SMS2_ICTPU
ID SMS2_ICTPU Reviewed; 105 AA.
AC P01172;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Somatostatin-2;
DE AltName: Full=Somatostatin II;
DE Contains:
DE RecName: Full=Somatostatin-22;
DE Short=SS-22;
DE Flags: Precursor;
GN Name=sst2;
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=6127673; DOI=10.1073/pnas.79.17.5152;
RA Magazin M.D., Minth C.D., Funckes C.L., Deschenes R.J., Tavianini M.A.,
RA Dixon J.E.;
RT "Sequence of a cDNA encoding pancreatic preprosomatostatin-22.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:5152-5156(1982).
RN [3]
RP PROTEIN SEQUENCE OF 84-105, GLYCOSYLATION AT THR-88, AND MASS SPECTROMETRY.
RX PubMed=6149220; DOI=10.1016/s0021-9258(18)90688-5;
RA Andrews P.C., Pubols M.H., Hermodson M.A., Sheares B.T., Dixon J.E.;
RT "Structure of the 22-residue somatostatin from catfish. An O-glycosylated
RT peptide having multiple forms.";
RL J. Biol. Chem. 259:13267-13272(1984).
RN [4]
RP PROTEIN SEQUENCE OF 84-105.
RX PubMed=7358665; DOI=10.1016/s0021-9258(19)85880-5;
RA Oyama H., Bradshaw R.A., Bates O.J., Permutt A.;
RT "Amino acid sequence of catfish pancreatic somatostatin I.";
RL J. Biol. Chem. 255:2251-2254(1980).
CC -!- FUNCTION: Somatostatin inhibits the release of somatotropin.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Pancreas.
CC -!- PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is
CC modified with sialic acid residues (microheterogeneity).
CC {ECO:0000269|PubMed:6149220}.
CC -!- MASS SPECTROMETRY: Mass=2943; Mass_error=2; Method=FAB;
CC Evidence={ECO:0000269|PubMed:6149220};
CC -!- MISCELLANEOUS: Biological activity of somatostatin-22 on rat pituitary
CC cells was found to be only 0.01-0.1% of somatostatin-14 activity.
CC -!- SIMILARITY: Belongs to the somatostatin family. {ECO:0000305}.
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DR EMBL; M25904; AAA49341.1; -; mRNA.
DR EMBL; J00945; AAA49340.1; -; mRNA.
DR PIR; S00293; RIIDS2.
DR RefSeq; XP_017351534.1; XM_017496045.1.
DR AlphaFoldDB; P01172; -.
DR iPTMnet; P01172; -.
DR GeneID; 100305027; -.
DR KEGG; ipu:100305027; -.
DR CTD; 79186; -.
DR OMA; WKSRTAC; -.
DR OrthoDB; 1483326at2759; -.
DR Proteomes; UP000221080; Chromosome 20.
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 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; Glycoprotein; Hormone; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..81
FT /id="PRO_0000033126"
FT PEPTIDE 84..105
FT /note="Somatostatin-22"
FT /id="PRO_0000033127"
FT CARBOHYD 88
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:6149220"
FT DISULFID 94..105
FT /evidence="ECO:0000250|UniProtKB:P61278"
FT CONFLICT 88
FT /note="T -> R (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="R -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 105 AA; 11769 MW; E4948F90853AC57C CRC64;
MSSSPLRLAL ALMCLVSAVG VISCGRPHVV LNSALEEARN VPFGEEVPER LTLPELQWML
SNNELTPVQV EEAPRSRLEL VRRDNTVTSK PLNCMNYFWK SRTAC