ID   BR1YA_RANBO             Reviewed;          24 AA.
AC   P84111;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Brevinin-1BYa;
OS   Rana boylii (Foothill yellow-legged frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=160499;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:14531844};
RX   PubMed=14531844; DOI=10.1034/j.1399-3011.2003.00090.x;
RA   Conlon J.M., Sonnevend A., Patel M., Davidson C., Nielsen P.F., Pal T.,
RA   Rollins-Smith L.A.;
RT   "Isolation of peptides of the brevinin-1 family with potent candidacidal
RT   activity from the skin secretions of the frog Rana boylii.";
RL   J. Pept. Res. 62:207-213(2003).
CC   -!- FUNCTION: Antibacterial activity against Gram-positive bacterium
CC       S.aureus and Gram-negative bacterium E.coli. High antifungal activity
CC       against C.albicans and a strong hemolytic activity.
CC       {ECO:0000269|PubMed:14531844}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14531844}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- MASS SPECTROMETRY: Mass=2605.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14531844};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000269|PubMed:14531844}.
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DR   PDB; 6G4I; NMR; -; A=1-24.
DR   PDB; 6G4K; NMR; -; A=1-24.
DR   PDB; 6G4U; NMR; -; A=1-24.
DR   PDB; 6G4V; NMR; -; A=1-24.
DR   PDB; 6G4X; NMR; -; A=1-24.
DR   PDB; 6R95; NMR; -; A=1-23.
DR   PDB; 6R96; NMR; -; A=1-23.
DR   PDBsum; 6G4I; -.
DR   PDBsum; 6G4K; -.
DR   PDBsum; 6G4U; -.
DR   PDBsum; 6G4V; -.
DR   PDBsum; 6G4X; -.
DR   PDBsum; 6R95; -.
DR   PDBsum; 6R96; -.
DR   AlphaFoldDB; P84111; -.
DR   BMRB; P84111; -.
DR   SMR; P84111; -.
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.
DR   InterPro; IPR012520; Antimicrobial_frog_1.
DR   Pfam; PF08018; Antimicrobial_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cytolysis; Direct protein sequencing; Disulfide bond; Fungicide; Hemolysis;
KW   Secreted.
FT   PEPTIDE         1..24
FT                   /note="Brevinin-1BYa"
FT                   /id="PRO_0000043532"
FT   DISULFID        18..24
FT                   /evidence="ECO:0000269|PubMed:14531844"
FT   HELIX           3..20
FT                   /evidence="ECO:0007829|PDB:6G4I"
SQ   SEQUENCE   24 AA;  2609 MW;  CEC2E08E1CB63DF4 CRC64;
     FLPILASLAA KFGPKLFCLV TKKC