ID   BR1SY_LITSY             Reviewed;          24 AA.
AC   P82871;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Brevinin-1SY;
OS   Lithobates sylvaticus (Wood frog) (Rana sylvatica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=45438;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=11042268; DOI=10.1016/s0014-5793(00)02102-5;
RA   Matutte B., Storey K.B., Knoop F.C., Conlon J.M.;
RT   "Induction of synthesis of an antimicrobial peptide in the skin of the
RT   freeze-tolerant frog, Rana sylvatica, in response to environmental
RT   stimuli.";
RL   FEBS Lett. 483:135-138(2000).
CC   -!- FUNCTION: Antibacterial activity against Gram-positive bacterium
CC       S.aureus and Gram-negative bacterium E.coli.
CC       {ECO:0000269|PubMed:11042268}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- MASS SPECTROMETRY: Mass=2440.1; Mass_error=0.02; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11042268};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P82871; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR012520; Antimicrobial_frog_1.
DR   Pfam; PF08018; Antimicrobial_1; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   PEPTIDE         1..24
FT                   /note="Brevinin-1SY"
FT                   /id="PRO_0000043549"
FT   DISULFID        18..24
SQ   SEQUENCE   24 AA;  2442 MW;  0997425723E01DFD CRC64;
     FLPVVAGLAA KVLPSIICAV TKKC