ID   DMS1_PHYTS              Reviewed;          29 AA.
AC   P84921;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Dermaseptin-1 {ECO:0000303|Ref.1};
DE            Short=DStar 01 {ECO:0000303|Ref.1};
OS   Phyllomedusa tarsius (Brownbelly leaf frog) (Phyllomedusa tarsia).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=306084;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT VAL-29.
RC   TISSUE=Skin secretion {ECO:0000269|Ref.1};
RA   Prates M.V., Jardim D.P., Silva L.P., Gordo M., Leite J.R.S.A.,
RA   Figueredo R.C.R., Amaral A.C., Felipe M.S.S., Bloch C. Jr.;
RT   "Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia).";
RL   Submitted (AUG-2006) to UniProtKB.
CC   -!- FUNCTION: Antimicrobial peptide, active against the Gram-positive
CC       bacterium S.aureus, the Gram-negative bacteria E.coli and P.aeruginosa,
CC       and the yeasts C.albicans and P.brasiliensis. Has hemolytic activity
CC       (40% hemolysis at 128 ug/ml). {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands. {ECO:0000269|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=2952.70; Mass_error=0.1; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P84921; -.
DR   SMR; P84921; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; 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; Cytolysis;
KW   Direct protein sequencing; Hemolysis; Secreted.
FT   PEPTIDE         1..29
FT                   /note="Dermaseptin-1"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000376033"
FT   MOD_RES         29
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   29 AA;  2954 MW;  CEA47A1A1BD88E13 CRC64;
     GLWSKIKETG KEAAKAAGKA ALNKIAEAV