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P80280

- DMS4_PHYSA

UniProt

P80280 - DMS4_PHYSA

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Protein

Dermaseptin-4

Gene
N/A
Organism
Phyllomedusa sauvagei (Sauvage's leaf frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB-KW
  2. defense response to fungus Source: UniProtKB-KW
  3. hemolysis in other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Amphibian defense peptide, Antibiotic, Antimicrobial, Fungicide

Keywords - Biological processi

Cytolysis, Hemolysis

Names & Taxonomyi

Protein namesi
Recommended name:
Dermaseptin-4
Alternative name(s):
DS IV
Dermaseptin-S4
Short name:
DS4
OrganismiPhyllomedusa sauvagei (Sauvage's leaf frog)
Taxonomic identifieri8395 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaHyloideaHylidaePhyllomedusinaePhyllomedusa

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41M → 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.
Mutagenesisi14 – 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. Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 2727Dermaseptin-4PRO_0000043642Add
BLAST

Expressioni

Tissue specificityi

Expressed by the skin glands.

Structurei

Secondary structure

1
27
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Beta strandi7 – 115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DCXNMR-A1-13[»]
2DD6NMR-A1-13[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80280.

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Complete.

P80280-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20 
ALWMTLLKKV LKAAAKALNA VLVGANA
Length:27
Mass (Da):2,779
Last modified:February 1, 1994 - v1
Checksum:i43C94D2DC19721A8
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DCX NMR - A 1-13 [» ]
2DD6 NMR - A 1-13 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P80280.

Family and domain databases

ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiDMS4_PHYSA
AccessioniPrimary (citable) accession number: P80280
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 26, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3