PTC1_PHYBI
ID PTC1_PHYBI Reviewed; 70 AA.
AC Q800R4;
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-B1 {ECO:0000303|PubMed:18644413, ECO:0000303|PubMed:25291467};
DE Short=PTC-B1 {ECO:0000303|PubMed:18644413, ECO:0000303|PubMed:25291467};
DE AltName: Full=Dermaseptin PBN2 {ECO:0000303|PubMed:18644413};
DE Short=DRP-PBN2 {ECO:0000303|PubMed:17128968};
DE AltName: Full=PBN2 KF {ECO:0000303|PubMed:17128968};
DE Flags: Precursor;
OS Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=8393;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SYNTHESIS OF 45-70.
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 NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-70, FUNCTION OF NATIVE
RP PEPTIDE AND SHORT ANALOG, 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 OF SHORT ANALOG, AND SYNTHESIS OF 45-67.
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 45-70 IN MEMBRANE-MIMETIC ENVIRONMENT, AND SUBUNIT.
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: The native peptide is a cationic amphipathic alpha-helical
CC antimicrobial peptide with potent activity against both Gram-positive
CC and Gram-negative bacteria (PubMed:12709067, PubMed:15222751). It has
CC weak activity against fungi and shows low hemolytic activity
CC (PubMed:12709067, PubMed:15222751). Acts in a synergistic effect in
CC combination with Phylloseptin-B1 or Dermaseptin-B2 at doses that are
CC not active alone (PubMed:12709067, PubMed:15222751). In membrane-
CC mimetic environment, it adopts well-defined helices that lie parallel
CC to the micelle surface (Probable). A short amidated analog (AA 45-67),
CC shows potent activity against Gram-positive, Gram-negative bacteria,
CC and fungi (Probable) (PubMed:15222751, PubMed:17128968). In synergy
CC with Phylloseptin-B1, this analog acts more potently (PubMed:15222751).
CC Its rapid rate for killing E.coli suggests that the membrane is its
CC primary target (PubMed:15222751). This analog is cytotoxic toward
CC differentiated eukaryotic cells (nucleus fragmentation and apoptotic
CC bodies are observed in Hela cells) (PubMed:17128968). This analog has a
CC moderate hemolytic activity (PubMed:17128968). It may interact with
CC anionic phospholipids (DMPG) by decreasing the associated water content
CC of the phospholipid heads (CO), replacing water molecules by peptides
CC themselves (Probable). This analog may have a strong capacity to cross
CC membranes (Probable). {ECO:0000269|PubMed:12709067,
CC ECO:0000269|PubMed:15222751, ECO:0000269|PubMed:17128968, ECO:0000305,
CC ECO:0000305|PubMed:17128968, ECO:0000305|PubMed:25291467}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25291467}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15222751}. Target
CC cell membrane {ECO:0000305|PubMed:15222751}.
CC -!- TISSUE SPECIFICITY: Highly expressed by the skin glands, and intestine
CC and weakly expressed in brain. {ECO:0000269|PubMed:15222751}.
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 -!- CAUTION: Functional studies have principally been done on a short
CC synthetic amidated peptide (AA 45-67) instead of the native peptide (AA
CC 45-70) which is not amidated. {ECO:0000305|PubMed:15222751,
CC ECO:0000305|PubMed:17128968}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00737";
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DR EMBL; AY218783; AAO62958.1; -; mRNA.
DR AlphaFoldDB; Q800R4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; 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 Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Hemolysis; Immunity; Innate immunity; Membrane; Secreted; Signal;
KW Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..44
FT /evidence="ECO:0000305|PubMed:15222751"
FT /id="PRO_0000449903"
FT PEPTIDE 45..70
FT /note="Plasticin-B1"
FT /evidence="ECO:0000269|PubMed:15222751"
FT /id="PRO_5004295649"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 70 AA; 7602 MW; 42BD4AAACA1E5D5D CRC64;
MAFLKKSLFL VLFLALVPLS ICEEKKSEEE NEEKQEDDQS EEKRGLVTSL IKGAGKLLGG
LFGSVTGGQS
