DRATY_PHYSA
ID DRATY_PHYSA Reviewed; 69 AA.
AC Q1EN15;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Atypical cationic antimicrobial peptide {ECO:0000303|PubMed:24146759};
DE AltName: Full=Dermaseptin-S9 {ECO:0000303|PubMed:16401077, ECO:0000303|PubMed:20086159, ECO:0000303|PubMed:24146759};
DE Short=DRS-S9 {ECO:0000303|PubMed:16401077, ECO:0000303|PubMed:20086159, ECO:0000303|PubMed:24146759};
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 46-69, SUBCELLULAR
RP LOCATION, STRUCTURE BY NMR OF 46-69 IN TFE, AND SUBUNIT.
RC TISSUE=Skin;
RX PubMed=16401077; DOI=10.1021/bi051711i;
RA Lequin O., Ladram A., Chabbert L., Bruston F., Convert O., Vanhoye D.,
RA Chassaing G., Nicolas P., Amiche M.;
RT "Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic
RT core and cationic termini.";
RL Biochemistry 45:468-480(2006).
RN [2]
RP FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18637027; DOI=10.1111/j.1742-4658.2008.06554.x;
RA Auvynet C., El Amri C., Lacombe C., Bruston F., Bourdais J., Nicolas P.,
RA Rosenstein Y.;
RT "Structural requirements for antimicrobial versus chemoattractant
RT activities for dermaseptin S9.";
RL FEBS J. 275:4134-4151(2008).
RN [3]
RP MUTAGENESIS OF LYS-50; LYS-65 AND LYS-68.
RX PubMed=20086159; DOI=10.1128/aac.01448-09;
RA Wang G., Watson K.M., Peterkofsky A., Buckheit R.W. Jr.;
RT "Identification of novel human immunodeficiency virus type 1-inhibitory
RT peptides based on the antimicrobial peptide database.";
RL Antimicrob. Agents Chemother. 54:1343-1346(2010).
RN [4]
RP FUNCTION, SUBUNIT, AND SYNTHESIS OF 46-69.
RX PubMed=24146759; DOI=10.1371/journal.pone.0075528;
RA Caillon L., Killian J.A., Lequin O., Khemtemourian L.;
RT "Biophysical investigation of the membrane-disrupting mechanism of the
RT antimicrobial and amyloid-like peptide dermaseptin S9.";
RL PLoS ONE 8:E75528-E75528(2013).
CC -!- FUNCTION: Atypical cationic antimicrobial peptide with potent activity
CC against Gram-negative and Gram-positive bacteria (PubMed:16401077,
CC PubMed:18637027). Acts by inducing permeabilization of bacterial
CC membrane (PubMed:16401077). In vitro, also shows chemoattractant
CC activity, which is mediated through a G protein-coupled receptor
CC (probably FPR2 coupled to the ERK1/2 MAPK kinase pathway)
CC (PubMed:18637027). Has slow-kinetic self-association and amyloid-like
CC properties that modulate its activity (PubMed:18637027,
CC PubMed:24146759). The soluble, weakly self-associated forms act on
CC leukocytes to promote chemotaxis but have low antibacterial activity,
CC the oligomers exhibit potent antimicrobial activity, whereas the
CC amyloid-like fibrils have a very weak antibacterial activity
CC (PubMed:18637027). The membrane composition has a great influence on
CC the peptide behavior (PubMed:24146759). The peptide induces membrane
CC leakage and insertion to a lesser extent in model membranes of the
CC anionic lipid phospatidylglycerol (PG) than in the model membranes of
CC the zwitterionic lipid phosphatidylcholine (PC) vesicles
CC (PubMed:24146759). It forms more fibrils in PC than in PG
CC (PubMed:24146759). Membrane perturbations are more observed in the
CC presence of PG than in the presence of PC (PubMed:24146759). The
CC peptide shows low hemolytic activity (PubMed:16401077).
CC {ECO:0000269|PubMed:16401077, ECO:0000269|PubMed:18637027,
CC ECO:0000269|PubMed:24146759}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable. {ECO:0000269|PubMed:18637027};
CC -!- SUBUNIT: Monomer and/or weakly self-associated, oligomer, and amyloid-
CC like fibril (PubMed:18637027, PubMed:24146759). Can adopt a monomeric
CC nonamphipathic alpha-helical conformation, possibly with the aid of its
CC cationic N- and C-termini, when bound to anionic membranes (Probable)
CC (PubMed:16401077). Forms stable and ordered beta-sheet aggregates in
CC aqueous environment or when bound to anionic or zwitterionic
CC phospholipid vesicles (PubMed:18637027, PubMed:24146759).
CC {ECO:0000269|PubMed:16401077, ECO:0000269|PubMed:18637027,
CC ECO:0000269|PubMed:24146759, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16401077}. Target
CC cell membrane {ECO:0000269|PubMed:16401077}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:16401077}.
CC -!- DOMAIN: Has a highly hydrophobic core sequence flanked at either side
CC by cationic termini. {ECO:0000305|PubMed:18637027}.
CC -!- MISCELLANEOUS: The mutant DRS S9r3 shows antiviral activity against
CC HIV. {ECO:0000269|PubMed:20086159}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00764";
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DR EMBL; AJ972905; CAI99864.1; -; mRNA.
DR AlphaFoldDB; Q1EN15; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; 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 Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Amyloid; Antibiotic; Antimicrobial; Chemotaxis;
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..45
FT /evidence="ECO:0000305|PubMed:16401077"
FT /id="PRO_0000449896"
FT PEPTIDE 46..69
FT /note="Atypical cationic antimicrobial peptide"
FT /evidence="ECO:0000305|PubMed:16401077"
FT /id="PRO_5004188775"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 50
FT /note="K->R: In DRS S9r3; Shows high inhibitory activity
FT against HIV."
FT /evidence="ECO:0000269|PubMed:20086159"
FT MUTAGEN 65
FT /note="K->R: In DRS S9r3; Shows high inhibitory activity
FT against HIV."
FT /evidence="ECO:0000269|PubMed:20086159"
FT MUTAGEN 68
FT /note="K->R: In DRS S9r3; Shows high inhibitory activity
FT against HIV."
FT /evidence="ECO:0000269|PubMed:20086159"
SQ SEQUENCE 69 AA; 8383 MW; 47057EC35FE88FFF CRC64;
MAFLKKSLFL VLFLGLVSLS ICDEEKRENE DEENQEDDEQ SEMRRGLRSK IWLWVLLMIW
QESNKFKKM
