ID   DRS1_PITOR              Reviewed;          29 AA.
AC   P83637;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Dermaseptin-O1 {ECO:0000303|PubMed:18644413};
DE            Short=DRS-O1 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermaseptin-01;
DE            Short=DS 01;
OS   Pithecopus oreades (Orange-legged leaf frog) (Phyllomedusa oreades).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Pithecopus.
OX   NCBI_TaxID=239355;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AMIDATION AT LEU-29, AND SYNTHESIS.
RC   TISSUE=Skin secretion;
RX   PubMed=12379643; DOI=10.1074/jbc.m209289200;
RA   Brand G.D., Leite J.R.S.A., Silva L.P., Albuquerque S., Prates M.V.,
RA   Azevedo R.B., Carregaro V., Silva J.S., Sa V.C.L., Brandao R.A.,
RA   Bloch C. Jr.;
RT   "Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta. Anti-
RT   Trypanosoma cruzi activity without cytotoxicity to mammalian cells.";
RL   J. Biol. Chem. 277:49332-49340(2002).
RN   [2]
RP   FUNCTION, AND SYNTHESIS.
RX   PubMed=17409003; DOI=10.1016/j.cbpa.2007.02.031;
RA   Silva L.P., Leite J.R.S.A., Brand G.D., Regis W.B., Tedesco A.C.,
RA   Azevedo R.B., Freitas S.M., Bloch C. Jr.;
RT   "Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta:
RT   liposomes fusion and/or lysis investigated by fluorescence and atomic force
RT   microscopy.";
RL   Comp. Biochem. Physiol. 151A:329-335(2008).
RN   [3]
RP   FUNCTION, AND SYNTHESIS.
RX   PubMed=17442605; DOI=10.1016/j.cbpa.2007.03.016;
RA   Leite J.R.S.A., Brand G.D., Silva L.P., Kuckelhaus S.A.S., Bento W.R.C.,
RA   Araujo A.L.T., Martins G.R., Lazzari A.M., Bloch C. Jr.;
RT   "Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta:
RT   Secondary structure, antimicrobial activity, and mammalian cell toxicity.";
RL   Comp. Biochem. Physiol. 151A:336-343(2008).
RN   [4]
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: Has antibacterial activity against the Gram-positive bacteria
CC       S.aureus (MIC=5.7 uM), S.dysgalactiae (MIC=5.7 uM), Nocardia sp
CC       (MIC=22.9 uM) and S.uberis (MIC=5.7 uM), and the Gram-negative bacteria
CC       P.aeruginosa, E.coli and A.calcoaceticus. Has antiprotozoal activity
CC       against T.cruzi. Has antifungal activity against the yeasts
CC       C.tropicalis (MIC=0.37 uM), C.guilliermondii (MIC=22.9 uM), C.albicans
CC       (MIC=5.7 uM) and C.albicans ATCC 1023 (MIC=5.7 uM). Lacks hemolytic
CC       activity against human and murine erythrocytes. Does not cause
CC       morphological changes in murine liver, spleen and kidney. Decreases
CC       viability of murine peritoneal cells. Fuses to, and disrupts liposomes.
CC       {ECO:0000269|PubMed:12379643, ECO:0000269|PubMed:17409003,
CC       ECO:0000269|PubMed:17442605}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12379643}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:12379643}.
CC   -!- MASS SPECTROMETRY: Mass=2793.39; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12379643};
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Dermaseptin-H7 from Phyllomedusa hypochondrialis (AC P84600).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P83637; -.
DR   SMR; P83637; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
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..29
FT                   /note="Dermaseptin-O1"
FT                   /evidence="ECO:0000269|PubMed:12379643"
FT                   /id="PRO_0000043640"
FT   MOD_RES         29
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:12379643"
SQ   SEQUENCE   29 AA;  2795 MW;  B2B596776E2074C6 CRC64;
     GLWSTIKQKG KEAAIAAAKA AGQAALGAL