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UniProtKB - P56637 (SIXE_HOTJU)
Protein
Beta-insect excitatory toxin Bj-xtrIT
Gene
N/A
Organism
Hottentotta judaicus (Black scorpion) (Buthotus judaicus)
Status
Functioni
Excitatory insect toxins induce a spastic 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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 33 | May be involved in voltage sensor trapping upon activation of sodium channel | 1 | |
Sitei | 48 | May interact with a positively charged residue of the receptor site | 1 |
GO - Molecular functioni
- sodium channel inhibitor activity Source: InterPro
- toxin activity Source: UniProtKB-KW
Keywordsi
Molecular function | Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin |
Names & Taxonomyi
Protein namesi | Recommended name: Beta-insect excitatory toxin Bj-xtrIT1 PublicationShort name: Bj-xtrIT1 Publication Short name: Bjxtr-IT Short name: BjxtrIT |
Organismi | Hottentotta judaicus (Black scorpion) (Buthotus judaicus) |
Taxonomic identifieri | 6863 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Chelicerata › Arachnida › Scorpiones › Buthida › Buthoidea › Buthidae › Hottentotta |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPathology & Biotechi
Toxic dosei
Both variants Bjxtr-IT.56E and Bjxtr-IT.56K have an PD50 of 9.6 ng/100 mg of body weight of blowfly larvae.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 19 | K → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 20 | K → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 26 | D → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 30 | K → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 33 | E → A: 47.5-fold decrease in toxicity and little effect on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 33 | E → F: 743-fold decrease in toxicity and little effect on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 33 | E → R: >10000-fold decrease in toxicity and little decrease in binding affinity. 1 Publication | 1 | |
Mutagenesisi | 48 | E → D: 8.3-fold decrease in toxicity and 43.6-fold decrease in binding affinity. 1 Publication | 1 | |
Mutagenesisi | 48 | E → L: 29-fold decrease in toxicity and 158-fold decrease in binding affinity. 1 Publication | 1 | |
Mutagenesisi | 48 | E → Q: 27.3-fold decrease in toxicity and 74.5-fold decrease in binding affinity. 1 Publication | 1 | |
Mutagenesisi | 48 | E → R: 608-fold decrease in toxicity and 11455-fold decrease in binding affinity. 1 Publication | 1 | |
Mutagenesisi | 51 | K → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 56 | E → I: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 71 – 73 | EDD → AAA: Little effect on toxicity and on the binding affinity. 1 Publication | 3 | |
Mutagenesisi | 71 – 73 | EDD → KRR: Little effect on toxicity and on the binding affinity. 1 Publication | 3 | |
Mutagenesisi | 72 | D → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 73 | D → A: Little effect on toxicity and on the binding affinity. | 1 | |
Mutagenesisi | 74 | K → T: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 81 | D → N: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 84 | K → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 85 | K → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 88 | D → A: Little effect on toxicity and on the binding affinity. 1 Publication | 1 | |
Mutagenesisi | 93 – 94 | Missing : 4.6-fold reduction of toxicity. | 2 | |
Mutagenesisi | 94 | Missing : 5.7-fold reduction of toxicity. | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | 1 PublicationAdd BLAST | 18 | |
ChainiPRO_0000035199 | 19 – 94 | Beta-insect excitatory toxin Bj-xtrIT1 PublicationAdd BLAST | 76 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 34 ↔ 60 | Combined sources2 Publications | ||
Disulfide bondi | 45 ↔ 65 | Combined sources2 Publications | ||
Disulfide bondi | 49 ↔ 67 | Combined sources2 Publications | ||
Disulfide bondi | 61 ↔ 87 | Combined sources2 Publications |
Keywords - PTMi
Disulfide bondExpressioni
Tissue specificityi
Expressed by the venom gland.1 Publication
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P56637 |
SMRi | P56637 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P56637 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 20 – 88 | LCN-type CS-alpha/betaPROSITE-ProRule annotationAdd BLAST | 69 |
Domaini
Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).Curated
Sequence similaritiesi
Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.Curated
Keywords - Domaini
SignalFamily and domain databases
Gene3Di | 3.30.30.10, 1 hit |
InterProi | View protein in InterPro IPR044062, LCN-type_CS_alpha_beta_dom IPR036574, Scorpion_toxin-like_sf IPR002061, Scorpion_toxinL/defensin |
Pfami | View protein in Pfam PF00537, Toxin_3, 1 hit |
SUPFAMi | SSF57095, SSF57095, 1 hit |
PROSITEi | View protein in PROSITE PS51863, LCN_CSAB, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P56637-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKFFLMCLII FPIMGVLGKK NGYPLDRNGK TTECSGVNAI APHYCNSECT
60 70 80 90
KVYYAESGYC CWGACYCFGL EDDKPIGPMK DITKKYCDVQ IIPS
Mass spectrometryi
Molecular mass is 8455 Da. 1 Publication
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 56 | E → K. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ012312 mRNA Translation: CAA09987.1 AJ012313 mRNA Translation: CAA09988.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ012312 mRNA Translation: CAA09987.1 AJ012313 mRNA Translation: CAA09988.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BCG | X-ray | 2.10 | A | 19-94 | [»] | |
4KYP | X-ray | 1.70 | A/B/C/D | 19-94 | [»] | |
AlphaFoldDBi | P56637 | |||||
SMRi | P56637 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P56637 |
Family and domain databases
Gene3Di | 3.30.30.10, 1 hit |
InterProi | View protein in InterPro IPR044062, LCN-type_CS_alpha_beta_dom IPR036574, Scorpion_toxin-like_sf IPR002061, Scorpion_toxinL/defensin |
Pfami | View protein in Pfam PF00537, Toxin_3, 1 hit |
SUPFAMi | SSF57095, SSF57095, 1 hit |
PROSITEi | View protein in PROSITE PS51863, LCN_CSAB, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SIXE_HOTJU | |
Accessioni | P56637Primary (citable) accession number: P56637 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 15, 1998 |
Last sequence update: | December 15, 1998 | |
Last modified: | May 25, 2022 | |
This is version 108 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Animal Toxin Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families