ID   DRT3_PHAJA              Reviewed;          32 AA.
AC   P86623;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Dermatoxin-J3 {ECO:0000303|PubMed:20932854};
DE            Short=DRT-J3 {ECO:0000303|PubMed:20932854};
OS   Phasmahyla jandaia (Jandaia leaf frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phasmahyla.
OX   NCBI_TaxID=762504;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT GLN-32.
RC   TISSUE=Skin secretion;
RX   PubMed=20932854; DOI=10.1016/j.toxicon.2010.09.010;
RA   Rates B., Silva L.P., Ireno I.C., Leite F.S., Borges M.H., Bloch C. Jr.,
RA   De Lima M.E., Pimenta A.M.;
RT   "Peptidomic dissection of the skin secretion of Phasmahyla jandaia
RT   (Bokermann and Sazima, 1978) (Anura, Hylidae, Phyllomedusinae).";
RL   Toxicon 57:35-52(2011).
CC   -!- FUNCTION: Antimicrobial peptide. {ECO:0000250|UniProtKB:P84928}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20932854}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:20932854}.
CC   -!- MASS SPECTROMETRY: Mass=3126.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20932854};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermatoxin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P86623; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..32
FT                   /note="Dermatoxin-J3"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT                   /id="PRO_0000404609"
FT   MOD_RES         32
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          2
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          6
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          7
FT                   /note="K or Q"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          11
FT                   /note="K or Q"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          13
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          18
FT                   /note="K or Q"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          23
FT                   /note="Q or K"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          27
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          28
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          32
FT                   /note="Q or K"
FT                   /evidence="ECO:0000269|PubMed:20932854"
SQ   SEQUENCE   32 AA;  3130 MW;  A0B4EC8A8E70C0BE CRC64;
     SLGGFLKGVG KVLAGVGKVV ADQFGNLLEA GQ