ID   DRS8_PHYSA              Reviewed;          79 AA.
AC   Q7T3K7;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Dermaseptin-S8 {ECO:0000303|PubMed:18644413};
DE            Short=DRS-S8 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermaseptin DS VIII {ECO:0000303|PubMed:14599725};
DE   Flags: Precursor;
OS   Phyllomedusa sauvagei (Sauvage's leaf frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=8395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-76, AMIDATION AT GLN-76,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin;
RX   PubMed=14599725; DOI=10.1016/j.regpep.2003.08.001;
RA   Chen T., Tang L., Shaw C.;
RT   "Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-
RT   sVIII) by cloning from a skin secretion-derived cDNA library.";
RL   Regul. Pept. 116:139-146(2003).
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: Potent antimicrobial peptide with activity against bacteria,
CC       fungi and protozoa. Probably acts by disturbing membrane functions with
CC       its amphipathic structure. {ECO:0000250|UniProtKB:P24302}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14599725}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:14599725}.
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=0935";
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DR   EMBL; AJ564793; CAD92231.1; -; mRNA.
DR   AlphaFoldDB; Q7T3K7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; 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   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Coiled coil; Direct protein sequencing;
KW   Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000269|PubMed:14599725"
FT                   /id="PRO_0000449587"
FT   CHAIN           46..76
FT                   /note="Dermaseptin-S8"
FT                   /evidence="ECO:0000269|PubMed:14599725"
FT                   /id="PRO_5004291442"
FT   PROPEP          78..79
FT                   /evidence="ECO:0000269|PubMed:14599725"
FT                   /id="PRO_0000449588"
FT   MOD_RES         76
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:14599725"
SQ   SEQUENCE   79 AA;  8750 MW;  F8ADE66A144F8004 CRC64;
     MDILKKSLFL VLFLGLVSLS ICEEEKRENE DEEKQEDDEQ SEMKRALWKT MLKKLGTVAL
     HAGKAALGAA ADTISQGAQ