ID   BR2EF_PELLE             Reviewed;          74 AA.
AC   P40842;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Brevinin-2Ef {ECO:0000303|PubMed:8163497};
DE   Flags: Precursor;
OS   Pelophylax lessonae (Pool frog) (Rana lessonae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=45623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=8163497; DOI=10.1016/s0021-9258(17)32666-2;
RA   Simmaco M., Mignogna G., Barra D., Bossa F.;
RT   "Antimicrobial peptides from skin secretions of Rana esculenta. Molecular
RT   cloning of cDNAs encoding esculentin and brevinins and isolation of new
RT   active peptides.";
RL   J. Biol. Chem. 269:11956-11961(1994).
CC   -!- FUNCTION: Shows antibacterial activity against representative Gram-
CC       negative and Gram-positive bacterial species, and hemolytic activity.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:8163497}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:8163497}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   EMBL; X77832; CAA54843.1; -; mRNA.
DR   PIR; B53578; B53578.
DR   AlphaFoldDB; P40842; -.
DR   SMR; P40842; -.
DR   TCDB; 1.C.52.1.2; the dermaseptin (dermaseptin) family.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR012521; Antimicrobial_frog_2.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08023; Antimicrobial_2; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   3: Inferred from homology;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Disulfide bond; Hemolysis;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..41
FT                   /evidence="ECO:0000305|PubMed:8163497"
FT                   /id="PRO_0000003445"
FT   PEPTIDE         42..74
FT                   /note="Brevinin-2Ef"
FT                   /evidence="ECO:0000305|PubMed:8163497"
FT                   /id="PRO_0000003446"
FT   DISULFID        68..74
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  8134 MW;  48044D3F01E6D78D CRC64;
     MFTMKKSLLL IFFLGTISLS LCQEERNADD DDGEMTEEEK RGIMDTLKNL AKTAGKGALQ
     SLVKMASCKL SGQC