ID   SMS2_LOPAM              Reviewed;         125 AA.
AC   P01170; Q91066;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Somatostatin-2;
DE   AltName: Full=Somatostatin II;
DE   Contains:
DE     RecName: Full=[Tyr7,Gly10]-somatostatin-14;
DE   Contains:
DE     RecName: Full=[Tyr13,Gly16]-somatostatin-28;
DE   Flags: Precursor;
GN   Name=sst2;
OS   Lophius americanus (American angler) (Anglerfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Lophiiformes; Lophiidae; Lophius.
OX   NCBI_TaxID=8073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6107860; DOI=10.1038/288137a0;
RA   Hobart P.M., Crawford R., Shen L., Pictet R., Rutter W.J.;
RT   "Cloning and sequence analysis of cDNAs encoding two distinct somatostatin
RT   precursors found in the endocrine pancreas of anglerfish.";
RL   Nature 288:137-141(1980).
RN   [2]
RP   PROTEIN SEQUENCE OF 98-125, AND HYDROXYLATION.
RX   PubMed=2857489; DOI=10.1073/pnas.82.2.277;
RA   Spiess J., Noe B.D.;
RT   "Processing of an anglerfish somatostatin precursor to a hydroxylysine-
RT   containing somatostatin 28.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:277-281(1985).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, SIGNAL SEQUENCE CLEAVAGE SITE, PYROGLUTAMATE
RP   FORMATION AT GLN-25, PROTEOLYTIC PROCESSING, HYDROXYLATION AT LYS-120, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=2887572; DOI=10.1016/s0021-9258(18)45262-3;
RA   Andrews P.C., Nichols R., Dixon J.E.;
RT   "Post-translational processing of preprosomatostatin-II examined using fast
RT   atom bombardment mass spectrometry.";
RL   J. Biol. Chem. 262:12692-12699(1987).
CC   -!- FUNCTION: Somatostatin inhibits the release of somatotropin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Somatostatin II may have a different degree of activity
CC       or a different type of target cell from somatostatin I.
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; V00641; CAA23987.1; -; mRNA.
DR   PIR; B93236; RIAFS2.
DR   AlphaFoldDB; P01170; -.
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; Hydroxylation; Pyrrolidone carboxylic acid;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:2887572"
FT   PROPEP          25..97
FT                   /evidence="ECO:0000269|PubMed:2857489"
FT                   /id="PRO_0000033132"
FT   PEPTIDE         98..125
FT                   /note="[Tyr13,Gly16]-somatostatin-28"
FT                   /id="PRO_0000033133"
FT   PEPTIDE         112..125
FT                   /note="[Tyr7,Gly10]-somatostatin-14"
FT                   /id="PRO_0000033134"
FT   REGION          82..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2887572"
FT   MOD_RES         120
FT                   /note="5-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:2887572"
FT   DISULFID        114..125
FT                   /evidence="ECO:0000269|PubMed:2887572"
FT   CONFLICT        77..78
FT                   /note="DV -> TG (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        90
FT                   /note="G -> E (in Ref. 1; CAA23987)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   125 AA;  14052 MW;  5E14605D7B9A46FE CRC64;
     MQCIRCPAIL ALLALVLCGP SVSSQLDREQ SDNQDLDLEL RQHWLLERAR SAGLLSQEWS
     KRAVEELLAQ MSLPEADVQR EAEDASMATG GRMNLERSVD STNNLPPRER KAGCKNFYWK
     GFTSC