ID   PLS2_PITAZ              Reviewed;          66 AA.
AC   P85882;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Phylloseptin-Az2 {ECO:0000305};
DE            Short=PLS-Az2 {ECO:0000305};
DE   AltName: Full=Phylloseptin-7 {ECO:0000303|PubMed:17553595};
DE            Short=PS-7 {ECO:0000303|PubMed:17553595};
DE   Flags: Precursor;
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}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-65, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION
RP   AT PHE-65.
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: Has antibacterial activity against the Gram-negative bacteria
CC       E.coli ATCC 11775 (MIC=7.2 uM), and the Gram-positive bacteria S.aureus
CC       ATCC 12600 (MIC=3.6 uM) and M.luteus ATCC 49732 (MIC=1.8 uM). Does not
CC       inhibit the growth of the fungus C.albicans.
CC       {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=2047.21; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17553595};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Phylloseptin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P85882; -.
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   InterPro; IPR016322; FSAP.
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..44
FT                   /evidence="ECO:0000269|PubMed:17553595"
FT                   /id="PRO_0000372701"
FT   PEPTIDE         47..65
FT                   /note="Phylloseptin-Az2"
FT                   /evidence="ECO:0000269|PubMed:17553595"
FT                   /id="PRO_0000372702"
FT   REGION          24..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         65
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:17553595"
SQ   SEQUENCE   66 AA;  7553 MW;  F6AD0A7B3A2C53AF CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEEKRETE EKENEQEDDD KSEEKRFLSL IPHAINAVSA
     IAKHFG