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UniProtKB/Swiss-Prot entry P80280


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DMS4_PHYSA
Primary accession number P80280
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1994
Sequence was last modified on February 1, 1994 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 42)
Name and origin of the protein
Protein name Dermaseptin-4
Synonyms DS IV
Dermaseptin-S4
DS4
Gene name None
From
Phyllomedusa sauvagei (Sauvage's leaf frog) [TaxID: 8395] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae; Phyllomedusa.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE, AND FUNCTION.
TISSUE=Skin secretion;
PubMed=8306981 [NCBI, ExPASy, EBI, Israel, Japan]
Mor A., Nicolas P.;
"Isolation and structure of novel defensive peptides from frog skin.";
Eur. J. Biochem. 219:145-154(1994).
[2]
FUNCTION.
DOI=10.1074/jbc.272.50.31609; PubMed=9395500 [NCBI, ExPASy, EBI, Israel, Japan]
Ghosh J.K., Shaool D., Guillaud P., Ciceron L., Mazier D., Kustanovich I., Shai Y., Mor A.;
"Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis.";
J. Biol. Chem. 272:31609-31616(1997).
[3]
POTENTIAL THERAPEUTIC USAGE.
DOI=10.1016/S0196-9781(01)00504-6; PubMed=11587797 [NCBI, ExPASy, EBI, Israel, Japan]
Feder R., Nehushtai R., Mor A.;
"Affinity driven molecular transfer from erythrocyte membrane to target cells.";
Peptides 22:1683-1690(2001).
[4]
POTENTIAL THERAPEUTIC USAGE IN TREATMENT OF BACTERIAL INFECTIONS.
DOI=10.1128/AAC.46.3.689-694.2002; PubMed=11850249 [NCBI, ExPASy, EBI, Israel, Japan]
Navon-Venezia S., Feder R., Gaidukov L., Carmeli Y., Mor A.;
"Antibacterial properties of dermaseptin S4 derivatives with in vivo activity.";
Antimicrob. Agents Chemother. 46:689-694(2002).
[5]
POTENTIAL THERAPEUTIC USAGE.
DOI=10.1021/bi0201466; PubMed=12119035 [NCBI, ExPASy, EBI, Israel, Japan]
Hariton-Gazal E., Feder R., Mor A., Graessmann A., Brack-Werner R., Jans D., Gilon C., Loyter A.;
"Targeting of nonkaryophilic cell-permeable peptides into the nuclei of intact cells by covalently attached nuclear localization signals.";
Biochemistry 41:9208-9214(2002).
[6]
POTENTIAL THERAPEUTIC USAGE IN TREATMENT OF MALARIA.
DOI=10.1074/jbc.M202089200; PubMed=11937508 [NCBI, ExPASy, EBI, Israel, Japan]
Efron L., Dagan A., Gaidukov L., Ginsburg H., Mor A.;
"Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity in culture.";
J. Biol. Chem. 277:24067-24072(2002).
[7]
POTENTIAL THERAPEUTIC USAGE IN PREVENTION OF HERPES SIMPLEX VIRUS TYPE 1 INFECTION.
DOI=10.1002/jmv.2134; PubMed=11782932 [NCBI, ExPASy, EBI, Israel, Japan]
Belaid A., Aouni M., Khelifa R., Trabelsi A., Jemmali M., Hani K.;
"In vitro antiviral activity of dermaseptins against herpes simplex virus type 1.";
J. Med. Virol. 66:229-234(2002).
[8]
POTENTIAL THERAPEUTIC USAGE IN PREVENTION OF HIV-1 INFECTION.
DOI=10.1016/j.virol.2005.02.002; PubMed=15780876 [NCBI, ExPASy, EBI, Israel, Japan]
Lorin C., Saidi H., Belaid A., Zairi A., Baleux F., Hocini H., Belec L., Hani K., Tangy F.;
"The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro.";
Virology 334:264-275(2005).
[9]
POTENTIAL THERAPEUTIC USAGE IN TREATMENT OF BACTERIAL INFECTIONS.
DOI=10.1128/AAC.00030-06; PubMed=16870756 [NCBI, ExPASy, EBI, Israel, Japan]
Rotem S., Radzishevsky I., Mor A.;
"Physicochemical properties that enhance discriminative antibacterial activity of short dermaseptin derivatives.";
Antimicrob. Agents Chemother. 50:2666-2672(2006).
[10]
STRUCTURE BY NMR OF 1-14 OF MUTANT MET-4 AND 14-ALA--ALA-27 DEL.
DOI=10.1074/jbc.M513051200; PubMed=16407175 [NCBI, ExPASy, EBI, Israel, Japan]
Shalev D.E., Rotem S., Fish A., Mor A.;
"Consequences of N-acylation on structure and membrane binding properties of dermaseptin derivative K4-S4-(1-13).";
J. Biol. Chem. 281:9432-9438(2006).
Comments
  • FUNCTION: Possesses a potent antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi, protozoa, and the enveloped herpes simplex virus type 1. Probably acts by disturbing membrane functions with its amphipathic structure. Binds to healthy erythrocytes (this binding is receptor independent), and has strong hemolytic activity. Does not bind to P.falciparum infected erythrocytes, but accumulates within the parasite. Kills the parasite, and only at high concentrations has an hemolytic activity on the host cell.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Expressed by the skin glands.
  • PHARMACEUTICAL: Derivatives of this peptide may be used as therapeutic agents to treat bacterial infections and malaria, and to prevent infection by herpes simplex virus type 1 and HIV-1.
  • SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
3D structure databases
PDB
2DCX; NMR; -; A=1-14.[ExPASy / RCSB / EBI]
2DD6; NMR; -; A=1-14.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2DCX; -.
2DD6; -.
ModBase P80280.
Family and domain databases
BLOCKS P80280.
Phylogenomic databases
HOVERGEN P80280; -.
Other
ProtoNet P80280.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Fungicide; Hemolysis; Pharmaceutical; Secreted.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
PEPTIDE   1   27  27     Dermaseptin-4. PRO_0000043642
MUTAGEN   4    4        M->K: K4-S4-(1-13) selectively disrupts the plasma membrane of the intracellular parasite P.falciparum without harming that of the mammalian host cell; when associated with 14-A--A-27 DEL. 
MUTAGEN   14   27        Missing: K4-S4-(1-13) selectively disrupts the plasma membrane of the intracellular parasite P.falciparum without harming that of the mammalian host cell; when associated with K-4. 
STRAND   3    5  3      
HELIX   6   10  5      
Sequence information
Length: 27 AA [This is the length of the unprocessed precursor] Molecular weight: 2779 Da [This is the MW of the unprocessed precursor] CRC64: 43C94D2DC19721A8 [This is a checksum on the sequence]
        10         20 
ALWMTLLKKV LKAAAKALNA VLVGANA 

P80280 in FASTA format

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