PLS1_PHYBI
ID PLS1_PHYBI Reviewed; 66 AA.
AC Q800R3;
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=Phylloseptin-B1 {ECO:0000303|PubMed:18644413};
DE Short=PLS-B1 {ECO:0000303|PubMed:18644413};
DE AltName: Full=Dermaseptin PBN1 {ECO:0000303|PubMed:15222751};
DE Short=DRP-PBN1 {ECO:0000303|PubMed:15222751};
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].
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], FUNCTION, AMIDATION AT LEU-65, AND SYNTHESIS OF
RP 47-66.
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 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: Antimicrobial peptide with activity against only a few
CC strains of Gram-positive bacteria (S.aureus and B.megaterium)
CC (PubMed:15222751). Acts in a synergistic effect in combination with
CC Plasticin-B1 at doses that are not active alone (PubMed:15222751).
CC {ECO:0000269|PubMed:15222751}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15222751}. Target
CC cell membrane {ECO:0000305|PubMed:15222751}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:15222751}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Phylloseptin subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00911";
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DR EMBL; AY218784; AAO62959.1; -; mRNA.
DR AlphaFoldDB; Q800R3; -.
DR TCDB; 1.C.52.1.10; the dermaseptin (dermaseptin) family.
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: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 Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Immunity; Innate immunity; Membrane;
KW Secreted; Signal; Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..46
FT /evidence="ECO:0000305|PubMed:15222751"
FT /id="PRO_0000449897"
FT PEPTIDE 47..65
FT /note="Phylloseptin-B1"
FT /evidence="ECO:0000305|PubMed:15222751"
FT /id="PRO_5004298810"
FT MOD_RES 65
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:15222751"
SQ SEQUENCE 66 AA; 7467 MW; A95E305A92111294 CRC64;
MAFLKKSLFL VLFLGLVSLS ICEEEKRETE EKEYDQGEDD KSEEKRFLSL IPHIVSGVAA
LAKHLG