ID PTC1_PACDA Reviewed; 71 AA. AC O93454; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 22-APR-2020, entry version 52. DE RecName: Full=Plasticin-DA1 {ECO:0000303|PubMed:18644413}; DE Short=PTC-DA1 {ECO:0000303|PubMed:18644413}; DE AltName: Full=Dermaseptin PD-3-6 {ECO:0000303|PubMed:9774745}; DE Flags: Precursor; OS Pachymedusa dacnicolor (Giant mexican leaf frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae; OC Pachymedusa. OX NCBI_TaxID=75988; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT GLY-68. 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: Possesses a potent antimicrobial activity against Gram- CC positive and Gram-negative bacteria. Probably acts by disturbing CC membrane functions with its amphipathic structure (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:9774745}. CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. CC {ECO:0000305|PubMed:9774745}. 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="http://aps.unmc.edu/AP/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 GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0042742; P:defense response to bacterium; 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; Antibiotic; Antimicrobial; KW Cleavage on pair of basic residues; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..42 FT /evidence="ECO:0000305" FT /id="PRO_0000007084" FT PEPTIDE 46..68 FT /note="Plasticin-DA1" FT /evidence="ECO:0000305|PubMed:9774745" FT /id="PRO_0000007085" FT PROPEP 70..71 FT /evidence="ECO:0000305" FT /id="PRO_0000007086" FT MOD_RES 68 FT /note="Glycine amide" FT /evidence="ECO:0000305|PubMed:9774745" SQ SEQUENCE 71 AA; 7781 MW; 94FD43979DCBA150 CRC64; MAFLKKSLFL VLFLALVPLS ICEAEKREEE NEEKQEDDDE SEKKRGVVTD LLNTAGGLLG NLVGSLSGGE R //