BR2_PELPV
ID BR2_PELPV Reviewed; 33 AA.
AC P32424;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Brevinin-2;
OS Pelophylax porosus brevipodus (Nagoya Daruma pond frog) (Rana brevipoda
OS porosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=88447;
RN [1]
RP PROTEIN SEQUENCE, AND DISULFIDE BOND.
RC TISSUE=Skin secretion;
RX 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 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 PIR; JC1356; JC1356.
DR AlphaFoldDB; P32424; -.
DR SMR; P32424; -.
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..33
FT /note="Brevinin-2"
FT /id="PRO_0000044646"
FT DISULFID 27..33
FT /evidence="ECO:0000269|PubMed:1449472"
SQ SEQUENCE 33 AA; 3254 MW; BCD5D32E27DBCB96 CRC64;
GLLDSLKGFA ATAGKGVLQS LLSTASCKLA KTC