B2DYB_RANDY
ID B2DYB_RANDY Reviewed; 33 AA.
AC P0C5X2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Brevinin-2DYb;
OS Rana dybowskii (Dybovsky's frog) (Korean brown frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX NCBI_TaxID=71582;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion;
RX PubMed=17688900; DOI=10.1016/j.toxicon.2007.06.023;
RA Conlon J.M., Kolodziejek J., Nowotny N., Leprince J., Vaudry H., Coquet L.,
RA Jouenne T., Iwamuro S.;
RT "Cytolytic peptides belonging to the brevinin-1 and brevinin-2 families
RT isolated from the skin of the Japanese brown frog, Rana dybowskii.";
RL Toxicon 50:746-756(2007).
CC -!- FUNCTION: Antimicrobial peptide. Active against the Gram-positive
CC bacterium S.aureus (MIC=30 uM) and the Gram-negative bacterium E.coli
CC (MIC=30 uM). {ECO:0000269|PubMed:17688900}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- MASS SPECTROMETRY: Mass=3286.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17688900};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C5X2; -.
DR SMR; P0C5X2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; 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;
KW Direct protein sequencing; Disulfide bond; Secreted.
FT PEPTIDE 1..33
FT /note="Brevinin-2DYb"
FT /id="PRO_0000311600"
FT DISULFID 27..33
FT /evidence="ECO:0000250"
SQ SEQUENCE 33 AA; 3290 MW; DCB25A53E32E5015 CRC64;
GLFDVVKGVL KGAGKNVAGS LLEQLKCKLS GGC