DRS1_PHYSA
ID DRS1_PHYSA Reviewed; 79 AA.
AC P24302; P80277; Q7T3K6;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 3.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Dermaseptin-S1 {ECO:0000303|PubMed:18644413};
DE Short=DRS-S1 {ECO:0000303|PubMed:18644413, ECO:0000303|PubMed:9647785};
DE AltName: Full=Dermaseptin {ECO:0000303|PubMed:16140737, ECO:0000303|PubMed:21262294, ECO:0000303|PubMed:8294443, ECO:0000303|PubMed:9647785};
DE Short=DS {ECO:0000303|PubMed:8294443};
DE AltName: Full=Dermaseptin I {ECO:0000303|PubMed:8306981};
DE Short=DS I {ECO:0000303|PubMed:8306981};
DE AltName: Full=Dermaseptin-1 {ECO:0000303|PubMed:16307969};
DE Short=DS1 {ECO:0000303|PubMed:16307969};
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=14599725; DOI=10.1016/j.regpep.2003.08.001;
RA Chen T., Tang L., Shaw C.;
RT "Identification of three novel Phyllomedusa sauvagei dermaseptins (sVI-
RT sVIII) by cloning from a skin secretion-derived cDNA library.";
RL Regul. Pept. 116:139-146(2003).
RN [2]
RP PROTEIN SEQUENCE OF 46-79, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Skin secretion;
RX PubMed=1909573; DOI=10.1021/bi00100a014;
RA Mor A., Nguyen V.H., Delfour A., Migliore-Samour D., Nicolas P.;
RT "Isolation, amino acid sequence, and synthesis of dermaseptin, a novel
RT antimicrobial peptide of amphibian skin.";
RL Biochemistry 30:8824-8830(1991).
RN [3]
RP PROTEIN SEQUENCE OF 46-79, 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 [4]
RP FUNCTION, MUTAGENESIS OF 46-ALA--ALA-71 AND 64-LYS--GLN-79, AND SYNTHESIS
RP OF 46-79.
RX PubMed=8294443; DOI=10.1016/s0021-9258(17)42116-8;
RA Mor A., Nicolas P.;
RT "The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible
RT for antimicrobial activity.";
RL J. Biol. Chem. 269:1934-1939(1994).
RN [5]
RP FUNCTION ON POLYMORPHONUCLEAR LEUKOCYTES, MUTAGENESIS OF 46-ALA--HIS-61 AND
RP 56-GLY--GLN-79, AND SYNTHESIS OF 46-79.
RX PubMed=9647785; DOI=10.1006/bbrc.1998.8879;
RA Ammar B., Perianin A., Mor A., Sarfati G., Tissot M., Nicolas P.,
RA Giroud J.P., Roch-Arveiller M.;
RT "Dermaseptin, a peptide antibiotic, stimulates microbicidal activities of
RT polymorphonuclear leukocytes.";
RL Biochem. Biophys. Res. Commun. 247:870-875(1998).
RN [6]
RP FUNCTION AS ANTIVIRAL PEPTIDE.
RX PubMed=15193922; DOI=10.1016/j.virol.2004.02.029;
RA Chinchar V.G., Bryan L., Silphadaung U., Noga E., Wade D.,
RA Rollins-Smith L.;
RT "Inactivation of viruses infecting ectothermic animals by amphibian and
RT piscine antimicrobial peptides.";
RL Virology 323:268-275(2004).
RN [7]
RP FUNCTION AS SPERMICIDE.
RX PubMed=16307969; DOI=10.1016/j.contraception.2005.06.055;
RA Zairi A., Belaid A., Gahbiche A., Hani K.;
RT "Spermicidal activity of dermaseptins.";
RL Contraception 72:447-453(2005).
RN [8]
RP FUNCTION ON HIV.
RX PubMed=16140737; DOI=10.1128/jvi.79.18.11598-11606.2005;
RA VanCompernolle S.E., Taylor R.J., Oswald-Richter K., Jiang J., Youree B.E.,
RA Bowie J.H., Tyler M.J., Conlon J.M., Wade D., Aiken C., Dermody T.S.,
RA KewalRamani V.N., Rollins-Smith L.A., Unutmaz D.;
RT "Antimicrobial peptides from amphibian skin potently inhibit human
RT immunodeficiency virus infection and transfer of virus from dendritic cells
RT to T cells.";
RL J. Virol. 79:11598-11606(2005).
RN [9]
RP FUNCTION ON LEISHMANIA.
RX PubMed=21262294; DOI=10.1016/j.peptides.2011.01.011;
RA Perez-Cordero J.J., Lozano J.M., Cortes J., Delgado G.;
RT "Leishmanicidal activity of synthetic antimicrobial peptides in an
RT infection model with human dendritic cells.";
RL Peptides 32:683-690(2011).
RN [10]
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 activity with potent activity against Gram-
CC positive and Gram-negative bacteria, fungi and protozoa
CC (PubMed:1909573, PubMed:8306981, PubMed:8294443). Also stimulates the
CC microbicidal activity of polymorphonuclear leukocytes (PubMed:9647785).
CC Probably acts by disturbing membrane functions with its amphipathic
CC structure (PubMed:8306981). Does not show cytotoxicity on lymphocytes
CC or KB cells (PubMed:8294443). Does not show hemolytic activity
CC (PubMed:1909573, PubMed:8294443, PubMed:21262294). In vitro, shows
CC spermicidal, antiviral, and anti-leishmanial activities
CC (PubMed:16307969, PubMed:16140737, PubMed:21262294).
CC {ECO:0000269|PubMed:15193922, ECO:0000269|PubMed:16140737,
CC ECO:0000269|PubMed:16307969, ECO:0000269|PubMed:1909573,
CC ECO:0000269|PubMed:21262294, ECO:0000269|PubMed:8294443,
CC ECO:0000269|PubMed:8306981, ECO:0000269|PubMed:9647785}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1909573,
CC ECO:0000269|PubMed:8306981}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:1909573, ECO:0000305|PubMed:8306981}.
CC -!- MASS SPECTROMETRY: Mass=3455.4; Method=FAB;
CC Evidence={ECO:0000269|PubMed:1909573};
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=0157";
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DR EMBL; AJ564794; CAD92232.1; -; mRNA.
DR PIR; A40298; A40298.
DR AlphaFoldDB; P24302; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0050688; P:regulation of defense response to virus; 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 Amphibian defense peptide; Antibiotic; Antimicrobial; Antiviral protein;
KW Direct protein sequencing; Fungicide; Immunity; Innate immunity; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..45
FT /evidence="ECO:0000269|PubMed:1909573,
FT ECO:0000269|PubMed:8306981"
FT /id="PRO_0000449895"
FT PEPTIDE 46..79
FT /note="Dermaseptin-S1"
FT /evidence="ECO:0000269|PubMed:1909573,
FT ECO:0000269|PubMed:8306981"
FT /id="PRO_0000044732"
FT MUTAGEN 46..71
FT /note="Missing: DS(20-34); Loss of antimicrial activity
FT (only tested against fungi)."
FT /evidence="ECO:0000269|PubMed:8294443"
FT MUTAGEN 46..61
FT /note="Missing: Loss of stimulation of polymorphonuclear
FT leukocytes."
FT /evidence="ECO:0000269|PubMed:9647785"
FT MUTAGEN 56..79
FT /note="Missing: Loss of stimulation of polymorphonuclear
FT leukocytes."
FT /evidence="ECO:0000269|PubMed:9647785"
FT MUTAGEN 64..79
FT /note="Missing: DS(1-18); Increase in antimicrial activity
FT (tested against bacteria, and fungi). No change in activity
FT against erythrocytes."
FT /evidence="ECO:0000269|PubMed:8294443"
SQ SEQUENCE 79 AA; 8812 MW; F8B1966A145E8114 CRC64;
MDILKKSLFL VLFLGLVSLS ICEEEKRENE DEEKQEDDEQ SEMKRALWKT MLKKLGTMAL
HAGKAALGAA ADTISQGTQ
