BR1_PELPV
ID BR1_PELPV Reviewed; 24 AA.
AC P32423;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Brevinin-1;
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; JC1355; JC1355.
DR AlphaFoldDB; P32423; -.
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; IPR012520; Antimicrobial_frog_1.
DR Pfam; PF08018; Antimicrobial_1; 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..24
FT /note="Brevinin-1"
FT /id="PRO_0000043539"
FT DISULFID 18..24
FT /evidence="ECO:0000269|PubMed:1449472"
SQ SEQUENCE 24 AA; 2531 MW; C866285B191EFDF4 CRC64;
FLPVLAGIAA KVVPALFCKI TKKC