ID   BR2ED_RANES             Reviewed;          29 AA.
AC   P40840;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 40.
DE   RecName: Full=Brevinin-2Ed;
OS   Rana esculenta (Edible frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana;
OC   Pelophylax.
OX   NCBI_TaxID=8401;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion;
RX   MEDLINE=94216303; PubMed=8163497;
RA   Simmaco M., Mignogna G., Barra D., Bossa F.;
RT   "Antimicrobial peptides from skin secretions of Rana esculenta.
RT   Molecular cloning of cDNAs encoding esculentin and brevinins and
RT   isolation of new active peptides.";
RL   J. Biol. Chem. 269:11956-11961(1994).
CC   -!- FUNCTION: Shows antibacterial activity against representative
CC       Gram-negative and Gram-positive bacterial species, and 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.
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DR   PIR; D55998; D55998.
DR   HOVERGEN; P40840; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0019836; P:hemolysis by symbiont of host red blood cells; IEA:UniProtKB-KW.
DR   InterPro; IPR012521; Antimicrobial_2.
DR   Pfam; PF08023; Antimicrobial_2; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Hemolysis; Secreted.
FT   PEPTIDE       1     29       Brevinin-2Ed.
FT                                /FTId=PRO_0000043537.
FT   DISULFID     23     29
SQ   SEQUENCE   29 AA;  3002 MW;  33299AFDA6CE8612 CRC64;
     GILDSLKNLA KNAGQILLNK ASCKLSGQC
//