ID   BR1E_PELRI              Reviewed;          24 AA.
AC   P86149;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Brevinin-1E {ECO:0000303|PubMed:18855342};
OS   Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=8406;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:18280749};
RX   PubMed=18280749; DOI=10.1016/j.jasms.2007.12.010;
RA   Samgina T.Y., Artemenko K.A., Gorshkov V.A., Poljakov N.B., Lebedev A.T.;
RT   "Oxidation versus carboxamidomethylation of S-S bond in ranid frog
RT   peptides: pro and contra for de novo MALDI-MS sequencing.";
RL   J. Am. Soc. Mass Spectrom. 19:479-487(2008).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:18855342};
RX   PubMed=18855342; DOI=10.1002/rcm.3759;
RA   Samgina T.Y., Artemenko K.A., Gorshkov V.A., Ogourtsov S.V., Zubarev R.A.,
RA   Lebedev A.T.;
RT   "De novo sequencing of peptides secreted by the skin glands of the
RT   caucasian green frog Rana ridibunda.";
RL   Rapid Commun. Mass Spectrom. 22:3517-3525(2008).
CC   -!- FUNCTION: Shows antibacterial activity against representative Gram-
CC       negative and Gram-positive bacterial species, and hemolytic activity.
CC       {ECO:0000250|UniProtKB:P32412}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18280749,
CC       ECO:0000269|PubMed:18855342}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:18280749, ECO:0000269|PubMed:18855342}.
CC   -!- MASS SPECTROMETRY: Mass=2673; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18280749, ECO:0000269|PubMed:18855342};
CC   -!- MASS SPECTROMETRY: Mass=2676.75; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18280749, ECO:0000269|PubMed:18855342};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P86149; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; 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   Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Hemolysis; Secreted.
FT   PEPTIDE         1..24
FT                   /note="Brevinin-1E"
FT                   /evidence="ECO:0000269|PubMed:18280749,
FT                   ECO:0000269|PubMed:18855342"
FT                   /id="PRO_0000361057"
FT   DISULFID        18..24
FT                   /evidence="ECO:0000269|PubMed:18280749,
FT                   ECO:0000269|PubMed:18855342"
SQ   SEQUENCE   24 AA;  2678 MW;  CA892D77EF90CCF4 CRC64;
     FLPLLAGLAA NFLPKIFCKI TRKC