ID   MDS_AGASP               Reviewed;          68 AA.
AC   A0A5Q0MU22;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Medusin-AS {ECO:0000303|PubMed:31671555};
DE            Short=MDS-AS {ECO:0000305};
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], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   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: Antimicrobial peptide active against Gram-positive bacteria
CC       and fungi but inactive against Gram-negative bacteria. Also inhibits
CC       growth of B.dendrobatidis zoospores at high concentrations. Shows
CC       anticancer activities. Shows hemolytic activity.
CC       {ECO:0000250|UniProtKB:L0P329, ECO:0000250|UniProtKB:P0DQK9}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31671555}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:31671555}.
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Phylloseptin-L1 (AC P0DQK9) and of medusin-AS (AC L0P329).
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=00973";
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DR   EMBL; MK766840; QFZ95566.1; -; mRNA.
DR   AlphaFoldDB; A0A5Q0MU22; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; 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; Fungicide; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305|PubMed:31671555"
FT                   /id="PRO_0000449979"
FT   PEPTIDE         50..67
FT                   /note="Medusin-AS"
FT                   /evidence="ECO:0000305|PubMed:31671555"
FT                   /id="PRO_0000449980"
FT   REGION          24..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         67
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250|UniProtKB:L0P329,
FT                   ECO:0000250|UniProtKB:P0DQK9"
SQ   SEQUENCE   68 AA;  7729 MW;  14AE6852FCF37B79 CRC64;
     MAFLKKSLFL VLFLGLVSLS VCEEEKRESE EEKNEQEEDD RDERSEEKRL LGMIPLAISA
     ISALSKLG