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P80280 (DMS4_PHYSA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dermaseptin-4
Alternative name(s):
DS IV
Dermaseptin-S4
Short name=DS4
OrganismPhyllomedusa sauvagei (Sauvage's leaf frog)
Taxonomic identifier8395 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaHylidaePhyllomedusinaePhyllomedusa

Protein attributes

Sequence length27 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 a hemolytic activity on the host cell. Ref.1 Ref.2

Subcellular location

Secreted.

Tissue specificity

Expressed by the skin glands.

Pharmaceutical use

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.

Sequence similarities

Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 2727Dermaseptin-4
PRO_0000043642

Experimental info

Mutagenesis41M → 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.
Mutagenesis14 – 2714Missing: 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.

Secondary structure

.... 27
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80280 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 43C94D2DC19721A8

FASTA272,779
        10         20 
ALWMTLLKKV LKAAAKALNA VLVGANA 

« Hide

References

[1]"Isolation and structure of novel defensive peptides from frog skin."
Mor A., Nicolas P.
Eur. J. Biochem. 219:145-154(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION.
Tissue: Skin secretion.
[2]"Selective cytotoxicity of dermaseptin S3 toward intraerythrocytic Plasmodium falciparum and the underlying molecular basis."
Ghosh J.K., Shaool D., Guillaud P., Ciceron L., Mazier D., Kustanovich I., Shai Y., Mor A.
J. Biol. Chem. 272:31609-31616(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"Affinity driven molecular transfer from erythrocyte membrane to target cells."
Feder R., Nehushtai R., Mor A.
Peptides 22:1683-1690(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL THERAPEUTIC USAGE.
[4]"Antibacterial properties of dermaseptin S4 derivatives with in vivo activity."
Navon-Venezia S., Feder R., Gaidukov L., Carmeli Y., Mor A.
Antimicrob. Agents Chemother. 46:689-694(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL THERAPEUTIC USAGE IN TREATMENT OF BACTERIAL INFECTIONS.
[5]"Targeting of nonkaryophilic cell-permeable peptides into the nuclei of intact cells by covalently attached nuclear localization signals."
Hariton-Gazal E., Feder R., Mor A., Graessmann A., Brack-Werner R., Jans D., Gilon C., Loyter A.
Biochemistry 41:9208-9214(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL THERAPEUTIC USAGE.
[6]"Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity in culture."
Efron L., Dagan A., Gaidukov L., Ginsburg H., Mor A.
J. Biol. Chem. 277:24067-24072(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL THERAPEUTIC USAGE IN TREATMENT OF MALARIA.
[7]"In vitro antiviral activity of dermaseptins against herpes simplex virus type 1."
Belaid A., Aouni M., Khelifa R., Trabelsi A., Jemmali M., Hani K.
J. Med. Virol. 66:229-234(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL THERAPEUTIC USAGE IN PREVENTION OF HERPES SIMPLEX VIRUS TYPE 1 INFECTION.
[8]"The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro."
Lorin C., Saidi H., Belaid A., Zairi A., Baleux F., Hocini H., Belec L., Hani K., Tangy F.
Virology 334:264-275(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL THERAPEUTIC USAGE IN PREVENTION OF HIV-1 INFECTION.
[9]"Physicochemical properties that enhance discriminative antibacterial activity of short dermaseptin derivatives."
Rotem S., Radzishevsky I., Mor A.
Antimicrob. Agents Chemother. 50:2666-2672(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: POTENTIAL THERAPEUTIC USAGE IN TREATMENT OF BACTERIAL INFECTIONS.
[10]"Consequences of N-acylation on structure and membrane binding properties of dermaseptin derivative K4-S4-(1-13)."
Shalev D.E., Rotem S., Fish A., Mor A.
J. Biol. Chem. 281:9432-9438(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-14 OF MUTANT MET-4 AND 14-ALA--ALA-27 DEL.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DCXNMR-A1-13[»]
2DD6NMR-A1-13[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Other

EvolutionaryTraceP80280.

Entry information

Entry nameDMS4_PHYSA
AccessionPrimary (citable) accession number: P80280
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references