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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}.
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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
 
 
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