ID   PTC1_AGAAN              Reviewed;          73 AA.
AC   O93222;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Plasticin-A1 {ECO:0000303|PubMed:18644413};
DE            Short=PTC-A1 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermaseptin AA-2-5 {ECO:0000303|PubMed:9774745};
DE   Flags: Precursor;
OS   Agalychnis annae (Blue-sided leaf frog) (Phyllomedusa annae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=75990;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=9774745; DOI=10.1016/s0167-4838(98)00202-7;
RA   Wechselberger C.;
RT   "Cloning of cDNAs encoding new peptides of the dermaseptin-family.";
RL   Biochim. Biophys. Acta 1388:279-283(1998).
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: Peptide with no antimicrobial activity. May act in synergy
CC       with cationic peptides by enhancing their activity. Has a moderate
CC       hemolytic activity. {ECO:0000250|UniProtKB:O93454}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:9774745}. Target
CC       cell membrane {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:9774745}.
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=1383";
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DR   EMBL; AJ005184; CAA06421.1; -; mRNA.
DR   AlphaFoldDB; O93222; -.
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..42
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000007062"
FT   PEPTIDE         45..70
FT                   /note="Plasticin-A1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000007063"
FT   PROPEP          72..73
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000007064"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         70
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   73 AA;  7855 MW;  4BDACDA9DD8F0944 CRC64;
     MAFLKKSLFL VLFLAIVPLS ICEEEKREEE NEEKQEDDDQ SEKRGLVSGL LNTAGGLLGD
     LLGSLGSLSG GES