ID   TPB_RANDY               Reviewed;          62 AA.
AC   B3VZU4;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Temporin-CDYb {ECO:0000303|PubMed:19539775, ECO:0000312|EMBL:ACF08004.1};
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:ACF08004.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Skin {ECO:0000312|EMBL:ACF08004.1};
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>100 uM) and the Gram-negative
CC       bacterium E.coli (MIC>100 uM). Has weak hemolytic activity against
CC       human erythrocytes. {ECO:0000269|PubMed:19539775}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P56918}.
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       Temporin 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; EU827804; ACF08004.1; -; mRNA.
DR   AlphaFoldDB; B3VZU4; -.
DR   GO; GO:0005576; C:extracellular region; ISS: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; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Hemolysis; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255, ECO:0000312|EMBL:ACF08004.1"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000250|UniProtKB:P56918"
FT                   /id="PRO_0000391433"
FT   PEPTIDE         48..60
FT                   /note="Temporin-CDYb"
FT                   /evidence="ECO:0000269|PubMed:19539775"
FT                   /id="PRO_5000381483"
FT   MOD_RES         60
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P56918"
SQ   SEQUENCE   62 AA;  7083 MW;  07E29AA5A32FE57E CRC64;
     MFTLKKSLLL LFFLGTINLS LCEEERDADE EERRDDPEER AVQVEKRILP ILAPLIGGLL
     GK