DRS9_PHYTS
ID DRS9_PHYTS Reviewed; 71 AA.
AC A0A5P9NYS6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Dermaseptin-PT9 {ECO:0000303|PubMed:31635388};
DE Short=DPT9 {ECO:0000303|PubMed:31635388};
DE Short=DRS-PT9 {ECO:0000305};
DE Flags: Precursor;
OS Phyllomedusa tarsius (Brownbelly leaf frog) (Phyllomedusa tarsia).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=306084;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP SYNTHESIS OF 44-68, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-51 AND GLU-66,
RP AND AMIDATION AT VAL-68.
RC TISSUE=Skin secretion;
RX PubMed=31635388; DOI=10.3390/biom9100628;
RA Li M., Xi X., Ma C., Chen X., Zhou M., Burrows J.F., Chen T., Wang L.;
RT "A novel dermaseptin isolated from the skin secretion of phyllomedusa
RT tarsius and its cationicity-enhanced analogue exhibiting effective
RT antimicrobial and anti-proliferative activities.";
RL Biomolecules 9:0-0(2019).
CC -!- FUNCTION: Antimicrobial peptide with activity against fungi, Gram-
CC positive and Gram-negative bacteria (PubMed:31635388). Is active
CC against S.aureus (MIC=16 uM), MRSA (MIC=32 uM), E.faecalis (MIC=16 uM),
CC E.coli (MIC=8 uM), P.aeruginosa (MIC=16 uM), K.pneumoniae (MIC=8 uM),
CC and C. albicans (MIC=64 uM) (PubMed:31635388). Also inhibits biofilm
CC formation (PubMed:31635388). Acts by disrupting cell membranes
CC (PubMed:31635388). Also exhibits anti-proliferative effect against
CC various human cancer cells (PubMed:31635388). Shows weak hemolytic
CC activity towards horse erythrocytes (PubMed:31635388).
CC {ECO:0000269|PubMed:31635388}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31635388}. Target
CC cell membrane {ECO:0000269|PubMed:31635388}. Note=Forms a helical
CC membrane channel in the prey. {ECO:0000305|PubMed:31635388}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:31635388}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermaseptin subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=03133";
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DR EMBL; MN399674; QFU80916.1; -; mRNA.
DR AlphaFoldDB; A0A5P9NYS6; -.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR022731; Dermaseptin.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF12121; DD_K; 1.
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; Fungicide; Immunity; Innate immunity;
KW Membrane; Secreted; Signal; Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..43
FT /evidence="ECO:0000269|PubMed:31635388"
FT /id="PRO_0000449995"
FT PEPTIDE 44..68
FT /note="Dermaseptin-PT9"
FT /evidence="ECO:0000269|PubMed:31635388"
FT /id="PRO_0000449996"
FT PROPEP 69..71
FT /evidence="ECO:0000269|PubMed:31635388"
FT /id="PRO_0000449997"
FT MOD_RES 68
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:31635388"
FT MUTAGEN 51
FT /note="D->K: Important increase in antimicrobial activity
FT (both on bacteria and biofilms), increase of anti-
FT proliferative effects against cancer cells, small increase
FT in hemolysis, and increase in helicity; when associated
FT with K-66."
FT /evidence="ECO:0000269|PubMed:31635388"
FT MUTAGEN 66
FT /note="E->K: Important increase in antimicrobial activity
FT (both on bacteria and biofilms), increase of anti-
FT proliferative effects against cancer cells, small increase
FT in hemolysis, and increase in helicity; when associated
FT with K-51."
FT /evidence="ECO:0000269|PubMed:31635388"
SQ SEQUENCE 71 AA; 8026 MW; BF8D141F06AAFD22 CRC64;
MAFLKKSLFL VLFLGLVSLS ICEEEKRENE MEQEDDEQSE MKRGLWSKIK DAAKTAGKAA
LGFVNEMVGE Q
