PLS3_PHYSA
ID PLS3_PHYSA Reviewed; 66 AA.
AC F7UI86;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Phylloseptin-S3 {ECO:0000303|PubMed:23967105};
DE Short=PLS-S3 {ECO:0000303|PubMed:23967105};
DE Flags: Precursor;
OS Phyllomedusa sauvagei (Sauvage's leaf frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=8395;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS OF 47-65, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Skin secretion;
RX PubMed=23967105; DOI=10.1371/journal.pone.0070782;
RA Raja Z., Andre S., Piesse C., Sereno D., Nicolas P., Foulon T., Oury B.,
RA Ladram A.;
RT "Structure, antimicrobial activities and mode of interaction with membranes
RT of novel [corrected] phylloseptins from the painted-belly leaf frog,
RT Phyllomedusa sauvagii.";
RL PLoS ONE 8:E70782-E70782(2013).
CC -!- FUNCTION: Antimicrobial peptide with activity against the Gram-positive
CC S.pyogenes (MIC=12.5 uM), but not against all other bacteria tested
CC (both Gram-positive and Gram-negative) (PubMed:23967105). Does not show
CC activity against fungi, and against Leishmania species
CC (PubMed:23967105). {ECO:0000269|PubMed:23967105}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is <7. Is active against E.coli ATCC25922 at pH 5 (MIC=50
CC uM), whereas is not active at pH 7 (MIC>200 uM).
CC {ECO:0000269|PubMed:23967105};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23967105}. Target
CC cell membrane {ECO:0000305|PubMed:23967105}. Note=Forms a helical
CC membrane channel in the target. {ECO:0000305|PubMed:23967105}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:23967105}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Phylloseptin subfamily. {ECO:0000305}.
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DR EMBL; AM903079; CAP17492.1; -; mRNA.
DR AlphaFoldDB; F7UI86; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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; Cleavage on pair of basic residues;
KW Immunity; Innate immunity; Membrane; Secreted; Signal;
KW Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..46
FT /evidence="ECO:0000305"
FT /id="PRO_0000449583"
FT PEPTIDE 47..65
FT /note="Phylloseptin-S3"
FT /id="PRO_5003369566"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:F7UI85"
SQ SEQUENCE 66 AA; 7549 MW; B24A694B78332AD6 CRC64;
MAFLKKSLFL VLFLGLVSLS ICEEEKRETE EEEHDQEEDD KSEEKRFLSL IPHIVSGVAS
LAIHFG