ID   DMS3_PITAZ              Reviewed;          69 AA.
AC   Q17UY8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Dermaseptin-H3 {ECO:0000303|PubMed:17553595};
DE   AltName: Full=Dermaseptin-like peptide 3 {ECO:0000303|PubMed:17553595};
DE            Short=DMS3 {ECO:0000303|PubMed:17553595};
DE   Flags: Precursor;
GN   Name=dpp-H3 {ECO:0000312|EMBL:CAK51561.1};
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:CAK51561.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=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: Possesses a potent antimicrobial activity against Gram-
CC       positive and Gram-negative bacteria. Probably acts by disturbing
CC       membrane functions with its amphipathic structure (By similarity).
CC       {ECO:0000250|UniProtKB:P81486}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17553595}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {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; AM269412; CAK51561.1; -; mRNA.
DR   AlphaFoldDB; Q17UY8; -.
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:0000250|UniProtKB:Q1EJP5"
FT                   /id="PRO_0000248609"
FT   PEPTIDE         46..66
FT                   /note="Dermaseptin-H3"
FT                   /id="PRO_0000248610"
FT   PROPEP          68..69
FT                   /evidence="ECO:0000250|UniProtKB:Q1EJP5"
FT                   /id="PRO_0000248611"
FT   REGION          24..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250|UniProtKB:Q1EJP5"
SQ   SEQUENCE   69 AA;  7663 MW;  A5A134ECE8D4C7D9 CRC64;
     MAFLKKSLFL VLFLGMVSLS ICEEEKRENE DEEKQEDDEQ SEMKRGLWST IKNVAAAAGK
     AALGALGEQ