ID   MDS1_AGALE              Reviewed;          18 AA.
AC   P0DQK9;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Medusin-L1 {ECO:0000305};
DE            Short=MDS-L1 {ECO:0000305};
DE   AltName: Full=Phylloseptin-L1 {ECO:0000303|PubMed:17561225};
DE            Short=PLS-L1 {ECO:0000303|PubMed:18644413};
OS   Agalychnis lemur (Lemur leaf frog) (Hylomantis lemur).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=317382;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT LEU-18.
RC   TISSUE=Skin secretion;
RX   PubMed=17561225; DOI=10.1016/j.toxicon.2007.04.017;
RA   Conlon J.M., Woodhams D.C., Raza H., Coquet L., Leprince J., Jouenne T.,
RA   Vaudry H., Rollins-Smith L.A.;
RT   "Peptides with differential cytolytic activity from skin secretions of the
RT   lemur leaf frog Hylomantis lemur (Hylidae: Phyllomedusinae).";
RL   Toxicon 50:498-506(2007).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=18644413; DOI=10.1016/j.peptides.2008.06.017;
RA   Amiche M., Ladram A., Nicolas P.;
RT   "A consistent nomenclature of antimicrobial peptides isolated from frogs of
RT   the subfamily Phyllomedusinae.";
RL   Peptides 29:2074-2082(2008).
CC   -!- FUNCTION: Antimicrobial peptide active against S.aureus (MIC=8 uM) but
CC       inactive against E.coli (PubMed:17561225). Shows also fungicide
CC       activity (By similarity). Also inhibits growth of B.dendrobatidis
CC       zoospores at high concentrations (above 25 uM) (PubMed:17561225). Shows
CC       anticancer activities since it is cytolytic against HepG2 human
CC       hepatoma-derived cells (LC(50)=35 uM) (PubMed:17561225). Is strongly
CC       hemolytic on human erythrocytes (LC(50)=40 uM) (PubMed:17561225).
CC       {ECO:0000250|UniProtKB:L0P329, ECO:0000269|PubMed:17561225}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17561225}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:17561225}.
CC   -!- MASS SPECTROMETRY: Mass=1809.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17561225};
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Medusin-AC (AC L0P329) and of Medusin-AS (AC A0A5Q0MU22).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Medusin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=0973";
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DR   AlphaFoldDB; P0DQK9; -.
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.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Fungicide; Hemolysis; Immunity; Innate immunity;
KW   Secreted.
FT   PEPTIDE         1..18
FT                   /note="Medusin-L1"
FT                   /evidence="ECO:0000269|PubMed:17561225"
FT                   /id="PRO_0000449601"
FT   MOD_RES         18
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:17561225"
SQ   SEQUENCE   18 AA;  1811 MW;  67E372AC148FC233 CRC64;
     LLGMIPLAIS AISALSKL