ID   DRS4_PHYBI              Reviewed;          76 AA.
AC   P81486;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Dermaseptin-B4 {ECO:0000303|PubMed:18644413, ECO:0000303|PubMed:9614066};
DE            Short=DRS-B4 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermaseptin BIV;
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, SUBCELLULAR
RP   LOCATION, AMIDATION AT GLN-73, AND MASS 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: Potent antimicrobial peptide with potent activity against
CC       Gram-positive and Gram-negative bacteria (PubMed:9614066). Probably
CC       acts by disturbing membrane functions with its amphipathic structure
CC       (PubMed:9614066). Has an activity of stimulation of insulin release,
CC       which may protect the species from being eaten by predators by causing
CC       fatal hypoglycemia (By similarity). Has hemolytic activity (By
CC       similarity). {ECO:0000250|UniProtKB:C0HLC4,
CC       ECO:0000250|UniProtKB:P84922, ECO:0000269|PubMed:9614066}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9614066}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:9614066}.
CC   -!- MASS SPECTROMETRY: Mass=2997.15; Mass_error=0.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9614066};
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Insulin-releasing peptide from Phyllomedusa trinitatis (AC
CC       C0HLC4), and Dermaseptin-2 from P.tarsius (AC P84922). {ECO:0000305}.
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=0163";
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DR   EMBL; Y16565; CAA76289.1; -; mRNA.
DR   AlphaFoldDB; P81486; -.
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; Direct protein sequencing; Immunity;
KW   Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..43
FT                   /evidence="ECO:0000305|PubMed:9614066"
FT                   /id="PRO_0000007097"
FT   PEPTIDE         46..73
FT                   /note="Dermaseptin-B4"
FT                   /evidence="ECO:0000269|PubMed:9614066"
FT                   /id="PRO_0000007098"
FT   PROPEP          75..76
FT                   /evidence="ECO:0000305|PubMed:9614066"
FT                   /id="PRO_0000007099"
FT   MOD_RES         73
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:9614066"
SQ   SEQUENCE   76 AA;  8642 MW;  A8A0525F0709F447 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEEKRENK DEIEQEDDEQ SEEKRALWKD ILKNVGKAAG
     KAVLNTVTDM VNQGEQ