ID   SMS_CANLF               Reviewed;         116 AA.
AC   P49670;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gastric mucosa;
RX   PubMed=8988514; DOI=10.1016/s0167-0115(96)00126-7;
RA   Dickinson C.J., Delvalle J., Todisco A., Gantz I., Tong L., Finniss S.,
RA   Yamada T.;
RT   "Canine prosomatostatin: isolation of a cDNA, regulation of gene
RT   expression, and characterization of post-translational processing
RT   intermediates.";
RL   Regul. Pept. 67:145-152(1996).
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; L42325; AAA67099.1; -; mRNA.
DR   RefSeq; NP_001003307.1; NM_001003307.1.
DR   AlphaFoldDB; P49670; -.
DR   STRING; 9612.ENSCAFP00000020465; -.
DR   PaxDb; P49670; -.
DR   Ensembl; ENSCAFT00030035606; ENSCAFP00030031050; ENSCAFG00030019362.
DR   Ensembl; ENSCAFT00040033861; ENSCAFP00040029464; ENSCAFG00040018320.
DR   Ensembl; ENSCAFT00845040007; ENSCAFP00845031328; ENSCAFG00845022661.
DR   GeneID; 403993; -.
DR   KEGG; cfa:403993; -.
DR   CTD; 6750; -.
DR   VEuPathDB; HostDB:ENSCAFG00845022661; -.
DR   eggNOG; ENOG502S11K; Eukaryota.
DR   GeneTree; ENSGT00510000047914; -.
DR   HOGENOM; CLU_124515_1_1_1; -.
DR   InParanoid; P49670; -.
DR   OMA; PDEMRME; -.
DR   OrthoDB; 1561305at2759; -.
DR   TreeFam; TF333185; -.
DR   Reactome; R-CFA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-CFA-418594; G alpha (i) signalling events.
DR   Proteomes; UP000002254; Chromosome 34.
DR   Bgee; ENSCAFG00000013891; Expressed in pancreas and 27 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
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_0000033083"
FT   PEPTIDE         31..43
FT                   /note="Neuronostatin"
FT                   /evidence="ECO:0000250|UniProtKB:P61278"
FT                   /id="PRO_0000447374"
FT   PEPTIDE         89..116
FT                   /note="Somatostatin-28"
FT                   /id="PRO_0000033084"
FT   PEPTIDE         103..116
FT                   /note="Somatostatin-14"
FT                   /id="PRO_0000033085"
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;  12736 MW;  AB49BD231E731C9E CRC64;
     MLSCRLQCAL AALSIVLALG GVTCAPSDPR LRQFLQKSLA AAAGKQELAK YFLAELLSEP
     NQTENDALEP EDLSQAAEQD EMRLELQRSA NSNPAMAPRE RKAGCKNFFW KTFTSC