ID   FRE22_SPHLA             Reviewed;          16 AA.
AC   P0DTV6;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Frenatin 2.2S {ECO:0000303|PubMed:24704757};
DE            Short=F2.2S {ECO:0000305};
OS   Sphaenorhynchus lacteus (Orinoco lime treefrog) (Hyla lactea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Hylinae; Dendropsophini;
OC   Sphaenorhynchus.
OX   NCBI_TaxID=279984;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   AMIDATION AT SER-16.
RC   TISSUE=Skin secretion;
RX   PubMed=24704757; DOI=10.1016/j.peptides.2014.03.020;
RA   Conlon J.M., Mechkarska M., Radosavljevic G., Attoub S., King J.D.,
RA   Lukic M.L., McClean S.;
RT   "A family of antimicrobial and immunomodulatory peptides related to the
RT   frenatins from skin secretions of the Orinoco lime frog Sphaenorhynchus
RT   lacteus (Hylidae).";
RL   Peptides 56:132-140(2014).
RN   [2]
RP   FUNCTION AS INSULINOTROPIC PEPTIDE.
RX   PubMed=30244134; DOI=10.1016/j.biochi.2018.09.008;
RA   Musale V., Guilhaudis L., Abdel-Wahab Y.H.A., Flatt P.R., Conlon J.M.;
RT   "Insulinotropic activity of the host-defense peptide frenatin 2D:
RT   conformational, structure-function and mechanistic studies.";
RL   Biochimie 156:12-21(2019).
CC   -!- FUNCTION: Antimicrobial peptide with potent activity against Gram-
CC       negative bacteria (PubMed:24704757). In vitro, is cytotoxic to non-
CC       small cell lung adenocarcinoma A549 cells (PubMed:24704757). Also,
CC       stimulates production of some pro-inflammatory cytokines (IL-1beta, and
CC       IL-23, but not TNF-alpha) by mouse peritoneal macrophages and down-
CC       regulates production of the anti-inflammatory cytokine IL-10 by
CC       lipopolysaccharide (LPS)-stimulated cells (PubMed:24704757). Very
CC       weakly stimulates insulin release (PubMed:30244134). Has a very weak
CC       activity in hemolysis (PubMed:24704757). {ECO:0000269|PubMed:24704757,
CC       ECO:0000269|PubMed:30244134}.
CC   -!- MASS SPECTROMETRY: Mass=1547.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:24704757};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Frenatin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DTV6; -.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Immunity; Innate immunity.
FT   PEPTIDE         1..16
FT                   /note="Frenatin 2.2S"
FT                   /evidence="ECO:0000269|PubMed:24704757"
FT                   /id="PRO_0000450237"
FT   MOD_RES         16
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000269|PubMed:24704757"
SQ   SEQUENCE   16 AA;  1549 MW;  3622026180E1A07A CRC64;
     GLVGTLLGHI GKAILS