UniProtKB - P0DPC2 (TXDF1_DAFVA)
Protein
Mu-theraphotoxin-Df1a
Gene
N/A
Organism
Davus fasciatus (Costa Rican tiger rump) (Cyclosternum fasciatus)
Status
Functioni
Inhibits sodium channel Nav1.7/SCN9A with high potency (IC50=117 nM) and Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.6/SCN8A and Nav1.5/SCN5 with weaker potency. Also inhibits voltage-gated calcium channel Cav3.1/CACNA1G, Cav3.2/CACNA1H and Cav3.3/CACNA1I.1 Publication
Miscellaneous
Does not show activity on voltage-gated potassium channels (Kv).1 Publication
GO - Molecular functioni
- calcium channel inhibitor activity Source: UniProtKB
- sodium channel inhibitor activity Source: UniProtKB
- toxin activity Source: UniProtKB
GO - Biological processi
- pathogenesis Source: InterPro
Keywordsi
Molecular function | Calcium channel impairing toxin, Ion channel impairing toxin, Toxin, Voltage-gated calcium channel impairing toxin, Voltage-gated sodium channel impairing toxin |
Names & Taxonomyi
Protein namesi | Recommended name: Mu-theraphotoxin-Df1a1 PublicationShort name: Mu-TRTX-Df1a1 Publication |
Organismi | Davus fasciatus (Costa Rican tiger rump) (Cyclosternum fasciatus) |
Taxonomic identifieri | 2024242 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Chelicerata › Arachnida › Araneae › Mygalomorphae › Theraphosidae › Davus |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000442773 | 1 – 34 | Mu-theraphotoxin-Df1a1 PublicationAdd BLAST | 34 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 2 ↔ 16 | By similarity | ||
Disulfide bondi | 9 ↔ 21 | By similarity | ||
Disulfide bondi | 15 ↔ 28 | By similarity | ||
Modified residuei | 34 | Phenylalanine amide1 Publication | 1 |
Post-translational modificationi
C-terminal amidation is important for the high potency of the toxin.1 Publication
Keywords - PTMi
Amidation, Disulfide bondExpressioni
Tissue specificityi
Expressed by the venom gland.1 Publication
Family & Domainsi
Domaini
The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.By similarity
Sequence similaritiesi
Keywords - Domaini
KnottinFamily and domain databases
InterProi | View protein in InterPro IPR011696, Huwentoxin-1 |
Pfami | View protein in Pfam PF07740, Toxin_12, 1 hit |
i Sequence
Sequence statusi: Complete.
Mass spectrometryi
Molecular mass is 4075.8 Da. Determined by MALDI. 1 Publication
Similar proteinsi
Cross-referencesi
3D structure databases
SMRi | P0DPC2 |
ModBasei | Search... |
Family and domain databases
InterProi | View protein in InterPro IPR011696, Huwentoxin-1 |
Pfami | View protein in Pfam PF07740, Toxin_12, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TXDF1_DAFVA | |
Accessioni | P0DPC2Primary (citable) accession number: P0DPC2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 20, 2017 |
Last sequence update: | December 20, 2017 | |
Last modified: | February 10, 2021 | |
This is version 7 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
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families