ID   BR2_RANBP               Reviewed;          33 AA.
AC   P32424;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2008, entry version 38.
DE   RecName: Full=Brevinin-2;
OS   Rana brevipoda porsa (Japanese frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana;
OC   Pelophylax.
OX   NCBI_TaxID=88447;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion;
RX   MEDLINE=93080555; PubMed=1449472; DOI=10.1016/0006-291X(92)91542-X;
RA   Morikawa N., Hagiwara K., Nakajima T.;
RT   "Brevinin-1 and -2, unique antimicrobial peptides from the skin of the
RT   frog, Rana brevipoda porsa.";
RL   Biochem. Biophys. Res. Commun. 189:184-190(1992).
CC   -!- FUNCTION: Shows antibacterial activity against representative
CC       Gram-negative and Gram-positive bacterial species, and a very high
CC       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.
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DR   PIR; JC1356; JC1356.
DR   HOVERGEN; P32424; -.
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-2.
FT                                /FTId=PRO_0000044646.
FT   DISULFID     27     33
SQ   SEQUENCE   33 AA;  3254 MW;  BCD5D32E27DBCB96 CRC64;
     GLLDSLKGFA ATAGKGVLQS LLSTASCKLA KTC
//