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Protein

Hge-scorpine

Gene
N/A
Organism
Hadrurus gertschi (Scorpion)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hge-scorpine has antibacterial activity against B.subtilis, but not against S.aureus. Also has hemolytic and cytolytic activities.1 Publication
Hge36 peptide blocks Kv1.1/KCNA1 (IC50=185 nM) potassium channels. Shows a weak hemolytic activity.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide, Ion channel impairing toxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

Keywords - Biological processi

Cytolysis

Names & Taxonomyi

Protein namesi
Recommended name:
Hge-scorpine
Alternative name(s):
Hg-scorpine-like 1
Short name:
HgeScplp1
Short name:
Hgscplike1
Cleaved into the following chain:
OrganismiHadrurus gertschi (Scorpion)
Taxonomic identifieri380989 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesIuridaIuroideaHadrurus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000027468220 – 95Hge-scorpineAdd BLAST76
ChainiPRO_000035688748 – 95Hge36Add BLAST48

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 81By similarity
Disulfide bondi68 ↔ 86By similarity
Disulfide bondi72 ↔ 88By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni50 – 52Combined sources3
Beta strandi53 – 55Combined sources3
Helixi68 – 74Combined sources7
Beta strandi77 – 81Combined sources5
Beta strandi86 – 92Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IPONMR-A48-95[»]
5JYHNMR-A52-95[»]
SMRiQ0GY40.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR029237. Long_scorpion_toxin.
[Graphical view]
PfamiPF14866. Toxin_38. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q0GY40-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTKLTVLCF LGIVTIVSCG WMSEKKVQGI LDKKLPEGII RNAAKAIVHK
60 70 80 90
MAKNQFGCFA NVDVKGDCKR HCKAEDKEGI CHGTKCKCGV PISYL
Length:95
Mass (Da):10,412
Last modified:October 3, 2006 - v1
Checksum:iEA797C1F58CF6C3C
GO

Mass spectrometryi

Molecular mass is 8370.0 Da from positions 20 - 95. Determined by ESI. 1 Publication
Molecular mass is 8370.0 Da from positions 20 - 95. Determined by MALDI. 1 Publication
Molecular mass is 5294.95 Da from positions 48 - 95. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ465351 mRNA. Translation: ABE98267.1.
EF613116 Genomic DNA. Translation: ABU94956.1.
EL698908 mRNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ465351 mRNA. Translation: ABE98267.1.
EF613116 Genomic DNA. Translation: ABU94956.1.
EL698908 mRNA. No translation available.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IPONMR-A48-95[»]
5JYHNMR-A52-95[»]
SMRiQ0GY40.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR029237. Long_scorpion_toxin.
[Graphical view]
PfamiPF14866. Toxin_38. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKBX3_HADGE
AccessioniPrimary (citable) accession number: Q0GY40
Secondary accession number(s): A8SDT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: October 3, 2006
Last modified: November 2, 2016
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

The C-terminus (AA 52-95) blocks Kv1.1/KCNA1, Kv1.2/KCNA2, and Kv1.3/KCNA2 potassium channels, showing a potential important role of AA 48-51.
Hge36 peptide does not block Kv1.2/KCNA2 and Kv1.3/KCNA3.1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Scorpion potassium channel toxins
    Nomenclature of scorpion potassium channel toxins and list of entries
  3. 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.