ID   PLS4_PITAZ              Reviewed;          57 AA.
AC   Q17UY9;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Phylloseptin-Az4 {ECO:0000305};
DE            Short=PLS-Az4 {ECO:0000305};
DE   AltName: Full=Phylloseptin-12 {ECO:0000303|PubMed:17553595, ECO:0000312|EMBL:CAK51560.1};
DE            Short=PS-12 {ECO:0000303|PubMed:17553595};
DE   Flags: Precursor; Fragment;
GN   Name=psn12; Synonyms=ppp-12, psn-12;
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:CAK51560.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 38-56, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION
RP   AT LEU-56.
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-positive
CC       bacterium M.luteus ATCC 49732 (MIC=1.3 uM). Does not inhibit the growth
CC       of the fungus C.albicans. {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=1941.19; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17553595};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Phylloseptin subfamily. {ECO:0000255}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=00977";
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DR   EMBL; AM269411; CAK51560.1; -; mRNA.
DR   AlphaFoldDB; Q17UY9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 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..13
FT                   /evidence="ECO:0000255"
FT   PROPEP          14..35
FT                   /evidence="ECO:0000269|PubMed:17553595"
FT                   /id="PRO_0000248618"
FT   PEPTIDE         38..56
FT                   /note="Phylloseptin-Az4"
FT                   /id="PRO_0000248619"
FT   REGION          16..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:17553595"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:CAK51560.1"
SQ   SEQUENCE   57 AA;  6381 MW;  CCDCE6335D0275DF CRC64;
     LVLFLGLVSL SICEEEKRET EEEENDQEED DKSEEKRFLS LLPSIVSGAV SLAKKLG