ID   PTC_PHYTB               Reviewed;          22 AA.
AC   C0HLE0;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Plasticin-TR {ECO:0000303|PubMed:29980138};
DE            Short=PTC-TR {ECO:0000305};
OS   Phyllomedusa trinitatis (Trinidad leaf frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=332092;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SYNTHESIS, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=29980138; DOI=10.1016/j.cbd.2018.06.006;
RA   Mechkarska M., Coquet L., Leprince J., Auguste R.J., Jouenne T.,
RA   Mangoni M.L., Conlon J.M.;
RT   "Peptidomic analysis of the host-defense peptides in skin secretions of the
RT   Trinidadian leaf frog Phyllomedusa trinitatis (Phyllomedusidae).";
RL   Comp. Biochem. Physiol. 28:72-79(2018).
RN   [2]
RP   FUNCTION, SYNTHESIS, AND SUBUNIT.
RX   PubMed=30734396; DOI=10.1002/psc.3153;
RA   Pantic J., Guilhaudis L., Musale V., Attoub S., Lukic M.L., Mechkarska M.,
RA   Conlon J.M.;
RT   "Immunomodulatory, insulinotropic, and cytotoxic activities of
RT   phylloseptins and plasticin-TR from the Trinidanian leaf frog Phyllomedusa
RT   trinitatis.";
RL   J. Pept. Sci. 25:E3153-E3153(2019).
CC   -!- FUNCTION: Has no antimicrobial activity against Gram-negative bacterium
CC       E.coli ATCC 25922, Gram-positive bacterium S.epidermidis ATCC 12228 and
CC       against fungus C.albicans ATCC 24433 at concentrations up to 100 uM
CC       (PubMed:29980138). Has an anti-inflammatory effect, since it inhibits
CC       the production of the pro-inflammatory cytokines TNF-alpha and IL-1
CC       beta (PubMed:30734396). Has high activity of stimulation of insulin
CC       release, which may protect the species from being eaten by predators by
CC       causing fatal hypoglycemia (PubMed:30734396). Is not cytotoxic to
CC       cancer line cells (PubMed:30734396). Does not show hemolysis on mouse
CC       erythrocytes (PubMed:30734396). Adopts a mixture of alpha-helical and
CC       beta-sheet structures (PubMed:30734396). {ECO:0000269|PubMed:29980138,
CC       ECO:0000269|PubMed:30734396}.
CC   -!- SUBUNIT: Exhibits a propensity to self-association and forms helical
CC       oligomers in membrane-mimetic environments.
CC       {ECO:0000305|PubMed:30734396}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29980138}. Target
CC       cell membrane {ECO:0000305|PubMed:29980138}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:29980138}.
CC   -!- DOMAIN: Plasticins have huge conformational plasticity. They can
CC       display random coil, alpha-helical, beta-sheet or beta-harpin
CC       structures. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=2004.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29980138};
CC   -!- PHARMACEUTICAL: This peptide may represent a template for the design of
CC       potent anti-inflammatory agents for use in the control
CC       hyperinflammatory phase of sepsis, since it has the ability to inhibit
CC       production of TNF-alpha and IL-1 beta and to stimulate IL-10 production
CC       by peritoneal cells coupled with very low toxicity against mouse
CC       erythrocytes and A549 human lung adenocarcinoma cells.
CC       {ECO:0000305|PubMed:30734396}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Plasticin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=02995";
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DR   AlphaFoldDB; C0HLE0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Direct protein sequencing; Membrane;
KW   Pharmaceutical; Secreted; Target cell membrane; Target membrane.
FT   PEPTIDE         1..22
FT                   /note="Plasticin-TR"
FT                   /evidence="ECO:0000269|PubMed:29980138"
FT                   /id="PRO_0000445208"
SQ   SEQUENCE   22 AA;  1982 MW;  1753A69A64263BB0 CRC64;
     GLVSGLLNSV TGLLGNLAGG GL