ID   BR2EA_RANES             Reviewed;          33 AA.
AC   P40837;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   22-JUL-2008, entry version 37.
DE   RecName: Full=Brevinin-2Ea;
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; A55998; A55998.
DR   HOVERGEN; P40837; -.
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     33       Brevinin-2Ea.
FT                                /FTId=PRO_0000044643.
FT   DISULFID     27     33
SQ   SEQUENCE   33 AA;  3245 MW;  4C940BDE699FF616 CRC64;
     GILDTLKNLA ISAAKGAAQG LVNKASCKLS GQC
//