DRS3_PHYSA
ID DRS3_PHYSA Reviewed; 30 AA.
AC P80279;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Dermaseptin-S3 {ECO:0000303|PubMed:18644413, ECO:0000303|PubMed:9395500};
DE Short=DRS-S3 {ECO:0000303|PubMed:18644413};
DE AltName: Full=Dermaseptin III {ECO:0000303|PubMed:8306981};
DE Short=DS III {ECO:0000303|PubMed:8306981};
DE AltName: Full=Dermaseptin-3;
DE Short=DS3;
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 PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Skin secretion;
RX PubMed=8306981; DOI=10.1111/j.1432-1033.1994.tb19924.x;
RA Mor A., Nicolas P.;
RT "Isolation and structure of novel defensive peptides from frog skin.";
RL Eur. J. Biochem. 219:145-154(1994).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9395500; DOI=10.1074/jbc.272.50.31609;
RA Ghosh J.K., Shaool D., Guillaud P., Ciceron L., Mazier D., Kustanovich I.,
RA Shai Y., Mor A.;
RT "Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic
RT Plasmodium falciparum and the underlying molecular basis.";
RL J. Biol. Chem. 272:31609-31616(1997).
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: Potent antimicrobial peptide with activity against bacteria
CC and protozoa (By similarity). Also has activity against fungi
CC (PubMed:8306981). Probably acts by disturbing membrane functions with
CC its amphipathic structure (Probable). Binds to healthy erythrocytes
CC (this binding is receptor independent), but has very weak hemolytic
CC activity (PubMed:9395500). Does not bind to P.falciparum infected
CC erythrocytes, but accumulates within the parasite (PubMed:9395500).
CC Kills the parasite, but has no hemolytic activity on the host cell
CC (PubMed:9395500). {ECO:0000250|UniProtKB:P24302,
CC ECO:0000269|PubMed:8306981, ECO:0000269|PubMed:9395500, ECO:0000305}.
CC -!- SUBUNIT: Monomer and oligomer. Forms aggregates in aqueous
CC environments. {ECO:0000269|PubMed:9395500}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8306981}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:8306981}.
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=0159";
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DR AlphaFoldDB; P80279; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR022731; Dermaseptin.
DR Pfam; PF12121; DD_K; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Fungicide; Secreted.
FT PEPTIDE 1..30
FT /note="Dermaseptin-S3"
FT /evidence="ECO:0000269|PubMed:8306981"
FT /id="PRO_0000043641"
SQ SEQUENCE 30 AA; 3024 MW; FD5F190C3DCBB0D7 CRC64;
ALWKNMLKGI GKLAGKAALG AVKKLVGAES
