ID   PLS1_PHYSA              Reviewed;          66 AA.
AC   F7UI84; E3PQH3;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Phylloseptin-S1 {ECO:0000303|PubMed:23967105};
DE            Short=PLS-S1 {ECO:0000303|PubMed:23967105};
DE   AltName: Full=Phylloseptin-1 {ECO:0000303|PubMed:20451254};
DE            Short=PSN-1 {ECO:0000303|PubMed:20451254};
DE   Flags: Precursor;
OS   Phyllomedusa sauvagei (Sauvage's leaf frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=8395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS OF 47-65, IDENTIFICATION BY
RP   MASS SPECTROMETRY, AND AMIDATION AT PHE-65.
RC   TISSUE=Skin secretion;
RX   PubMed=20451254; DOI=10.1016/j.molimm.2010.04.010;
RA   Zhang R., Zhou M., Wang L., McGrath S., Chen T., Chen X., Shaw C.;
RT   "Phylloseptin-1 (PSN-1) from Phyllomedusa sauvagei skin secretion: a novel
RT   broad-spectrum antimicrobial peptide with antibiofilm activity.";
RL   Mol. Immunol. 47:2030-2037(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-65, AMIDATION AT PHE-65,
RP   SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Skin secretion;
RX   PubMed=23967105; DOI=10.1371/journal.pone.0070782;
RA   Raja Z., Andre S., Piesse C., Sereno D., Nicolas P., Foulon T., Oury B.,
RA   Ladram A.;
RT   "Structure, antimicrobial activities and mode of interaction with membranes
RT   of novel [corrected] phylloseptins from the painted-belly leaf frog,
RT   Phyllomedusa sauvagii.";
RL   PLoS ONE 8:E70782-E70782(2013).
CC   -!- FUNCTION: Antimicrobial peptide with high activity against Gram-
CC       positive bacteria, low activity against Gram-negative bacteria, and
CC       moderate activity against fungi (PubMed:20451254, PubMed:23967105).
CC       Acts on bacterial biofilms (S.aureus) with the same potency than on
CC       bacteria (PubMed:20451254). Acts by causing bacterial membrane
CC       disruption inducing leakage of the intracellular content followed by
CC       cell death (PubMed:23967105). It adopts an alpha-helical amphipathic
CC       structure in membrane environments (PubMed:23967105). Also shows highly
CC       potent antiparasitic activity against Leishmania species
CC       (PubMed:23967105). Shows low hemolytic activity on horse and human
CC       erythrocytes (LC(50)=39 uM) (PubMed:20451254, PubMed:23967105). Is also
CC       active on human monocytes (IC(50)=23 uM) (PubMed:23967105).
CC       {ECO:0000269|PubMed:20451254, ECO:0000269|PubMed:23967105}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is <7. Is active against E.coli ATCC25922 at pH 5
CC         (MIC=12.5 uM), whereas is almost not active at pH 7 (MIC=70 uM).
CC         {ECO:0000269|PubMed:23967105};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23967105}. Target
CC       cell membrane {ECO:0000269|PubMed:23967105}. Note=Forms a helical
CC       membrane channel in the target. {ECO:0000305|PubMed:23967105}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:23967105}.
CC   -!- MASS SPECTROMETRY: Mass=2035.16; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23967105};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Phylloseptin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=1581";
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DR   EMBL; FN667968; CBJ56559.1; -; mRNA.
DR   EMBL; AM903077; CAP17490.1; -; mRNA.
DR   AlphaFoldDB; F7UI84; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Fungicide; Hemolysis; Immunity; Innate immunity; Membrane; Secreted;
KW   Signal; Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000305|PubMed:20451254,
FT                   ECO:0000305|PubMed:23967105"
FT                   /id="PRO_0000449585"
FT   PEPTIDE         47..65
FT                   /note="Phylloseptin-S1"
FT                   /evidence="ECO:0000269|PubMed:20451254,
FT                   ECO:0000269|PubMed:23967105"
FT                   /id="PRO_5003363395"
FT   REGION          25..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         65
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:23967105,
FT                   ECO:0000305|PubMed:20451254"
FT   CONFLICT        2..3
FT                   /note="AF -> DI (in Ref. 1; CBJ56559)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   66 AA;  7564 MW;  B24A694818345AD6 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEEKRETE EEEHDQEEDD KSEEKRFLSL IPHIVSGVAS
     IAKHFG