ID   PLS1_AGASP              Reviewed;          68 AA.
AC   A0A5P9K461;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Phylloseptin-SP1 {ECO:0000303|PubMed:31671555};
DE            Short=PLS-SP1 {ECO:0000303|PubMed:31671555};
DE   Flags: Precursor;
OS   Agalychnis spurrelli (Gliding leaf frog) (Agalychnis litodryas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=317303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, AMIDATION AT
RP   LEU-67, SYNTHESIS OF 46-67, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
RX   PubMed=31671555; DOI=10.3390/biom9110667;
RA   Proano-Bolanos C., Blasco-Zuniga A., Almeida J.R., Wang L.,
RA   Llumiquinga M.A., Rivera M., Zhou M., Chen T., Shaw C.;
RT   "Unravelling the skin secretion peptides of the gliding leaf frog,
RT   Agalychnis spurrelli (Hylidae).";
RL   Biomolecules 9:1-20(2019).
CC   -!- FUNCTION: Weak cationic amphipathic alpha-helical antimicrobial peptide
CC       with weak activity against Gram-positive and Gram-negative bacteria and
CC       fungi (PubMed:31671555). Has been tested against E.coli (MIC>217.69
CC       uM), S.aureus (MIC>217.69 uM), K.pneumoniae (MIC>189.00 uM) and
CC       C.albicans (MIC>217.69 uM) (PubMed:31671555). Shows a moderate
CC       hemolytic activity (PubMed:31671555). {ECO:0000269|PubMed:31671555}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31671555}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:31671555}.
CC   -!- MASS SPECTROMETRY: Mass=2354; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:31671555};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Phylloseptin subfamily. {ECO:0000305}.
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DR   EMBL; MK532479; QFU19629.1; -; mRNA.
DR   AlphaFoldDB; A0A5P9K461; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; 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; Cytolysis; Fungicide; Hemolysis;
KW   Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000305|PubMed:31671555"
FT                   /id="PRO_0000449981"
FT   PEPTIDE         46..67
FT                   /note="Phylloseptin-SP1"
FT                   /evidence="ECO:0000269|PubMed:31671555"
FT                   /id="PRO_0000449982"
FT   MOD_RES         67
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:31671555"
SQ   SEQUENCE   68 AA;  7798 MW;  C5B75F5CAC0072B5 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEKERETK EEENEQEDDN REEKRFLSLI PHVISAIPHV
     VNALSNLG