ID   DRS4_AGADC              Reviewed;          32 AA.
AC   P0DTD5;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Dermaseptin-DA4 {ECO:0000303|PubMed:19843179};
DE            Short=DRS-DA4 {ECO:0000303|PubMed:19843179};
OS   Agalychnis dacnicolor (Giant mexican leaf frog) (Pachymedusa dacnicolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=75988;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19843179; DOI=10.1111/j.1742-4658.2009.07392.x;
RA   Auvynet C., Joanne P., Bourdais J., Nicolas P., Lacombe C., Rosenstein Y.;
RT   "Dermaseptin DA4, although closely related to dermaseptin B2, presents
RT   chemotactic and Gram-negative selective bactericidal activities.";
RL   FEBS J. 276:6773-6786(2009).
CC   -!- FUNCTION: Antimicrobial peptide with activity against Gram-negative
CC       bacteria, but not against Gram-positive bacteria (PubMed:19843179).
CC       Active against E.coli (MIC=5 uM), and P.aeruginosa (MIC=40 uM)
CC       (PubMed:19843179). Acts by disrupting cell membranes (PubMed:19843179).
CC       Is able to depolarize membranes of Gram-positive and Gram-negative
CC       bacteria (PubMed:19843179). Also acts as a potent chemoattractant for
CC       human leukocytes and activates them mainly through a GPCR, possibly
CC       FPRL1 coupled to the ERK1/2 MAPK pathway (PubMed:19843179). Is
CC       unstructured in water but become helical upon binding to anionic lipids
CC       (PubMed:19843179). In contrast to most dermaseptins, is not structured
CC       in the presence of zwitterionic lipids (PubMed:19843179). Does not show
CC       hemolytic activity (PubMed:19843179). {ECO:0000269|PubMed:19843179}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19843179}. Target
CC       cell membrane {ECO:0000269|PubMed:19843179}. Note=Forms a helical
CC       membrane channel in the prey. {ECO:0000305|PubMed:19843179}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:19843179}.
CC   -!- MASS SPECTROMETRY: Mass=3063.26; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19843179};
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=1546";
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DR   AlphaFoldDB; P0DTD5; -.
DR   SMR; P0DTD5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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   Pfam; PF12121; DD_K; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial; Chemotaxis;
KW   Direct protein sequencing; Immunity; Innate immunity; Membrane; Secreted;
KW   Target cell membrane; Target membrane.
FT   PEPTIDE         1..32
FT                   /note="Dermaseptin-DA4"
FT                   /evidence="ECO:0000269|PubMed:19843179"
FT                   /id="PRO_0000449600"
SQ   SEQUENCE   32 AA;  3060 MW;  9D2BCCB83209B38B CRC64;
     GMWSKIKNAG KAAKAAAKAA GKAALGAVSE AM