ID   MDS_AGACL               Reviewed;          68 AA.
AC   L0P329;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Medusin-C1 {ECO:0000305};
DE            Short=MDS-C1 {ECO:0000305};
DE   AltName: Full=Medusin-AC {ECO:0000303|PubMed:23415652};
DE   AltName: Full=Phyllin-AC {ECO:0000312|EMBL:CCI79382.1};
DE   Flags: Precursor;
OS   Agalychnis callidryas (Red-eyed tree frog) (Phyllomedusa callidryas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=197464;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 50-67, FUNCTION, AMIDATION
RP   AT LEU-67, SUBCELLULAR LOCATION, AND SYNTHESIS OF 50-67.
RC   TISSUE=Skin secretion;
RX   PubMed=23415652; DOI=10.1016/j.biochi.2013.02.005;
RA   Xi X., Li R., Jiang Y., Lin Y., Wu Y., Zhou M., Xu J., Wang L., Chen T.,
RA   Shaw C.;
RT   "Medusins: a new class of antimicrobial peptides from the skin secretions
RT   of phyllomedusine frogs.";
RL   Biochimie 95:1288-1296(2013).
CC   -!- FUNCTION: Antimicrobial peptide with activity against Gram-positive
CC       bacteria (S.aureus, MIC=8 uM) and fungi (C.albicans, MIC=32 uM)
CC       (PubMed:23415652). Shows anticancer activities (By similarity). Shows
CC       weak hemolytic activity (PubMed:23415652).
CC       {ECO:0000250|UniProtKB:P0DQK9, ECO:0000269|PubMed:23415652}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23415652}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:23415652}.
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Medusin-L1 (AC P0DQK9) and of Medusin-AS (AC A0A5Q0MU22).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Medusin subfamily. {ECO:0000255}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=0973";
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DR   EMBL; HE863819; CCI79382.1; -; mRNA.
DR   AlphaFoldDB; L0P329; -.
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   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; Cytolysis; Direct protein sequencing;
KW   Fungicide; Hemolysis; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305|PubMed:23415652"
FT                   /id="PRO_0000449603"
FT   PEPTIDE         50..67
FT                   /note="Medusin-C1"
FT                   /evidence="ECO:0000269|PubMed:23415652"
FT                   /id="PRO_5003946947"
FT   REGION          25..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         67
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:23415652"
SQ   SEQUENCE   68 AA;  7773 MW;  0EB46E2F87F40C09 CRC64;
     MDFLKKSLFL VVFLGLVSLS VCEEEKRESE EEKNEQEEDD REERSEEKRL LGMIPLAISA
     ISALSKLG