ID   PLS6_PHYSA              Reviewed;          66 AA.
AC   U3UBT3;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Phylloseptin-S6 {ECO:0000303|PubMed:23967105};
DE            Short=PLS-S6 {ECO:0000303|PubMed:23967105};
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].
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 (By similarity). Acts by causing
CC       bacterial membrane disruption inducing leakage of the intracellular
CC       content followed by cell death (By similarity). It adopts an alpha-
CC       helical amphipathic structure in membrane environments (By similarity).
CC       Also shows highly potent antiparasitic activity against Leishmania
CC       species (By similarity). Shows moderate hemolytic activity on human
CC       erythrocytes (By similarity). Is also active on human monocytes (By
CC       similarity). {ECO:0000250|UniProtKB:F7UI84}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23967105}. Target
CC       cell membrane {ECO:0000250|UniProtKB:F7UI84}. Note=Forms a helical
CC       membrane channel in the target. {ECO:0000250|UniProtKB:F7UI84}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:23967105}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Phylloseptin subfamily. {ECO:0000305}.
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DR   EMBL; HE974361; CCK33668.1; -; mRNA.
DR   AlphaFoldDB; U3UBT3; -.
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.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   3: Inferred from homology;
KW   Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW   Immunity; Innate immunity; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000250|UniProtKB:F7UI84"
FT                   /id="PRO_0000449581"
FT   PEPTIDE         47..65
FT                   /note="Phylloseptin-S6"
FT                   /evidence="ECO:0000250|UniProtKB:F7UI84"
FT                   /id="PRO_5004648567"
FT   REGION          25..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         65
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250|UniProtKB:F7UI84"
SQ   SEQUENCE   66 AA;  7530 MW;  B244894818345AD6 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEEKRETE EEEHDQEEDD KSEEKRFLSL IPHIVSGVAS
     IAKHLG