SMS_MOUSE
ID SMS_MOUSE Reviewed; 116 AA.
AC P60041; P01167;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Somatostatin;
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};
DE Short=NST {ECO:0000303|PubMed:24735892};
DE Flags: Precursor;
GN Name=Sst; Synonyms=Smst;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=1969620; DOI=10.1093/nar/18.5.1287;
RA Fuhrmann G., Heilig R., Kempf J., Ebel A.;
RT "Nucleotide sequence of the mouse preprosomatostatin gene.";
RL Nucleic Acids Res. 18:1287-1287(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP 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 [4]
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 [5]
RP FUNCTION (NEURONOSTATIN).
RX PubMed=25012062; DOI=10.1159/000362969;
RA Zhu X., Hu N., Chen X., Zhu M.Z., Dong H., Xu X., Luo F., Hua Y., Nair S.,
RA Samson W.K., Xiong L.;
RT "Neuronostatin attenuates myocardial contractile function through
RT inhibition of sarcoplasmic reticulum Ca2+-ATPase in murine heart.";
RL Cell. Physiol. Biochem. 33:1921-1932(2014).
RN [6]
RP FUNCTION (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:25012062). May compromise
CC cardiomyocyte viability (By similarity). In the central nervous system,
CC may impair memory retention and may affect hippocampal excitability (By
CC similarity). May also have anxiolytic and anorexigenic effects (By
CC similarity). May play a role in arterial pressure regulation (By
CC similarity). May inhibit basal, but not ghrelin- or GnRH-stimulated
CC secretion of GH1 or LH, but does not affect the release of other
CC pituitary hormones, including PRL, ACTH, FSH or TSH (By similarity).
CC Potentiates inhibitory action of somatostatin on ghrelin-stimulated
CC secretion of GH1, but not that on GnRH-stimulated secretion of LH (By
CC similarity). {ECO:0000250|UniProtKB:P60042,
CC ECO:0000250|UniProtKB:P61278, ECO:0000269|PubMed:24735892,
CC ECO:0000269|PubMed:25012062, ECO:0000269|PubMed:26561648}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P60042}.
CC -!- TISSUE SPECIFICITY: In the pancreas, somatostatin is expressed in delta
CC cells of the islets of Langerhans. In the stomach, it is expressed in
CC parietal cells of oxyntic mucosa and in the small intestine, it is
CC found in the villus (at protein level) (PubMed:18753129). Neuronostatin
CC is expressed in the pancreas in delta cells of the islets of
CC Langerhans, as well as in the stomach, in parietal cells of oxyntic
CC mucosa and in the small intestine, in the villus (at protein level)
CC (PubMed:18753129). {ECO:0000269|PubMed:18753129}.
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:0000250|UniProtKB:P60042}.
CC -!- SIMILARITY: Belongs to the somatostatin family. {ECO:0000305}.
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DR EMBL; X51468; CAA35831.1; -; Genomic_DNA.
DR EMBL; BC010770; AAH10770.1; -; mRNA.
DR CCDS; CCDS28080.1; -.
DR PIR; S08416; RIMSS1.
DR RefSeq; NP_033241.1; NM_009215.1.
DR AlphaFoldDB; P60041; -.
DR BioGRID; 203352; 1.
DR STRING; 10090.ENSMUSP00000004480; -.
DR iPTMnet; P60041; -.
DR PhosphoSitePlus; P60041; -.
DR PaxDb; P60041; -.
DR PeptideAtlas; P60041; -.
DR PRIDE; P60041; -.
DR ProteomicsDB; 257526; -.
DR ABCD; P60041; 1 sequenced antibody.
DR Antibodypedia; 3518; 543 antibodies from 41 providers.
DR DNASU; 20604; -.
DR Ensembl; ENSMUST00000004480; ENSMUSP00000004480; ENSMUSG00000004366.
DR GeneID; 20604; -.
DR KEGG; mmu:20604; -.
DR UCSC; uc007ytx.1; mouse.
DR CTD; 6750; -.
DR MGI; MGI:98326; Sst.
DR VEuPathDB; HostDB:ENSMUSG00000004366; -.
DR eggNOG; ENOG502S11K; Eukaryota.
DR GeneTree; ENSGT00510000047914; -.
DR HOGENOM; CLU_124515_1_1_1; -.
DR InParanoid; P60041; -.
DR OMA; PDEMRME; -.
DR OrthoDB; 1561305at2759; -.
DR PhylomeDB; P60041; -.
DR TreeFam; TF333185; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 20604; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Lmx1a; mouse.
DR PRO; PR:P60041; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P60041; protein.
DR Bgee; ENSMUSG00000004366; Expressed in islet of Langerhans and 116 other tissues.
DR ExpressionAtlas; P60041; baseline and differential.
DR Genevisible; P60041; MM.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006972; P:hyperosmotic response; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; Disulfide bond; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT PEPTIDE 25..34
FT /note="Antrin"
FT /id="PRO_0000033092"
FT PEPTIDE 31..43
FT /note="Neuronostatin"
FT /evidence="ECO:0000250|UniProtKB:P60042"
FT /id="PRO_0000447377"
FT PROPEP 35..88
FT /evidence="ECO:0000250"
FT /id="PRO_0000033093"
FT PEPTIDE 89..116
FT /note="Somatostatin-28"
FT /id="PRO_0000033094"
FT PEPTIDE 103..116
FT /note="Somatostatin-14"
FT /id="PRO_0000033095"
FT MOD_RES 43
FT /note="Threonine amide"
FT /evidence="ECO:0000250|UniProtKB:P60042"
FT DISULFID 105..116
FT /evidence="ECO:0000250"
SQ SEQUENCE 116 AA; 12746 MW; D48B5454C4490375 CRC64;
MLSCRLQCAL AALCIVLALG GVTGAPSDPR LRQFLQKSLA AATGKQELAK YFLAELLSEP
NQTENDALEP EDLPQAAEQD EMRLELQRSA NSNPAMAPRE RKAGCKNFFW KTFTSC
