BR2EC_PELLE
ID BR2EC_PELLE Reviewed; 34 AA.
AC P40839;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Brevinin-2Ec;
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 PROTEIN SEQUENCE, AND DISULFIDE BOND.
RC TISSUE=Skin secretion;
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.
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 PIR; C55998; C55998.
DR AlphaFoldDB; P40839; -.
DR SMR; P40839; -.
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 Pfam; PF08023; Antimicrobial_2; 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..34
FT /note="Brevinin-2Ec"
FT /id="PRO_0000044645"
FT DISULFID 28..34
FT /evidence="ECO:0000269|PubMed:8163497"
SQ SEQUENCE 34 AA; 3521 MW; EE173F0F4E5A5EFB CRC64;
GILLDKLKNF AKTAGKGVLQ SLLNTASCKL SGQC