ID   DRT1_PHYSA              Reviewed;          77 AA.
AC   Q5DVA5;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Dermatoxin-S1 {ECO:0000305};
DE            Short=DRT-S1 {ECO:0000305};
DE   AltName: Full=Dermatoxin {ECO:0000303|PubMed:15927704};
DE   Flags: Precursor;
GN   Name=DRT-S {ECO:0000303|PubMed:15927704};
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], PROTEIN SEQUENCE OF 45-76, MASS SPECTROMETRY,
RP   AMIDATION AT GLN-76, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
RX   PubMed=15927704; DOI=10.1016/j.regpep.2005.01.017;
RA   Chen T., Walker B., Zhou M., Shaw C.;
RT   "Dermatoxin and phylloxin from the waxy monkey frog, Phyllomedusa sauvagei:
RT   cloning of precursor cDNAs and structural characterization from lyophilized
RT   skin secretion.";
RL   Regul. Pept. 129:103-108(2005).
CC   -!- FUNCTION: Antimicrobial peptide with potent activity against Gram-
CC       positive bacteria B.megaterium, C.glutamicum and S.aureus and
CC       mollicutes A.laidlawii and S.melliferum. Less active against Gram-
CC       negative bacteria B.cepacia, P.aeruginosa, S.typhimurium and
CC       S.meliloti. Probably acts by disturbing membrane functions with its
CC       amphipathic structure. {ECO:0000250|UniProtKB:Q9PT75}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15927704}. Target
CC       cell membrane {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:15927704}.
CC   -!- MASS SPECTROMETRY: Mass=2945.96; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15927704};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermatoxin subfamily. {ECO:0000305}.
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DR   EMBL; AJ865345; CAI26288.1; -; mRNA.
DR   AlphaFoldDB; Q5DVA5; -.
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: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; Direct protein sequencing; Immunity;
KW   Innate immunity; Membrane; Secreted; Signal; Target cell membrane;
KW   Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..44
FT                   /evidence="ECO:0000305|PubMed:15927704"
FT                   /id="PRO_0000449668"
FT   PEPTIDE         45..76
FT                   /note="Dermatoxin-S1"
FT                   /evidence="ECO:0000269|PubMed:15927704"
FT                   /id="PRO_5004254443"
FT   MOD_RES         76
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:15927704"
SQ   SEQUENCE   77 AA;  8361 MW;  151D206871B19FA1 CRC64;
     MAFLKKSLFL ILFLGLVPLS FCENDKREGE NEEEQDDDQS EEKRALGTLL KGVGSAVATV
     GKMVADQFGK LLQAGQG