SMS_RAT
ID SMS_RAT Reviewed; 116 AA.
AC P60042; P01167;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Somatostatin;
DE AltName: Full=somatotropin release-inhibiting factor {ECO:0000303|PubMed:22170057};
DE Short=SRIF {ECO:0000303|PubMed:22170057};
DE Contains:
DE RecName: Full=Antrin;
DE Contains:
DE RecName: Full=Somatostatin-28;
DE Contains:
DE RecName: Full=Somatostatin-14;
DE Contains:
DE RecName: Full=Neuronostatin {ECO:0000303|PubMed:18753129, ECO:0000303|PubMed:24735892};
DE Short=NST {ECO:0000303|PubMed:24735892};
DE Flags: Precursor;
GN Name=Sst; Synonyms=Smst;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6148343; DOI=10.1016/s0021-9258(20)71282-2;
RA Tavianini M.A., Hayes T.E., Magazin M.D., Minth C.D., Dixon J.E.;
RT "Isolation, characterization, and DNA sequence of the rat somatostatin
RT gene.";
RL J. Biol. Chem. 259:11798-11803(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6133871; DOI=10.1016/s0021-9258(20)81928-0;
RA Goodman R.H., Aron D.C., Roos B.A.;
RT "Rat pre-prosomatostatin. Structure and processing by microsomal
RT membranes.";
RL J. Biol. Chem. 258:5570-5573(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2863939; DOI=10.1007/978-1-4615-7886-4_3;
RA Goodman R.H., Montminy M.R., Low M.J., Habener J.F.;
RT "Biosynthesis of rat preprosomatostatin.";
RL Adv. Exp. Med. Biol. 188:31-47(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6145156; DOI=10.1073/pnas.81.11.3337;
RA Montminy M.R., Goodman R.H., Horovitch S.J., Habener J.F.;
RT "Primary structure of the gene encoding rat preprosomatostatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3337-3340(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 38-116.
RX PubMed=6120163; DOI=10.1016/s0021-9258(19)68167-6;
RA Goodman R.H., Jacobs J.W., Dee P.C., Habener J.F.;
RT "Somatostatin-28 encoded in a cloned cDNA obtained from a rat medullary
RT thyroid carcinoma.";
RL J. Biol. Chem. 257:1156-1159(1982).
RN [6]
RP PROTEIN SEQUENCE OF 25-34.
RC STRAIN=Sprague-Dawley; TISSUE=Stomach;
RX PubMed=2891188; DOI=10.1126/science.2891188;
RA Benoit R., Ling N., Esch F.;
RT "A new prosomatostatin-derived peptide reveals a pattern for prohormone
RT cleavage at monobasic sites.";
RL Science 238:1126-1129(1987).
RN [7]
RP FUNCTION (NEURONOSTATIN), AND TISSUE SPECIFICITY (NEURONOSTATIN).
RC TISSUE=Pancreas;
RX PubMed=18753129; DOI=10.1074/jbc.m804784200;
RA Samson W.K., Zhang J.V., Avsian-Kretchmer O., Cui K., Yosten G.L.,
RA Klein C., Lyu R.M., Wang Y.X., Chen X.Q., Yang J., Price C.J., Hoyda T.D.,
RA Ferguson A.V., Yuan X.B., Chang J.K., Hsueh A.J.;
RT "Neuronostatin encoded by the somatostatin gene regulates neuronal,
RT cardiovascular, and metabolic functions.";
RL J. Biol. Chem. 283:31949-31959(2008).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=20056135; DOI=10.1016/j.neuroscience.2009.12.059;
RA Dun S.L., Brailoiu G.C., Tica A.A., Yang J., Chang J.K., Brailoiu E.,
RA Dun N.J.;
RT "Neuronostatin is co-expressed with somatostatin and mobilizes calcium in
RT cultured rat hypothalamic neurons.";
RL Neuroscience 166:455-463(2010).
RN [9]
RP FUNCTION (NEURONOSTATIN), AND AMIDATION AT THR-43.
RX PubMed=21325646; DOI=10.1152/ajpregu.00849.2010;
RA Yosten G.L., Pate A.T., Samson W.K.;
RT "Neuronostatin acts in brain to biphasically increase mean arterial
RT pressure through sympatho-activation followed by vasopressin secretion: the
RT role of melanocortin receptors.";
RL Am. J. Physiol. 300:R1194-R1199(2011).
RN [10]
RP FUNCTION (NEURONOSTATIN).
RX PubMed=21978882; DOI=10.1016/j.neuroscience.2011.09.040;
RA Carlini V.P., Ghersi M., Gabach L., Schioeth H.B., Perez M.F.,
RA Ramirez O.A., Fiol de Cuneo M., de Barioglio S.R.;
RT "Hippocampal effects of neuronostatin on memory, anxiety-like behavior and
RT food intake in rats.";
RL Neuroscience 197:145-152(2011).
RN [11]
RP FUNCTION (NEURONOSTATIN).
RX PubMed=22170057; DOI=10.1074/jbc.m111.289215;
RA Vainio L., Perjes A., Ryti N., Magga J., Alakoski T., Serpi R.,
RA Kaikkonen L., Piuhola J., Szokodi I., Ruskoaho H., Kerkelae R.;
RT "Neuronostatin, a novel peptide encoded by somatostatin gene, regulates
RT cardiac contractile function and cardiomyocyte survival.";
RL J. Biol. Chem. 287:4572-4580(2012).
RN [12]
RP FUNCTION (NEURONOSTATIN).
RX PubMed=24735892; DOI=10.1152/ajpendo.00599.2013;
RA Salvatori A.S., Elrick M.M., Samson W.K., Corbett J.A., Yosten G.L.;
RT "Neuronostatin inhibits glucose-stimulated insulin secretion via direct
RT action on the pancreatic alpha-cell.";
RL Am. J. Physiol. 306:E1257-E1263(2014).
RN [13]
RP FUNCTION (NEURONOSTATIN), AND TISSUE SPECIFICITY (NEURONOSTATIN).
RX PubMed=26561648; DOI=10.1152/ajpregu.00369.2014;
RA Elrick M.M., Samson W.K., Corbett J.A., Salvatori A.S., Stein L.M.,
RA Kolar G.R., Naatz A., Yosten G.L.;
RT "Neuronostatin acts via GPR107 to increase cAMP-independent PKA
RT phosphorylation and proglucagon mRNA accumulation in pancreatic alpha-
RT cells.";
RL Am. J. Physiol. 310:R143-R155(2016).
CC -!- FUNCTION: [Somatostatin-14]: Inhibits the secretion of pituitary
CC hormones, including that of growth hormone/somatotropin (GH1), PRL,
CC ACTH, luteinizing hormone (LH) and TSH. Also impairs ghrelin- and GnRH-
CC stimulated secretion of GH1 and LH; the inhibition of ghrelin-
CC stimulated secretion of GH1 can be further increased by neuronostatin.
CC {ECO:0000250|UniProtKB:P61278}.
CC -!- FUNCTION: [Neuronostatin]: May enhance low-glucose-induced glucagon
CC release by pancreatic alpha cells (PubMed:24735892). This effect may be
CC mediated by binding to GPR107 and PKA activation (PubMed:26561648). May
CC regulate cardiac contractile function (PubMed:22170057). May compromise
CC cardiomyocyte viability (PubMed:22170057). In the central nervous
CC system, may impair memory retention and may affect hippocampal
CC excitability (PubMed:21978882). May also have anxiolytic and
CC anorexigenic effects (PubMed:18753129, PubMed:21978882). May play a
CC role in arterial pressure regulation (PubMed:18753129,
CC PubMed:21978882). May inhibit basal, but not ghrelin- or GnRH-
CC stimulated secretion of GH1 or LH, but does not affect the release of
CC other pituitary hormones, including PRL, ACTH, FSH or TSH (By
CC similarity). Potentiates inhibitory action of somatostatin on ghrelin-
CC stimulated secretion of GH1, but not that on GnRH-stimulated secretion
CC of LH (By similarity). {ECO:0000250|UniProtKB:P61278,
CC ECO:0000269|PubMed:18753129, ECO:0000269|PubMed:21978882,
CC ECO:0000269|PubMed:22170057, ECO:0000269|PubMed:24735892,
CC ECO:0000269|PubMed:26561648}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26561648}.
CC -!- TISSUE SPECIFICITY: Somatostatin is detected in neurons throughout the
CC brain, including in the lateral septum, nucleus accumbens, amygdaloid
CC complex, hypothalamic periventricular nucleus, hippocampus, cortex,
CC cerebellum and several brainstem nuclei (at protein level)
CC (PubMed:20056135). Neuronostatin is widely expressed with highest
CC levels in pleen and pancreas, followed by cerebrum and hypothalamus (at
CC protein level) (PubMed:18753129, PubMed:26561648). Neuronostatin plasma
CC levels are higher in fasted, as compared to fed animals
CC (PubMed:26561648). In the brain, neuronostatin is mainly present in the
CC hypothalamic periventricular nucleus and median eminence (at protein
CC level) (PubMed:20056135). {ECO:0000269|PubMed:18753129,
CC ECO:0000269|PubMed:20056135, ECO:0000269|PubMed:26561648}.
CC -!- PTM: C-terminal amidation of the neuronostatin peptide is required for
CC its biological activity, including for the regulation of mean arterial
CC pressure. {ECO:0000269|PubMed:21325646}.
CC -!- SIMILARITY: Belongs to the somatostatin family. {ECO:0000305}.
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DR EMBL; K02248; AAA42161.1; -; Genomic_DNA.
DR EMBL; V01271; CAA24579.1; -; mRNA.
DR EMBL; J00787; AAA42164.1; -; Genomic_DNA.
DR EMBL; M25890; AAA42167.1; -; mRNA.
DR EMBL; J00788; AAA42162.1; -; mRNA.
DR PIR; A20983; RIRTS1.
DR RefSeq; NP_036791.1; NM_012659.2.
DR AlphaFoldDB; P60042; -.
DR ELM; P60042; -.
DR STRING; 10116.ENSRNOP00000002519; -.
DR BindingDB; P60042; -.
DR iPTMnet; P60042; -.
DR PhosphoSitePlus; P60042; -.
DR PaxDb; P60042; -.
DR ABCD; P60042; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000002519; ENSRNOP00000002519; ENSRNOG00000001837.
DR GeneID; 24797; -.
DR KEGG; rno:24797; -.
DR UCSC; RGD:3761; rat.
DR CTD; 6750; -.
DR RGD; 3761; Sst.
DR eggNOG; ENOG502S11K; Eukaryota.
DR GeneTree; ENSGT00510000047914; -.
DR HOGENOM; CLU_124515_1_1_1; -.
DR InParanoid; P60042; -.
DR OMA; PDEMRME; -.
DR OrthoDB; 1561305at2759; -.
DR PhylomeDB; P60042; -.
DR TreeFam; TF333185; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P60042; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001837; Expressed in stomach and 10 other tissues.
DR Genevisible; P60042; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005179; F:hormone activity; TAS:RGD.
DR GO; GO:0006972; P:hyperosmotic response; IEP:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0010447; P:response to acidic pH; IEP:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR InterPro; IPR004250; Somatostatin.
DR InterPro; IPR018142; Somatostatin/Cortistatin_C.
DR PANTHER; PTHR10558; PTHR10558; 1.
DR Pfam; PF03002; Somatostatin; 1.
DR PIRSF; PIRSF001814; Somatostatin; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2891188"
FT PEPTIDE 25..34
FT /note="Antrin"
FT /id="PRO_0000033099"
FT PEPTIDE 31..43
FT /note="Neuronostatin"
FT /evidence="ECO:0000269|PubMed:18753129"
FT /id="PRO_0000447379"
FT PROPEP 35..88
FT /id="PRO_0000033100"
FT PEPTIDE 89..116
FT /note="Somatostatin-28"
FT /id="PRO_0000033101"
FT PEPTIDE 103..116
FT /note="Somatostatin-14"
FT /id="PRO_0000033102"
FT MOD_RES 43
FT /note="Threonine amide"
FT /evidence="ECO:0000305|PubMed:21325646"
FT DISULFID 105..116
FT CONFLICT 43
FT /note="T -> Y (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="Q -> H (in Ref. 5; AAA42162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 12746 MW; D48B5454C4490375 CRC64;
MLSCRLQCAL AALCIVLALG GVTGAPSDPR LRQFLQKSLA AATGKQELAK YFLAELLSEP
NQTENDALEP EDLPQAAEQD EMRLELQRSA NSNPAMAPRE RKAGCKNFFW KTFTSC
