SMS_SHEEP
ID SMS_SHEEP Reviewed; 116 AA.
AC O46688;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Ile de France;
RX PubMed=9880082; DOI=10.1016/s0196-9781(98)00135-1;
RA Bruneau G., Tillet Y.;
RT "Localization of the preprosomatostatin-mRNA by in situ hybridization in
RT the ewe hypothalamus.";
RL Peptides 19:1749-1758(1998).
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}.
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DR EMBL; AF031488; AAC04697.1; -; mRNA.
DR EMBL; Y15267; CAA75556.1; -; mRNA.
DR PIR; A61322; A61322.
DR RefSeq; NP_001009196.1; NM_001009196.1.
DR AlphaFoldDB; O46688; -.
DR STRING; 9940.ENSOARP00000022014; -.
DR Ensembl; ENSOART00000022319; ENSOARP00000022014; ENSOARG00000020492.
DR Ensembl; ENSOART00020000280; ENSOARP00020000200; ENSOARG00020000243.
DR Ensembl; ENSOART00020000285; ENSOARP00020000206; ENSOARG00020000243.
DR Ensembl; ENSOART00020000290; ENSOARP00020000209; ENSOARG00020000243.
DR Ensembl; ENSOART00020000301; ENSOARP00020000219; ENSOARG00020000243.
DR GeneID; 443006; -.
DR KEGG; oas:443006; -.
DR CTD; 6750; -.
DR eggNOG; ENOG502S11K; Eukaryota.
DR HOGENOM; CLU_124515_1_1_1; -.
DR OMA; PDEMRME; -.
DR OrthoDB; 1561305at2759; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000020492; Expressed in pylorus and 18 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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_0000033103"
FT PEPTIDE 31..43
FT /note="Neuronostatin"
FT /evidence="ECO:0000250|UniProtKB:P61278"
FT /id="PRO_0000447380"
FT PEPTIDE 89..116
FT /note="Somatostatin-28"
FT /id="PRO_0000033104"
FT PEPTIDE 103..116
FT /note="Somatostatin-14"
FT /id="PRO_0000033105"
FT REGION 62..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; C18F17E31A3718DE CRC64;
MLSCRLQCAL AALSIVLALG GVTGAPSDPR LRQFLQKSLA AAAGKQELAK YFLAELLSEP
NQTENDALEP EDLSQAAEQD EMRLELQRSA NSNPAMAPRE RKAGCKNFFW KTFTSC
