ID PTC1_AGADC Reviewed; 71 AA. AC O93454; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 22-FEB-2023, entry version 60. DE RecName: Full=Plasticin-DA1 {ECO:0000303|PubMed:18644413, ECO:0000303|PubMed:25291467}; DE Short=PTC-DA1 {ECO:0000303|PubMed:18644413, ECO:0000303|PubMed:25291467}; DE AltName: Full=Dermaseptin PD-3-6 {ECO:0000303|PubMed:15222751, ECO:0000303|PubMed:9774745}; DE Short=DRP-PD3-6 {ECO:0000303|PubMed:15222751, ECO:0000303|PubMed:17128968}; DE Short=PD36 {ECO:0000303|PubMed:17128968}; DE Flags: Precursor; OS Agalychnis dacnicolor (Giant Mexican leaf frog) (Pachymedusa dacnicolor). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae; OC Agalychnis. OX NCBI_TaxID=75988; 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 PROTEIN SEQUENCE OF 46-68, FUNCTION, AMIDATION AT GLY-68, SYNTHESIS OF RP 46-68, MUTAGENESIS OF ASN-53; GLY-57 AND VAL-63, AND SUBCELLULAR LOCATION. RC TISSUE=Skin; RX PubMed=15222751; DOI=10.1021/bi0493158; RA Vanhoye D., Bruston F., El Amri S., Ladram A., Amiche M., Nicolas P.; RT "Membrane association, electrostatic sequestration, and cytotoxicity of RT Gly-Leu-rich peptide orthologs with differing functions."; RL Biochemistry 43:8391-8409(2004). RN [3] RP FUNCTION, MUTAGENESIS OF ASN-53; GLY-57 AND VAL-63, AND SYNTHESIS OF 46-78. RX PubMed=17128968; DOI=10.1021/bi060999o; RA El Amri C., Lacombe C., Zimmerman K., Ladram A., Amiche M., Nicolas P., RA Bruston F.; RT "The plasticins: membrane adsorption, lipid disorders, and biological RT activity."; RL Biochemistry 45:14285-14297(2006). RN [4] 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). RN [5] RP STRUCTURE BY NMR OF MUTANT PD36KF IN MEMBRANE-MIMETIC ENVIRONMENT. RX PubMed=25291467; DOI=10.1016/j.bpc.2014.09.004; RA Carlier L., Joanne P., Khemtemourian L., Lacombe C., Nicolas P., RA El Amri C., Lequin O.; RT "Investigating the role of GXXXG motifs in helical folding and self- RT association of plasticins, Gly/Leu-rich antimicrobial peptides."; RL Biophys. Chem. 196:40-52(2015). CC -!- FUNCTION: Neutral peptide with no antimicrobial activity CC (PubMed:15222751, PubMed:17128968). Does not permeate bacterial CC membranes (PubMed:15222751). May act in synergy with cationic peptides CC by enhancing their activity (Probable). Has a moderate hemolytic CC activity (PubMed:15222751, PubMed:17128968). It interacts with CC zwitterionic phospholipids (DMPC) without perturbing either the CC interface or inside of the bilayer, whereas it causes little CC perturbations at the interface peptide-anionic vesicles (DMPG) as well CC as in the bilayer alkyl chains (PubMed:15222751, PubMed:17128968). CC {ECO:0000269|PubMed:15222751, ECO:0000269|PubMed:17128968, CC ECO:0000305|PubMed:17128968}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15222751}. Target CC cell membrane {ECO:0000305|PubMed:15222751}. CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. CC {ECO:0000269|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|PubMed:25291467}. 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=1385"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ005192; CAA06429.1; -; mRNA. DR AlphaFoldDB; O93454; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0044218; C:other organism cell 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 1: Evidence at protein level; KW Amidation; Amphibian defense peptide; Cleavage on pair of basic residues; KW Cytolysis; Direct protein sequencing; Hemolysis; Membrane; Secreted; KW Signal; Target cell membrane; Target membrane. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..42 FT /evidence="ECO:0000305|PubMed:15222751" FT /id="PRO_0000007084" FT PEPTIDE 46..68 FT /note="Plasticin-DA1" FT /evidence="ECO:0000269|PubMed:15222751" FT /id="PRO_0000007085" FT PROPEP 70..71 FT /evidence="ECO:0000305|PubMed:15222751" FT /id="PRO_0000007086" FT REGION 25..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 68 FT /note="Glycine amide" FT /evidence="ECO:0000269|PubMed:15222751" FT MUTAGEN 53 FT /note="N->K: PD36K; Gain in antimicrobial activity and no FT change in hemolysis potency. PD36KF; Gain in antimicrobial FT activity and small increase in hemolysis potency." FT /evidence="ECO:0000269|PubMed:15222751, FT ECO:0000269|PubMed:17128968" FT MUTAGEN 57 FT /note="G->K: PD36K; Gain in antimicrobial activity and no FT change in hemolysis potency. PD36KF; Gain in antimicrobial FT activity and small increase in hemolysis potency." FT /evidence="ECO:0000269|PubMed:15222751, FT ECO:0000269|PubMed:17128968" FT MUTAGEN 63 FT /note="V->F: PD36KF; Gain in antimicrobial activity and FT small increase in hemolysis potency." FT /evidence="ECO:0000269|PubMed:15222751, FT ECO:0000269|PubMed:17128968" SQ SEQUENCE 71 AA; 7781 MW; 94FD43979DCBA150 CRC64; MAFLKKSLFL VLFLALVPLS ICEAEKREEE NEEKQEDDDE SEKKRGVVTD LLNTAGGLLG NLVGSLSGGE R //