ID   PTC2_AGACL              Reviewed;          71 AA.
AC   Q800S1;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Plasticin-C2 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=DRP-AC2 {ECO:0000303|PubMed:12709067};
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].
RC   TISSUE=Skin;
RX   PubMed=12709067; DOI=10.1046/j.1432-1033.2003.03584.x;
RA   Vanhoye D., Bruston F., Nicolas P., Amiche M.;
RT   "Antimicrobial peptides from hylid and ranin frogs originated from a 150-
RT   million-year-old ancestral precursor with a conserved signal peptide but a
RT   hypermutable antimicrobial domain.";
RL   Eur. J. Biochem. 270:2068-2081(2003).
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: Neutral peptide with no antimicrobial activity. May act in
CC       synergy with cationic peptides by enhancing their activity. Has a
CC       moderate hemolytic activity. {ECO:0000250|UniProtKB:O93454}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12709067}. Target
CC       cell membrane {ECO:0000305|PubMed:12709067}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:12709067}.
CC   -!- DOMAIN: Plasticins have huge conformational plasticity. They can
CC       display random coil, alpha-helical, beta-sheet or beta-harpin
CC       structures. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Plasticin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=01388";
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DR   EMBL; AY218776; AAO62951.1; -; mRNA.
DR   AlphaFoldDB; Q800S1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; 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   3: Inferred from homology;
KW   Amidation; Amphibian defense peptide; Cleavage on pair of basic residues;
KW   Cytolysis; Hemolysis; Membrane; Secreted; Signal; Target cell membrane;
KW   Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000305|PubMed:12709067,
FT                   ECO:0000305|PubMed:18644413"
FT                   /id="PRO_0000449901"
FT   PEPTIDE         46..68
FT                   /note="Plasticin-C2"
FT                   /id="PRO_5004295821"
FT   PROPEP          70..71
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000449902"
FT   REGION          25..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         68
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   71 AA;  7735 MW;  4E7AC469AE2F26CA CRC64;
     MAFLKKSLLL VLFLALVPLS ICEEEKREEE DEEKQEDDDQ SENKRGLLSG ILNSAGGLLG
     NLIGSLSNGE S