ID   SMS1_ICTPU              Reviewed;         114 AA.
AC   P01171;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Somatostatin-1;
DE   AltName: Full=Somatostatin I;
DE   Contains:
DE     RecName: Full=Somatostatin-14;
DE              Short=SS-14;
DE   Flags: Precursor;
GN   Name=sst1;
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2863931; DOI=10.1007/978-1-4615-7886-4_2;
RA   Dixon J.E., Andrews P.C.;
RT   "Somatostatins of the channel catfish.";
RL   Adv. Exp. Med. Biol. 188:19-29(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6179939; DOI=10.1016/s0021-9258(18)34029-8;
RA   Minth C.D., Taylor W.L., Magazin M.D., Tavianini M.A., Collier K.J.,
RA   Weith H.L., Dixon J.E.;
RT   "The structure of cloned DNA complementary to catfish pancreatic
RT   somatostatin-14 messenger RNA.";
RL   J. Biol. Chem. 257:10372-10377(1982).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 82-114.
RX   PubMed=6171821; DOI=10.1073/pnas.78.11.6694;
RA   Taylor W.L., Collier K.J., Deschenes R.J., Weith H.L., Dixon J.E.;
RT   "Sequence analysis of a cDNA coding for a pancreatic precursor to
RT   somatostatin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:6694-6698(1981).
RN   [4]
RP   PROTEIN SEQUENCE OF 101-114.
RX   PubMed=6114953; DOI=10.1016/s0021-9258(19)68835-6;
RA   Andrews P.C., Dixon J.E.;
RT   "Isolation and structure of a peptide hormone predicted from a mRNA
RT   sequence. A second somatostatin from the catfish pancreas.";
RL   J. Biol. Chem. 256:8267-8270(1981).
CC   -!- FUNCTION: Somatostatin inhibits the release of somatotropin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- SIMILARITY: Belongs to the somatostatin family. {ECO:0000305}.
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DR   EMBL; M25903; AAA49339.1; -; mRNA.
DR   EMBL; V00607; CAA23877.1; -; mRNA.
DR   EMBL; V00608; CAA23878.1; -; mRNA.
DR   PIR; I50798; I50798.
DR   PIR; S00292; RIIDS1.
DR   RefSeq; NP_001187259.1; NM_001200330.1.
DR   AlphaFoldDB; P01171; -.
DR   STRING; 7998.ENSIPUP00000002230; -.
DR   GeneID; 100381214; -.
DR   KEGG; ipu:100381214; -.
DR   CTD; 326018; -.
DR   OrthoDB; 1561305at2759; -.
DR   Proteomes; UP000221080; Chromosome 17.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hormone; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000305"
FT   PROPEP          25..98
FT                   /id="PRO_0000033124"
FT   PEPTIDE         101..114
FT                   /note="Somatostatin-14"
FT                   /evidence="ECO:0000269|PubMed:6114953"
FT                   /id="PRO_0000033125"
FT   DISULFID        103..114
FT                   /evidence="ECO:0000269|PubMed:6171821"
FT   CONFLICT        62
FT                   /note="E -> Q (in Ref. 2; CAA23877)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   114 AA;  12419 MW;  FEE0F2C76F74D99F CRC64;
     MPSTRIQCAL ALLAVALSVC SVSGAPSDAK LRQFLQRSIL APSVKQELTR YTLAELLAEL
     AEAENEVLDS DEVSRAAESE GARLEMERAA GPMLAPRERK AGCKNFFWKT FTSC