ID   DMS4_PITNO              Reviewed;          33 AA.
AC   C0HKP8;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Dermaseptin-4 {ECO:0000303|PubMed:24113627};
OS   Pithecopus nordestinus (Northeastern Brazilian leaf frog) (Phyllomedusa
OS   nordestina).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Pithecopus.
OX   NCBI_TaxID=2034992 {ECO:0000303|PubMed:24113627};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT LEU-33.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:24113627};
RX   PubMed=24113627; DOI=10.1016/j.exppara.2013.09.016;
RA   Pinto E.G., Pimenta D.C., Antoniazzi M.M., Jared C., Tempone A.G.;
RT   "Antimicrobial peptides isolated from Phyllomedusa nordestina (Amphibia)
RT   alter the permeability of plasma membrane of Leishmania and Trypanosoma
RT   cruzi.";
RL   Exp. Parasitol. 135:655-660(2013).
CC   -!- FUNCTION: Has antiparasitic activity against trypomastigote form of
CC       T.cruzi (IC(50)=0.25 uM) in vitro but not against L.infantum
CC       (PubMed:24113627). Probably acts by permeabilizing cell membranes
CC       (PubMed:24113627). In vitro, shows no cytotoxicity against macrophages
CC       (PubMed:24113627). Has antibacterial activity (By similarity).
CC       {ECO:0000250|UniProtKB:P83637, ECO:0000269|PubMed:24113627}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24113627}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:24113627}.
CC   -!- MASS SPECTROMETRY: Mass=3210.77; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:24113627};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKP8; -.
DR   SMR; C0HKP8; -.
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..33
FT                   /note="Dermaseptin-4"
FT                   /evidence="ECO:0000269|PubMed:24113627"
FT                   /id="PRO_0000441007"
FT   MOD_RES         33
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:24113627"
SQ   SEQUENCE   33 AA;  3211 MW;  353B8086C8459A47 CRC64;
     GLWSTIKQKG KEAAIAAAKA AGKAALNAAS EAL