ID   HLP1_BOAPU              Reviewed;          14 AA.
AC   P84292;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Hylaseptin-P1;
DE            Short=HSP1;
OS   Boana punctata (Polka-dot tree frog) (Hypsiboas punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Hylinae; Cophomantini;
OC   Boana.
OX   NCBI_TaxID=2499473;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   STRUCTURE BY NMR.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:14715660};
RX   PubMed=14715660; DOI=10.1074/jbc.m310838200;
RA   Prates M.V., Sforca M.L., Regis W.C.B., Leite J.R.S.A., Silva L.P.,
RA   Pertinhez T.A., Araujo A.L.T., Azevedo R.B., Spisni A., Bloch C. Jr.;
RT   "The NMR-derived solution structure of a new cationic antimicrobial peptide
RT   from the skin secretion of the anuran Hyla punctata.";
RL   J. Biol. Chem. 279:13018-13026(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT GLY-14.
RC   TISSUE=Skin secretion {ECO:0000269|Ref.2};
RA   Prates M.V.;
RT   "Bioactive peptides from the anuran Hyla punctata.";
RL   Thesis (2003), University of Brasilia, Brazil.
CC   -!- FUNCTION: Has antibacterial activity against the Gram-positive
CC       bacterium S.aureus, and the Gram-negative bacteria P.aeruginosa and
CC       E.coli. Has antifungal activity against C.albicans. No hemolytic
CC       activity has been detected. {ECO:0000269|PubMed:14715660,
CC       ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14715660,
CC       ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:14715660, ECO:0000269|Ref.2}.
CC   -!- MASS SPECTROMETRY: Mass=1311.77; Mass_error=0.03; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.2};
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DR   PDB; 6WPB; NMR; -; A=1-14.
DR   PDB; 6WPD; NMR; -; A=1-14.
DR   PDBsum; 6WPB; -.
DR   PDBsum; 6WPD; -.
DR   BMRB; P84292; -.
DR   SMR; P84292; -.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW   Antimicrobial; Direct protein sequencing; Fungicide; Secreted.
FT   PEPTIDE         1..14
FT                   /note="Hylaseptin-P1"
FT                   /id="PRO_0000043803"
FT   MOD_RES         14
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|Ref.2"
FT   HELIX           2..13
FT                   /evidence="ECO:0007829|PDB:6WPB"
SQ   SEQUENCE   14 AA;  1312 MW;  45008CD91BAAC6D3 CRC64;
     GILDAIKAIA KAAG