ID   BR1E_PELLE              Reviewed;          71 AA.
AC   P32412;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Brevinin-1E;
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] (VARIANT 1EC).
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 48-71, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion;
RX   PubMed=8508915; DOI=10.1016/0014-5793(93)81384-c;
RA   Simmaco M., Mignogna G., Barra D., Bossa F.;
RT   "Novel antimicrobial peptides from skin secretion of the European frog Rana
RT   esculenta.";
RL   FEBS Lett. 324:159-161(1993).
CC   -!- FUNCTION: Shows antibacterial activity against representative Gram-
CC       negative and Gram-positive bacterial species, and a very high hemolytic
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   EMBL; X77831; CAA54842.1; -; mRNA.
DR   PIR; C53578; C53578.
DR   AlphaFoldDB; P32412; -.
DR   TCDB; 1.C.52.1.16; the dermaseptin (dermaseptin) family.
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; IDA:UniProtKB.
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..45
FT                   /id="PRO_0000003443"
FT   PEPTIDE         48..71
FT                   /note="Brevinin-1E"
FT                   /id="PRO_0000003444"
FT   DISULFID        65..71
FT                   /evidence="ECO:0000269|PubMed:8508915"
FT   VARIANT         60
FT                   /note="L -> F (in brevinin-1Ec)"
SQ   SEQUENCE   71 AA;  8267 MW;  10900AC2BC71BB73 CRC64;
     MFTLKKSMLL LFFLGTINLS LCEEERDADE EERRDNPDES EVEVEKRFLP LLAGLAANFL
     PKIFCKITRK C