ID   PTC1_PHYSA              Reviewed;          70 AA.
AC   Q1EN14;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Plasticin-S1 {ECO:0000303|PubMed:18644413};
DE            Short=PTC-S1 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermaseptin-S10 {ECO:0000303|PubMed:16401077};
DE            Short=DRS-S10 {ECO:0000303|PubMed:16401077};
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;
RX   PubMed=16401077; DOI=10.1021/bi051711i;
RA   Lequin O., Ladram A., Chabbert L., Bruston F., Convert O., Vanhoye D.,
RA   Chassaing G., Nicolas P., Amiche M.;
RT   "Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic
RT   core and cationic termini.";
RL   Biochemistry 45:468-480(2006).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=18644413; DOI=10.1016/j.peptides.2008.06.017;
RA   Amiche M., Ladram A., Nicolas P.;
RT   "A consistent nomenclature of antimicrobial peptides isolated from frogs of
RT   the subfamily Phyllomedusinae.";
RL   Peptides 29:2074-2082(2008).
CC   -!- FUNCTION: The native peptide is a cationic amphipathic alpha-helical
CC       antimicrobial peptide with potent activity against both Gram-positive
CC       and Gram-negative bacteria (By similarity). It has weak activity
CC       against fungi and shows low hemolytic activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q800R4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16401077}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:16401077}.
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   -!- 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=0910";
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DR   EMBL; AJ972906; CAI99865.1; -; mRNA.
DR   AlphaFoldDB; Q1EN14; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Cleavage on pair of basic residues; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000305|PubMed:16401077"
FT                   /id="PRO_0000449898"
FT   PEPTIDE         46..70
FT                   /note="Plasticin-S1"
FT                   /evidence="ECO:0000305|PubMed:16401077"
FT                   /id="PRO_5004188490"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   70 AA;  7679 MW;  4164847B96ADBFD9 CRC64;
     MAFLKKSLFL VLFLALVPLS ICEEEKREGE NEKEQEDDNQ SEEKRGLVSD LLSTVTGLLG
     NLGGGGLKKI