ID   DMS4_PITAZ              Reviewed;          73 AA.
AC   Q1EJP5;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Dermaseptin-H4 {ECO:0000303|PubMed:17553595};
DE   AltName: Full=Dermaseptin-like peptide 4 {ECO:0000303|PubMed:17553595};
DE            Short=DMS4 {ECO:0000303|PubMed:17553595};
DE   Flags: Precursor;
GN   Name=dpp-H4 {ECO:0000312|EMBL:CAK50802.1};
OS   Pithecopus azureus (Orange-legged monkey tree frog) (Phyllomedusa azurea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Pithecopus.
OX   NCBI_TaxID=2034991;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAK50802.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-70, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION
RP   AT LEU-70.
RC   TISSUE=Skin, and Skin secretion {ECO:0000269|PubMed:17553595};
RX   PubMed=17553595; DOI=10.1016/j.peptides.2007.05.001;
RA   Thompson A.H., Bjourson A.J., Orr D.F., Shaw C., McClean S.;
RT   "A combined mass spectrometric and cDNA sequencing approach to the
RT   isolation and characterization of novel antimicrobial peptides from the
RT   skin secretions of Phyllomedusa hypochondrialis azurea.";
RL   Peptides 28:1331-1343(2007).
CC   -!- FUNCTION: Has antibacterial activity against the Gram-negative bacteria
CC       E.coli ATCC 11775 (MIC=0.8 uM), and the Gram-positive bacteria S.aureus
CC       ATCC 12600 (MIC=0.4 uM) and M.luteus ATCC 49732 (MIC=0.8 uM). Does not
CC       inhibit the growth of the fungus C.albicans. Probably acts by
CC       disturbing membrane functions with its amphipathic structure.
CC       {ECO:0000250|UniProtKB:P81486, ECO:0000269|PubMed:17553595}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17553595}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:17553595}.
CC   -!- MASS SPECTROMETRY: Mass=2408.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17553595};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000255}.
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DR   EMBL; AM268432; CAK50802.1; -; mRNA.
DR   AlphaFoldDB; Q1EJP5; -.
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   Amidation; 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                   /evidence="ECO:0000255, ECO:0000269|PubMed:17553595"
FT                   /id="PRO_0000248612"
FT   PEPTIDE         46..70
FT                   /note="Dermaseptin-H4"
FT                   /evidence="ECO:0000269|PubMed:17553595"
FT                   /id="PRO_0000248613"
FT   PROPEP          72..73
FT                   /evidence="ECO:0000269|PubMed:17553595"
FT                   /id="PRO_0000248614"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         70
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:17553595"
SQ   SEQUENCE   73 AA;  8050 MW;  639CA5CCEEA16798 CRC64;
     MAFMKKSLFL VLFLGMVSLS ICEEEKRENE DEAKQEDDEQ SEMKRGLWST IKNVGKEAAI
     AAGKAALGAL GEQ