535}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2342988}.
CC -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR PIR; C60415; C60415.
DR AlphaFoldDB; P32647; -.
DR SMR; P32647; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0046659; F:digestive hormone activity; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; ISS:UniProtKB.
DR GO; GO:0002024; P:diet induced thermogenesis; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; 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 InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR Pfam; PF00123; Hormone_2; 1.
DR SMART; SM00070; GLUCA; 1.
DR PROSITE; PS00260; GLUCAGON; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Hormone; Reference proteome;
KW Secreted.
FT PEPTIDE 1..27
FT /note="Secretin"
FT /evidence="ECO:0000269|PubMed:2342988"
FT /id="PRO_0000043936"
FT MOD_RES 27
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:2342988"
SQ SEQUENCE 27 AA; 3106 MW; 38A015800BDD3618 CRC64;
HSDGTLTSEL SRLRDRARLQ RLLQGLL