ID   DRS6_PHYBI              Reviewed;          72 AA.
AC   P81490; Q98TQ1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Dermaseptin-B6 {ECO:0000303|PubMed:18644413};
DE            Short=DRS-B6 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermaseptin BVI;
DE   Flags: Precursor;
OS   Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=8393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-69, AND AMIDATION AT
RP   GLN-69.
RC   TISSUE=Skin secretion;
RX   PubMed=9614066; DOI=10.1074/jbc.273.24.14690;
RA   Charpentier S., Amiche M., Mester J., Vouille V., Le Caer J.-P.,
RA   Nicolas P., Delfour A.;
RT   "Structure, synthesis, and molecular cloning of dermaseptins B, a family of
RT   skin peptide antibiotics.";
RL   J. Biol. Chem. 273:14690-14697(1998).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=18644413; DOI=10.1016/j.peptides.2008.06.017;
RA   Amiche M., Ladram A., Nicolas P.;
RT   "A consistent nomenclature of antimicrobial peptides isolated from frogs of
RT   the subfamily Phyllomedusinae.";
RL   Peptides 29:2074-2082(2008).
CC   -!- FUNCTION: Possesses a potent antimicrobial activity against Gram-
CC       positive and Gram-negative bacteria. Probably acts by disturbing
CC       membrane functions with its amphipathic structure.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=0756";
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DR   EMBL; Y16566; CAC29431.1; -; mRNA.
DR   AlphaFoldDB; P81490; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..43
FT                   /evidence="ECO:0000305|PubMed:9614066"
FT                   /id="PRO_0000007100"
FT   PEPTIDE         46..69
FT                   /note="Dermaseptin-B6"
FT                   /evidence="ECO:0000269|PubMed:9614066"
FT                   /id="PRO_0000007101"
FT   PROPEP          71..72
FT                   /evidence="ECO:0000305|PubMed:9614066"
FT                   /id="PRO_0000007102"
FT   MOD_RES         69
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:9614066"
SQ   SEQUENCE   72 AA;  8298 MW;  D0EE62810477A6A8 CRC64;
     MAFLKKSLFL VLFLGLVSLS VCEEEKRENE DEMEQEDDEQ SEEKRALWKD ILKNAGKAAL
     NEINQLVNQG EL