PTC1_AGADC
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 25-MAY-2022, entry version 58.
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";
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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: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
