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Entry version 88 (05 Dec 2018)
Sequence version 1 (01 Nov 1996)
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Protein

Beta-insect depressant toxin LqhIT2

Gene
N/A
Organism
Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus hebraeus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Depressant insect beta-toxins cause a transient contraction paralysis followed by a slow flaccid paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active only on insects.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei16Forms a hot-spot in the bioactive surface1
Sitei24Forms a hot-spot in the bioactive surface1
Sitei28Forms a hot-spot in the bioactive surface1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Beta-insect depressant toxin LqhIT2
Short name:
Insect toxin 2
Short name:
Lqh IT2
Alternative name(s):
LqhIT2-44
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiLeiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus hebraeus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6884 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeLeiurus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi24Y → F: 21-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi26K → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi27R → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi28R → D: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi29D → A: 22-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi30G → N: 55-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi32K → A: 240-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi32K → R: 25-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi32K → T: 122-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi33V → R: 50-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi33V → W: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi34A → E or R: 60-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi34A → S: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi34A → W: No significant increase in binding affinity to cockroach sodium channels, but significant increase of ability to shift the voltage dependence of activation in Drosophila sodium channel DmNav1 (para). 1 Publication1
Mutagenesisi36L → A: 24-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi37I → A: 700-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi38G → A: 33-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi39N → A: 35-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi40E → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi41G → A: 61-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi43D → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi44K → A: 600-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi45E → A: 119-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi45E → R: 460-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi49Y → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi49Y → W: 27-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi52S → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi53Y → V: 72-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi55Y → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi57W → A: 250-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi59W → A: 250-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi66E → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi69P → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi70D → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi71D → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi72K → D: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi73T → W: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi74W → V: 650-fold decrease in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi75K → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi77E → G: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi78T → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi79N → A: 110-fold decrease in binding affinity to cockroach sodium channels. 2 Publications1
Mutagenesisi79N → D: 950-fold decrease in binding affinity to cockroach sodium channels, and important loss of paralytic activity against Sarcophaga larvae. 2 Publications1
Mutagenesisi79N → G: 590-fold decrease in binding affinity to cockroach sodium channels. 2 Publications1
Mutagenesisi79N → Q: 99-fold decrease in binding affinity to cockroach sodium channels. 2 Publications1
Mutagenesisi79N → S: 24.4-fold decrease in binding affinity to cockroach sodium channels. 2 Publications1
Mutagenesisi80T → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1
Mutagenesisi82G → A: No significant change in binding affinity to cockroach sodium channels. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 211 PublicationAdd BLAST21
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003519322 – 82Beta-insect depressant toxin LqhIT2Add BLAST61

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi31 ↔ 81PROSITE-ProRule annotation1 PublicationImported
Disulfide bondi35 ↔ 56PROSITE-ProRule annotation1 PublicationImported
Disulfide bondi42 ↔ 63PROSITE-ProRule annotation1 PublicationImported
Disulfide bondi46 ↔ 65PROSITE-ProRule annotation1 PublicationImported
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei82Glycine amide1 Publication1

Keywords - PTMi

Amidation, Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q26292

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed by the venom gland.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

185
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I61X-ray1.20A22-82[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q26292

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q26292

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q26292

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini22 – 82LCN-type CS-alpha/betaPROSITE-ProRule annotationAdd BLAST61

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00107 Knot1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.30.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003614 Scorpion_toxin-like
IPR036574 Scorpion_toxin-like_sf
IPR018218 Scorpion_toxinL
IPR002061 Scorpion_toxinL/defensin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00537 Toxin_3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00285 SCORPNTOXIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00505 Knot1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57095 SSF57095, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51863 LCN_CSAB, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q26292-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLLLLLIVS ASMLIESLVN ADGYIKRRDG CKVACLIGNE GCDKECKAYG
60 70 80
GSYGYCWTWG LACWCEGLPD DKTWKSETNT CGGKK
Length:85
Mass (Da):9,334
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCFCE3BB0A7079297
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
S55538 mRNA Translation: AAB25386.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A61616

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S55538 mRNA Translation: AAB25386.1
PIRiA61616

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I61X-ray1.20A22-82[»]
ProteinModelPortaliQ26292
SMRiQ26292
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ26292

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ26292

Family and domain databases

CDDicd00107 Knot1, 1 hit
Gene3Di3.30.30.10, 1 hit
InterProiView protein in InterPro
IPR003614 Scorpion_toxin-like
IPR036574 Scorpion_toxin-like_sf
IPR018218 Scorpion_toxinL
IPR002061 Scorpion_toxinL/defensin
PfamiView protein in Pfam
PF00537 Toxin_3, 1 hit
PRINTSiPR00285 SCORPNTOXIN
SMARTiView protein in SMART
SM00505 Knot1, 1 hit
SUPFAMiSSF57095 SSF57095, 1 hit
PROSITEiView protein in PROSITE
PS51863 LCN_CSAB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSIX2_LEIHE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q26292
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 88 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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