ID   DRS8_PHYBI              Reviewed;          77 AA.
AC   Q90ZK5;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Dermaseptin-B8 {ECO:0000303|PubMed:18644413};
DE            Short=DRS-B8 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermaseptin-gene related 2;
DE            Short=Dermaseptin DRG2;
DE   Flags: Precursor;
GN   Name=DRG2;
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 [GENOMIC DNA].
RC   TISSUE=Skin;
RA   Amiche M.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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: Has antimicrobial activity. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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=0937";
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DR   EMBL; AJ312001; CAC37580.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90ZK5; -.
DR   SMR; Q90ZK5; -.
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   2: Evidence at transcript level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..43
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007106"
FT   PEPTIDE         45..74
FT                   /note="Dermaseptin-B8"
FT                   /id="PRO_0000007107"
FT   PROPEP          76..77
FT                   /id="PRO_0000007108"
FT   REGION          24..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         74
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   77 AA;  8418 MW;  85666BB7F7A94E55 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEEKRENE DEEEQEDDEQ SEMKRGLWSK IKEAGKAALT
     AAGKAALGAV SDAVGEQ