ID   DRS3_PHYBI              Reviewed;          74 AA.
AC   P81485;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Dermaseptin-B3 {ECO:0000303|PubMed:18644413};
DE            Short=DRS-B3 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermaseptin BIII;
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 46-73, AND MASS
RP   SPECTROMETRY.
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   -!- MASS SPECTROMETRY: Mass=2780.4; Mass_error=0.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9614066};
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=0165";
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DR   EMBL; Y16564; CAA76288.1; -; mRNA.
DR   PIR; T10456; T10456.
DR   AlphaFoldDB; P81485; -.
DR   SMR; P81485; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR022731; Dermaseptin.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF12121; DD_K; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   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                   /id="PRO_0000007095"
FT   PEPTIDE         46..74
FT                   /note="Dermaseptin-B3"
FT                   /id="PRO_0000007096"
SQ   SEQUENCE   74 AA;  8255 MW;  F9D5902A24F32C8D CRC64;
     MAFLKKSVFL VLFLGLVSLS ICEEEKREEE NEEKQEDDEQ SEEKRALWKN MLKGIGKLAG
     QAALGAVKTL VGAE