B1CYA_RANDY
ID B1CYA_RANDY Reviewed; 67 AA.
AC B3VZU0;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Brevinin-1CDYa {ECO:0000303|PubMed:19539775, ECO:0000312|EMBL:ACF08000.1};
DE Flags: Precursor;
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] {ECO:0000305, ECO:0000312|EMBL:ACF08000.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-67, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Skin {ECO:0000312|EMBL:ACF08000.1}, and
RC Skin secretion {ECO:0000269|PubMed:19539775};
RX PubMed=19539775; DOI=10.1016/j.cbpb.2009.05.015;
RA Jin L.-L., Li Q., Song S.-S., Feng K., Zhang D.-B., Wang Q.-Y., Chen Y.-H.;
RT "Characterization of antimicrobial peptides isolated from the skin of the
RT Chinese frog, Rana dybowskii.";
RL Comp. Biochem. Physiol. 154B:174-178(2009).
CC -!- FUNCTION: Antimicrobial peptide. Has low activity against the Gram-
CC positive bacterium S.aureus (MIC=12.5 uM) and the Gram-negative
CC bacterium E.coli (MIC=25 uM). Has weak hemolytic activity against human
CC erythrocytes. {ECO:0000269|PubMed:19539775}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19539775}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:19539775}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU827800; ACF08000.1; -; mRNA.
DR AlphaFoldDB; B3VZU0; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
DR InterPro; IPR012520; Antimicrobial_frog_1.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF08018; Antimicrobial_1; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Hemolysis; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255, ECO:0000312|EMBL:ACF08000.1"
FT PROPEP 23..45
FT /evidence="ECO:0000269|PubMed:19539775"
FT /id="PRO_0000391425"
FT PEPTIDE 48..67
FT /note="Brevinin-1CDYa"
FT /evidence="ECO:0000269|PubMed:19539775"
FT /id="PRO_5000381475"
FT DISULFID 61..67
FT /evidence="ECO:0000250|UniProtKB:P32412"
SQ SEQUENCE 67 AA; 7861 MW; F288DCE240CFF2E2 CRC64;
MFTLKKSLLL IFFLGTINLS LCEEERNADE EERRDDLEER DVEVEKRLLS LALAALPKLF
CLIFKKC