DRS11_PHYSA
ID DRS11_PHYSA Reviewed; 75 AA.
AC Q1EN13;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Dermaseptin-S11 {ECO:0000303|PubMed:16401077, ECO:0000303|PubMed:18644413};
DE Short=DRS-S11 {ECO:0000303|PubMed:16401077, ECO:0000303|PubMed:18644413};
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].
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 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 Gram-positive and
CC Gram-negative bacteria, and fungi. Has hemolytic activity.
CC {ECO:0000250|UniProtKB:P84923}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16401077}. Target
CC cell membrane {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:16401077}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermaseptin subfamily. {ECO:0000255}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=0939";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ972907; CAI99866.1; -; mRNA.
DR AlphaFoldDB; Q1EN13; -.
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; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF03032; FSAP_sig_propep; 1.
DR PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE 3: Inferred from homology;
KW 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..45
FT /evidence="ECO:0000305|PubMed:16401077"
FT /id="PRO_0000449595"
FT PEPTIDE 46..75
FT /note="Dermaseptin-S11"
FT /id="PRO_5004188695"
FT REGION 25..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 75 AA; 8548 MW; D7EC408E6F84AC05 CRC64;
MAFLKKSLFL VLFLGMVSLS ICEEEKRENE DEEEQEDDEQ SEEKRALWKT LLKGAGKVFG
HVAKQFLGSQ GQPES