ID   PTC1_LEPLD              Reviewed;          25 AA.
AC   P0DTD7;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Plasticin-L1 {ECO:0000303|PubMed:19428765};
DE            Short=PTC-L1 {ECO:0000305};
OS   Leptodactylus laticeps (Santa Fe frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Leptodactylidae; Leptodactylinae;
OC   Leptodactylus.
OX   NCBI_TaxID=1615745;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SYNTHESIS, MASS SPECTROMETRY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Skin secretion;
RX   PubMed=19428765; DOI=10.1016/j.peptides.2009.01.008;
RA   Conlon J.M., Abdel-Wahab Y.H., Flatt P.R., Leprince J., Vaudry H.,
RA   Jouenne T., Condamine E.;
RT   "A glycine-leucine-rich peptide structurally related to the plasticins from
RT   skin secretions of the frog Leptodactylus laticeps (Leptodactylidae).";
RL   Peptides 30:888-892(2009).
RN   [2]
RP   STRUCTURE BY NMR IN MEMBRANE-MIMETIC ENVIRONMENT, AND FUNCTION.
RX   PubMed=24073891; DOI=10.1021/bi4008287;
RA   Scorciapino M.A., Manzo G., Rinaldi A.C., Sanna R., Casu M., Pantic J.M.,
RA   Lukic M.L., Conlon J.M.;
RT   "Conformational analysis of the frog skin peptide, plasticin-L1, and its
RT   effects on production of proinflammatory cytokines by macrophages.";
RL   Biochemistry 52:7231-7241(2013).
CC   -!- FUNCTION: May play an immunomodulatory role in frog skin in response to
CC       microbial pathogens, since it increases the production of the pro-
CC       inflammatory cytokines TNF-alpha, IL-1 beta, IL-12, and IL-23 by mouse
CC       peritoneal macrophages and has no effect on the production of the anti-
CC       inflammatory cytokine IL-10 (PubMed:24073891). It is not known whether
CC       stimulation of cytokine production arises from a non-specific
CC       interaction of the peptide with the macrophage membrane or from
CC       interaction with a specific receptor (Probable). Shows a low activity
CC       in stimulating insulin release from rat BRIN-BD11 beta cells, and acts
CC       without loss of integrity of the plasma membrane (PubMed:19428765).
CC       Shows a marked affinity for both neutral and anionic membranes models
CC       (PubMed:24073891). Does not show antibacterial (E.coli and S.aureus)
CC       (PubMed:19428765). Does not show hemolytic activity against human
CC       erythrocytes (PubMed:19428765). {ECO:0000269|PubMed:19428765,
CC       ECO:0000269|PubMed:24073891, ECO:0000305|PubMed:24073891}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19428765}. Target
CC       cell membrane {ECO:0000269|PubMed:24073891}. Note=Forms a helical
CC       membrane channel in the target. {ECO:0000305|PubMed:24073891}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:19428765}.
CC   -!- DOMAIN: Amphipathic peptide that adopts a random coil conformation in
CC       water, a beta-sheet structure in methanol, and an alpha-helical
CC       conformation in trifluoroethanol-water. {ECO:0000305|PubMed:19428765}.
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=2164; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:19428765};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Plasticin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DTD7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Direct protein sequencing; Immunity;
KW   Innate immunity; Membrane; Secreted; Target cell membrane; Target membrane.
FT   PEPTIDE         1..25
FT                   /note="Plasticin-L1"
FT                   /evidence="ECO:0000269|PubMed:19428765"
FT                   /id="PRO_0000449664"
SQ   SEQUENCE   25 AA;  2166 MW;  B35B59FFE20B0E29 CRC64;
     GLVNGLLSSV LGGGQGGGGL LGGIL