ID   BR1PB_LITPI             Reviewed;          69 AA.
AC   Q8QFQ5; P82842;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Brevinin-1Pb;
DE   Flags: Precursor;
OS   Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=12413397; DOI=10.1042/bj20021343;
RA   Chen T., Farragher S.M., Bjourson A.J., Orr D.F., Rao P., Shaw C.;
RT   "Granular gland transcriptomes in stimulated amphibian skin secretions.";
RL   Biochem. J. 371:125-130(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-69, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=10651828; DOI=10.1046/j.1432-1327.2000.01074.x;
RA   Goraya J., Wang Y., Li Z., O'Flaherty M., Knoop F.C., Platz J.E.,
RA   Conlon J.M.;
RT   "Peptides with antimicrobial activity from four different families isolated
RT   from the skins of the North American frogs Rana luteiventris, Rana
RT   berlandieri and Rana pipiens.";
RL   Eur. J. Biochem. 267:894-900(2000).
CC   -!- FUNCTION: Antibacterial activity against Gram-positive bacterium
CC       S.aureus and Gram-negative bacterium E.coli. Has activity against
CC       C.albicans. {ECO:0000269|PubMed:10651828}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- MASS SPECTROMETRY: Mass=2577.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10651828};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   EMBL; AJ427746; CAD20745.1; -; mRNA.
DR   AlphaFoldDB; Q8QFQ5; -.
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.
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; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..43
FT                   /id="PRO_0000003447"
FT   PEPTIDE         46..69
FT                   /note="Brevinin-1Pb"
FT                   /id="PRO_0000003448"
FT   DISULFID        63..69
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   69 AA;  7929 MW;  31B16331997DC170 CRC64;
     MFTLNKFLLL LFFLGTINLS FCEEENAEEE RIDEPDETDV EVEKRFLPII AGIAAKVFPK
     IFCAISKKC