SMS_BOVIN
ID SMS_BOVIN Reviewed; 116 AA.
AC P26917; Q3Y5Z2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Somatostatin;
DE Contains:
DE RecName: Full=Somatostatin-28;
DE Contains:
DE RecName: Full=Somatostatin-14;
DE Contains:
DE RecName: Full=Neuronostatin;
DE Short=NST;
DE Flags: Precursor;
GN Name=SST;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2899837; DOI=10.1210/mend-2-3-209;
RA Su C.J., White J.W., Li W.H., Luo C.C., Frazier M.L., Saunders G.F.,
RA Chan L.;
RT "Structure and evolution of somatostatin genes.";
RL Mol. Endocrinol. 2:209-216(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein;
RX PubMed=10100681; DOI=10.2527/1999.772492x;
RA Furu L.M., Kazmer G.W., Strausbaugh L., Zinn S.A.;
RT "Cloning and characterization of the bovine somatostatin gene.";
RL J. Anim. Sci. 77:492-493(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Morsci N.S., Schnabel R.D., Taylor J.F.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. This effect may be mediated by
CC binding to GPR107 and PKA activation (By similarity). May regulate
CC cardiac contractile function (By similarity). May compromise
CC cardiomyocyte viability. In the central nervous system, may impair
CC memory retention and may affect hippocampal excitability. May also have
CC anxiolytic and anorexigenic effects. May play a role in arterial
CC pressure regulation (By similarity). May inhibit basal, but not
CC ghrelin- or GnRH-stimulated secretion of GH1 or LH, but does not affect
CC the release of other pituitary hormones, including PRL, ACTH, FSH or
CC TSH. 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:P60041,
CC ECO:0000250|UniProtKB:P60042, ECO:0000250|UniProtKB:P61278}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P60042}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M31217; AAA30744.1; -; mRNA.
DR EMBL; U97077; AAB58056.1; -; Genomic_DNA.
DR EMBL; DQ156121; AAZ81422.1; -; Genomic_DNA.
DR EMBL; BC103253; AAI03254.1; -; mRNA.
DR PIR; A40929; RIBOS1.
DR RefSeq; NP_776385.1; NM_173960.1.
DR AlphaFoldDB; P26917; -.
DR STRING; 9913.ENSBTAP00000023020; -.
DR PaxDb; P26917; -.
DR GeneID; 280932; -.
DR KEGG; bta:280932; -.
DR CTD; 6750; -.
DR eggNOG; ENOG502S11K; Eukaryota.
DR InParanoid; P26917; -.
DR OrthoDB; 1561305at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0030334; P:regulation of cell migration; ISS:AgBase.
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 3: Inferred from homology;
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 PROPEP 25..88
FT /evidence="ECO:0000250"
FT /id="PRO_0000033080"
FT PEPTIDE 31..43
FT /note="Neuronostatin"
FT /evidence="ECO:0000250|UniProtKB:P61278"
FT /id="PRO_0000447373"
FT PEPTIDE 89..116
FT /note="Somatostatin-28"
FT /id="PRO_0000033081"
FT PEPTIDE 103..116
FT /note="Somatostatin-14"
FT /id="PRO_0000033082"
FT MOD_RES 43
FT /note="Alanine amide"
FT /evidence="ECO:0000250|UniProtKB:P01168"
FT DISULFID 105..116
FT /evidence="ECO:0000250"
SQ SEQUENCE 116 AA; 12689 MW; C18F17E64A371D8E CRC64;
MLSCRLQCAL AALSIVLALG GVTGAPSDPR LRQFLQKSLA AAAGKQELAK YFLAELLSEP
NQTEIDALEP EDLSQAAEQD EMRLELQRSA NSNPAMAPRE RKAGCKNFFW KTFTSC
