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Protein

Dermaseptin-4

Gene
N/A
Organism
Phyllomedusa sauvagei (Sauvage's leaf frog)
Status
Reviewed-Annotation score: 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

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi4M → 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. 1
Mutagenesisi14 – 27Missing : 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 BLAST14

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000436421 – 27Dermaseptin-4Add BLAST27

Expressioni

Tissue specificityi

Expressed by the skin glands.

Structurei

Secondary structure

127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3
Beta strandi7 – 11Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DCXNMR-A1-13[»]
2DD6NMR-A1-13[»]
SMRiP80280.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DCXNMR-A1-13[»]
2DD6NMR-A1-13[»]
SMRiP80280.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80280.

Family and domain databases

ProtoNetiSearch...

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 2, 2016
This is version 60 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.