ID   DMS3_PHAJA              Reviewed;          26 AA.
AC   P86637;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Dermaseptin-J3 {ECO:0000303|PubMed:20932854};
DE            Short=DRS-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] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT VAL-26.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:20932854};
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: Has antimicrobial activity. {ECO:0000250|UniProtKB:P84926}.
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=2608.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20932854};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P86637; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR022731; Dermaseptin.
DR   Pfam; PF12121; DD_K; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..26
FT                   /note="Dermaseptin-J3"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT                   /id="PRO_0000404612"
FT   MOD_RES         26
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          2
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          4
FT                   /note="K or Q"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          7
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          10
FT                   /note="I or L"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          12
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          16
FT                   /note="Q or K"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          19
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          23
FT                   /note="K or Q"
FT                   /evidence="ECO:0000269|PubMed:20932854"
FT   UNSURE          25
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:20932854"
SQ   SEQUENCE   26 AA;  2611 MW;  FDCBADD96D1B6A23 CRC64;
     ALWKNMLSGI GKLAGQAALG AVKTLV