ID   ALBO1_BOAAL             Reviewed;          18 AA.
AC   P85982;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Hylin-a1;
DE            Short=Hy-a1 {ECO:0000303|PubMed:19056441};
OS   Boana albopunctata (Spotted tree frog) (Hypsiboas albopunctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Hylinae; Cophomantini;
OC   Boana.
OX   NCBI_TaxID=279985;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND AMIDATION AT LYS-18.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:19056441};
RX   PubMed=19056441; DOI=10.1016/j.peptides.2008.11.003;
RA   Castro M.S., Ferreira T.C.G., Cilli E.M., Crusca E. Jr.,
RA   Mendes-Giannini M.J.S., Sebben A., Ricart C.A.O., Sousa M.V., Fontes W.;
RT   "Hylin a1, the first cytolytic peptide isolated from the arboreal South
RT   American frog Hypsiboas albopunctatus ('spotted treefrog').";
RL   Peptides 30:291-296(2009).
CC   -!- FUNCTION: Has antibacterial activity against the Gram-positive bacteria
CC       S.aureus ATCC 25926 (MIC=8 uM), E.faecalis ATCC 29212 (MIC=16 uM), and
CC       B.subtilis ATCC 19659 (MIC=8 uM). Has a less potent antibacterial
CC       activity against the Gram-negative bacteria E.coli ATCC 25922 (MIC=32
CC       uM), and P.aeruginosa ATCC 27853 (MIC=64 uM). Has antifungal activity
CC       against C.albicans ATCC 90028 (MIC=16.7 uM), C.krusei ATCC 6258
CC       (MIC=16.7 uM), C.parapsilosis ATCC 22019 (MIC=67 uM), and C.neoformans
CC       ATCC 90012 (MIC=33.5 uM). Has hemolytic activity against human
CC       erythrocytes (HC50=18 uM). {ECO:0000269|PubMed:19056441}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1864.37; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19056441};
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DR   PDB; 2N0O; NMR; -; A=1-18.
DR   PDB; 5J6T; NMR; -; A=1-18.
DR   PDB; 5J6V; NMR; -; A=1-18.
DR   PDB; 5J6W; NMR; -; A=1-18.
DR   PDBsum; 2N0O; -.
DR   PDBsum; 5J6T; -.
DR   PDBsum; 5J6V; -.
DR   PDBsum; 5J6W; -.
DR   AlphaFoldDB; P85982; -.
DR   BMRB; P85982; -.
DR   SMR; P85982; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW   Antimicrobial; Cytolysis; Direct protein sequencing; Fungicide; Hemolysis;
KW   Secreted.
FT   PEPTIDE         1..18
FT                   /note="Hylin-a1"
FT                   /id="PRO_0000371455"
FT   MOD_RES         18
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:19056441"
FT   HELIX           2..17
FT                   /evidence="ECO:0007829|PDB:2N0O"
SQ   SEQUENCE   18 AA;  1865 MW;  9832F0ED0D11508A CRC64;
     IFGAILPLAL GALKNLIK