ID   B1DYB_RANDY             Reviewed;          66 AA.
AC   P0C5W7; B3VZT9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 2.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Brevinin-1DYb;
DE   AltName: Full=Brevinin-1CDYb;
DE   Flags: Precursor;
OS   Rana dybowskii (Dybovsky's frog) (Korean brown frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=71582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Skin;
RX   PubMed=19539775; DOI=10.1016/j.cbpb.2009.05.015;
RA   Jin L.-L., Li Q., Song S.-S., Feng K., Zhang D.-B., Wang Q.-Y., Chen Y.-H.;
RT   "Characterization of antimicrobial peptides isolated from the skin of the
RT   Chinese frog, Rana dybowskii.";
RL   Comp. Biochem. Physiol. 154B:174-178(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 47-66, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=17688900; DOI=10.1016/j.toxicon.2007.06.023;
RA   Conlon J.M., Kolodziejek J., Nowotny N., Leprince J., Vaudry H., Coquet L.,
RA   Jouenne T., Iwamuro S.;
RT   "Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families
RT   isolated from the skin of the Japanese brown frog, Rana dybowskii.";
RL   Toxicon 50:746-756(2007).
CC   -!- FUNCTION: Antimicrobial peptide. Has low activity against the Gram-
CC       positive bacterium S.aureus and the Gram-negative bacterium E.coli
CC       (MIC<15 uM). Has a strong hemolytic activity.
CC       {ECO:0000269|PubMed:17688900}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17688900}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:17688900, ECO:0000269|PubMed:19539775}.
CC   -!- MASS SPECTROMETRY: Mass=2236.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17688900};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   EMBL; EU827799; ACF07999.1; -; mRNA.
DR   AlphaFoldDB; P0C5W7; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR012520; Antimicrobial_frog_1.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08018; Antimicrobial_1; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Hemolysis; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..44
FT                   /id="PRO_0000391360"
FT   PEPTIDE         47..66
FT                   /note="Brevinin-1DYb"
FT                   /id="PRO_5000381473"
FT   DISULFID        60..66
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   66 AA;  7785 MW;  DED229683087C342 CRC64;
     MFTLKKSLLL LFFLGTISLS LCEEERNAEE ERRDYPEERD VEVEKRFLSL ALAALPKLFC
     LIFKKC