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Entry version 7 (13 Feb 2019)
Sequence version 1 (25 Oct 2017)
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Protein

Toxin GTx1-15

Gene
N/A
Organism
Grammostola porteri (Tarantula spider) (Lasiodora porteri)
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

Potent voltage-gated sodium channel blocker (PubMed:25658507). Potently inhibits the voltage-gated sodium channels Nav1.7/SCN9A (IC50=0.58-10 nM) (PubMed:25658507, PubMed:26999206) (By similarity). Shows a moderate activity on Nav1.1/SCN1A (IC50=6 nM), Nav1.2/SCN2A (IC50=5 nM), Nav1.3/SCN3A (IC50=20.3-170 nM), Nav1.4/SCN4A (IC50=200-326 nM), and Nav1.6/SCN8A (IC50=17 nM) (PubMed:25658507, PubMed:26999206) (By similarity). Shows an unclear inhibition of Nav1.5/SCN5A (IC50=140 nM to >10 µM) and Nav1.8/SCN10A (IC50=68-12200 nM) (PubMed:25658507, PubMed:26999206) (By similarity). Weakly blocks the low voltage-gated calcium channels Cav3.1/CACNA1G (30% inhibition of the peak current by 9.8 nM of the toxin) (By similarity).By similarity1 Publication

Miscellaneous

The mutant [Phe5Ala]GpTx1 is a tool for probing Nav1.7 inhibition in vivo.1 Publication
The primary structure of the mature peptide is identical to that of Gtx1-15 from Grammostola rosea (AC P0DJA9) and Gtx1-15 from Paraphysa scrofa (AC P0DL73).Curated

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>Sitei5Important for activity and sodium channel selectivity1 Publication1
Sitei6Important for activity1 Publication1
Sitei26Important for activity and sodium channel selectivity1 Publication1
Sitei27Important for activity1 Publication1
Sitei28Important for activity and sodium channel selectivity1 Publication1
Sitei29Important for activity1 Publication1
Sitei31Important for activity1 Publication1
Sitei32Important for activity1 Publication1
Sitei34Important for activity1 Publication1

<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

<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 functionCalcium channel impairing toxin, Ion channel impairing toxin, Toxin, Voltage-gated calcium channel impairing 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:
Toxin GTx1-15By similarity
Alternative name(s):
Beta/omega-theraphotoxin-Gr2aCurated
Short name:
Beta/omega-TRTX-Gr2aCurated
Toxin GpTx-11 Publication
<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>OrganismiGrammostola porteri (Tarantula spider) (Lasiodora porteri)
<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 identifieri1749325 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeTheraphosidaeGrammostola

<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>Mutagenesisi1D → A: Decrease in selectivity for hNav1.7 over hNav1.4. No change in activity on hNav1.7 and hNav1.5 and 1.5-fold increase in activity on hNav1.4. 1 Publication1
Mutagenesisi1D → AD: Decrease in selectivity for hNav1.7 over hNav1.4. 4-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1 Publication1
Mutagenesisi3L → A: Decrease in selectivity for hNav1.7 over hNav1.4. 5-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1 Publication1
Mutagenesisi4G → A: Decrease in selectivity for hNav1.7 over hNav1.4. 3-fold decrease in activity on hNav1.7, no change on hNav1.5 and 1.2 decrease in activity on hNav1.4. 1 Publication1
Mutagenesisi5 – 6FM → AF: 1200-fold increase in selectivity for hNav1.7 over hNav1.4; when associated with L-26 and R-28. 1 Publication2
Mutagenesisi5F → A: 2.5-fold increase in selectivity for hNav1.7 over hNav1.4. 2.7-7-fold decrease in activity on hNav1.7, more than 5-fold decrease in activity on hNav1.5 and 17-43-fold decrease in activity on hNav1.4 (depending on the method used). 3.6-fold decrease in activity on TTX-S sodium channels from mouse DRG neurons. 1 Publication1
Mutagenesisi6M → A: Decrease in selectivity for hNav1.7 over hNav1.4. 5-fold decrease in activity on hNav1.7, no change on hNav1.5 and 1.4 decrease in activity on hNav1.4. 1 Publication1
Mutagenesisi7R → A: Decrease in selectivity for hNav1.7 over hNav1.4. 10-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1 Publication1
Mutagenesisi8K → A: Decrease in selectivity for hNav1.7 over hNav1.4. 5-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1 Publication1
Mutagenesisi10I → A: Decrease in selectivity for hNav1.7 over hNav1.4. 2-fold decrease in activity on hNav1.7, no change on hNav1.5 and hNav1.4. 1 Publication1
Mutagenesisi11P → A: Decrease in selectivity for hNav1.7 over hNav1.4. No significant change on hNav1.7, hNav1.5 and hNav1.4. 1 Publication1
Mutagenesisi12D → A: Decrease in selectivity for hNav1.7 over hNav1.4. No change in activity on hNav1.7 and hNav1.5 and 3-fold increase in activity on hNav1.4. 1 Publication1
Mutagenesisi13N → A: Decrease in selectivity for hNav1.7 over hNav1.4. 2-fold decrease in activity on hNav1.7, no change on hNav1.5 and hNav1.4. 1 Publication1
Mutagenesisi15K → A: Decrease in selectivity for hNav1.7 over hNav1.4. 3-fold decrease in activity on hNav1.7, no change on hNav1.5 and 1.7 decrease in activity on hNav1.4. 1 Publication1
Mutagenesisi18R → A: Decrease in selectivity for hNav1.7 over hNav1.4. No change in activity on hNav1.7 and hNav1.4, and decrease in activity on hNav1.5. 1 Publication1
Mutagenesisi19P → A: Decrease in selectivity for hNav1.7 over hNav1.4. No change in activity on hNav1.7, decrease in activity on hNav1.5, and 1.8 increase in activity on hNav1.4. 1 Publication1
Mutagenesisi20N → A: Decrease in selectivity for hNav1.7 over hNav1.4. 8-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1 Publication1
Mutagenesisi21L → A: Decrease in selectivity for hNav1.7 over hNav1.4. 2-fold decrease in activity on hNav1.7 and hNav1.4, and decrease in activity on hNav1.5. 1 Publication1
Mutagenesisi22V → A: Decrease in selectivity for hNav1.7 over hNav1.4. 4-fold decrease in activity on hNav1.7, no change on hNav1.5 and 1.4-fold decrease in activity on hNav1.4. 1 Publication1
Mutagenesisi24S → A: Decrease in selectivity for hNav1.7 over hNav1.4. 5-fold decrease in activity on hNav1.7, no change on hNav1.5 and 1.4-fold increase in activity on hNav1.4. 1 Publication1
Mutagenesisi25R → A: Decrease in selectivity for hNav1.7 over hNav1.4. 4-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1 Publication1
Mutagenesisi26T → A: Decrease in selectivity for hNav1.7 over hNav1.4. 3-fold decrease in activity on hNav1.7, no change on hNav1.5 and 1.2 decrease in activity on hNav1.4. 1200-fold increase in selectivity for hNav1.7 over hNav1.4; when associated with 5-A-F-6 and R-28. 1 Publication1
Mutagenesisi27H → A: Decrease in selectivity for hNav1.7 over hNav1.4. 11-fold decrease in activity on hNav1.7, no change on hNav1.5 and 1.5 decrease in activity on hNav1.4. 1 Publication1
Mutagenesisi28K → A: Decrease in selectivity for hNav1.7 over hNav1.4. 5-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1200-fold increase in selectivity for hNav1.7 over hNav1.4; when associated with 5-A-F-6 and A-26. 1 Publication1
Mutagenesisi29W → A: Complete loss of activity on hNav1.7 and hNav1.4, and no change on hNav1.5. 1 Publication1
Mutagenesisi31K → A: Complete loss of activity on hNav1.7 and hNav1.4, and no change on hNav1.5. 1 Publication1
Mutagenesisi32Y → A: Decrease in selectivity for hNav1.7 over hNav1.4. 9-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1 Publication1
Mutagenesisi33V → A: Decrease in selectivity for hNav1.7 over hNav1.4. 2-fold decrease in activity on hNav1.7, no change on hNav1.5 and 1.7-fold decrease in activity on hNav1.4. 1 Publication1
Mutagenesisi34F → A: Decrease in selectivity for hNav1.7 over hNav1.4. 13-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 1 Publication1
Mutagenesisi34F → FA: Decrease in selectivity for hNav1.7 over hNav1.4. 5-fold decrease in activity on hNav1.7, no change on hNav1.5 and complete loss of activity on hNav1.4. 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004419291 – 34Toxin GTx1-151 PublicationAdd BLAST34

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 bondi2 ↔ 171 Publication
Disulfide bondi9 ↔ 231 Publication
Disulfide bondi16 ↔ 301 Publication
<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 residuei34Phenylalanine amide1 Publication1

Keywords - PTMi

Amidation, Disulfide bond

<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.1 Publication

<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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6MK5NMR-A1-34[»]

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

More...
SMRi
P0DL72

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.1 Publication
This toxin is amphipathic in nature with a hydrophobic face on one side of the molecule (composed of residues 5-Phe-Met-6 and 27-His--Phe-34) and a hydrophilic (mostly cationic) face on the opposite side (composed of residues 10-Ile--Lys-15 and 18-Arg--Pro-19).1 Publication

<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

Knottin

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011696 Huwentoxin-1
IPR013140 Huwentoxin_CS1

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07740 Toxin_12, 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.

P0DL72-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30 
DCLGFMRKCI PDNDKCCRPN LVCSRTHKWC KYVF
Length:34
Mass (Da):4,081
Last modified:October 25, 2017 - 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:iDDEF29032F4A84E2
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 4073.9 Da from positions 1 - 34. Determined by MALDI. Average mass.1 Publication

<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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6MK5NMR-A1-34[»]
SMRiP0DL72
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiView protein in InterPro
IPR011696 Huwentoxin-1
IPR013140 Huwentoxin_CS1
PfamiView protein in Pfam
PF07740 Toxin_12, 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 nameiTX15_GRAPO
<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: P0DL72
<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: October 25, 2017
Last sequence update: October 25, 2017
Last modified: February 13, 2019
This is version 7 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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