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Protein

Cytotoxic linear peptide IsCT

Gene
N/A
Organism
Opisthacanthus madagascariensis (Scorpion)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytotoxic linear peptide IsCT: shows weak hemolytic activity and antibacterial activity against both Gram-positive and Gram-negative bacteria probably by forming pores in the cell membrane. IsCT adopts an amphipathic alpha-helical structure.
Cytotoxic linear peptide IsCTf: shows neither hemolytic, nor antibacterial activities, probably because it cannot adopt amphipathic alpha-helical structure.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei29Important for antibacterial activity, and hemolysis activity1

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Toxin

Keywords - Biological processi

Cytolysis, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Cytotoxic linear peptide IsCT
Alternative name(s):
Non-disulfide-bridged peptide 4.11 Publication
Short name:
NDBP-4.11 Publication
Non-disulfide-bridged peptide 5.21 Publication
Short name:
NDBP-5.21 Publication
Cleaved into the following chain:
OrganismiOpisthacanthus madagascariensis (Scorpion)
Taxonomic identifieri167108 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesIuridaScorpionoideaHemiscorpiidaeOpisthacanthus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted, Target cell membrane, Target membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29W → A: Drastic reduction in antibacterial activity against both Gram-positive and Gram-negative bacteria, and complete loss of hemolysis activity. 1 Publication1
Mutagenesisi29W → L: Drastic reduction in antibacterial activity against both Gram-positive and Gram-negative bacteria, and big loss of hemolysis activity. Similar or 2-fold increase in antibacterial activity against both Gram-positive and Gram-negative bacteria, and big loss of hemolysis activity; when associated with K-34. 1 Publication1
Mutagenesisi30E → K: Similar or 2-fold increase in antibacterial activity against both Gram-positive and Gram-negative bacteria, and little loss of hemolysis activity. Similar or 2-fold increase in antibacterial activity against both Gram-positive and Gram-negative bacteria, and complete loss of hemolysis activity; when associated with P-31 and K-34. 1 Publication1
Mutagenesisi31G → P: Similar or 2-fold increase in antibacterial activity against both Gram-positive and Gram-negative bacteria, and complete loss of hemolysis activity; when associated with K-30 and K-34. 1 Publication1
Mutagenesisi34S → K: Similar or 2-fold increase in antibacterial activity against both Gram-positive and Gram-negative bacteria, and big loss of hemolysis activity; when associated with L-29. Similar or 2-fold increase in antibacterial activity against both Gram-positive and Gram-negative bacteria, and complete loss of hemolysis; when associated with K-30 and P-31. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 232 PublicationsAdd BLAST23
PeptideiPRO_000003535624 – 36Cytotoxic linear peptide IsCTAdd BLAST13
PeptideiPRO_000003535724 – 34Cytotoxic linear peptide IsCTfAdd BLAST11
PropeptideiPRO_000003535840 – 68Add BLAST29

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36Phenylalanine amide1

Post-translational modificationi

IsCTf is an enzymatic proteolytic cleavage product of IsCT by the proteases present in the venom.

Keywords - PTMi

Amidation, Cleavage on pair of basic residues

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

168
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 35Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T51NMR-A24-36[»]
1T52NMR-A24-36[»]
1T54NMR-A24-36[»]
1T55NMR-A24-36[»]
SMRiQ8MMJ7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8MMJ7.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8MMJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTQFAILLV ALVLFQMFAQ SDAILGKIWE GIKSLFGKRG LSDLDGLDEL
60
FDGEISKADR DFLRELMR
Length:68
Mass (Da):7,722
Last modified:October 1, 2002 - v1
Checksum:iFAFBC86E52583297
GO

Mass spectrometryi

Molecular mass is 1502.00 Da from positions 24 - 36. Determined by MALDI. 1 Publication
Molecular mass is 1502.9 Da from positions 24 - 36. Determined by MALDI. 1 Publication
Molecular mass is 1242.80 Da from positions 24 - 34. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF397895 mRNA. Translation: AAM76913.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF397895 mRNA. Translation: AAM76913.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T51NMR-A24-36[»]
1T52NMR-A24-36[»]
1T54NMR-A24-36[»]
1T55NMR-A24-36[»]
SMRiQ8MMJ7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ8MMJ7.

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiNDB41_OPIMA
AccessioniPrimary (citable) accession number: Q8MMJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.