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UniProtKB - P83480 (TXPR1_THRPR)

Entry version 75 (02 Dec 2020)
Sequence version 1 (15 Nov 2002)
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Protein

Beta/omega-theraphotoxin-Tp1a

Gene
N/A
Organism
Thrixopelma pruriens (Peruvian green velvet tarantula)
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

Ion channel impairing toxin that inhibits voltage-gated calcium channel Cav3.1/CACNA1G (IC50=53 nM), voltage-gated potassium channels Kv2.1/KCNB1 (IC50=411 nM), all sodium channels tested (Nav1.2/SCN2A (IC50=60-104 nM), Nav1.5/SCN5A (IC50=76-358 nM), Nav1.6/SCN8A (IC50=21-133 nM), Nav1.7/SCN9A (IC50=51-95 nM), and Nav1.8/SCN10A) and the nociceptor cation channel TRPA1 (IC50=389 nM) (PubMed:12475222, PubMed:17087985, PubMed:20351484, PubMed:24886690, PubMed:29703751, PubMed:31234412, PubMed:24530065). Acts as a potent and selective blocker of voltage-gated calcium channel Cav3.1/CACNA1G, but not of Cav3.2/CACNA1H, and Cav3.3/CACNA1I (PubMed:20351484, PubMed:24886690). On Nav1.7/SCN9A, primarily interacts with the DII and DIV voltage-sensor domains (PubMed:32511987). Also acts as an inhibitor of nociceptor cation channel TRPA1 (IC50~389 nM) by binding to the S1-S4 gating domain of TRPA1 (PubMed:24530065). It shows moderate affinity for lipid bilayers (PubMed:29703751).7 Publications

Miscellaneous

The primary structure of the mature peptide is identical to that of Beta/omega-theraphotoxin-Bp1a from Bumba pulcherrimaklaasi (AC P0DQN3).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>Sitei6Pharmacophore for Nav1.7/SCN9A1 Publication1
Sitei19Pharmacophore for Nav1.7/SCN9A1 Publication1
Sitei27Pharmacophore for Nav1.7/SCN9A1 Publication1
Sitei29Pharmacophore for Nav1.7/SCN9A1 Publication1
Sitei30Pharmacophore for Nav1.7/SCN9A1 Publication1
Sitei31Pharmacophore for Nav1.7/SCN9A1 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated calcium channel impairing toxin, Voltage-gated potassium channel impairing toxin, Voltage-gated sodium channel impairing toxin

Protein family/group databases

Transport Classification Database

More...TCDBi		8.B.5.1.1, the na(+)/k(+)/ca(2+) channel targeting tarantula huwentoxin (tht) family

<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%5Fand%5Ftaxonomy%5Fsection">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/omega-theraphotoxin-Tp1aCurated
Short name:
Beta/omega-TRTX-Tp1aCurated
Alternative name(s):
Protoxin-1Curated
Short name:
ProTx-1Curated
Short name:
ProTx1Curated
Protoxin-I2 Publications
Short name:
ProTx-I7 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiThrixopelma pruriens (Peruvian green velvet tarantula)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri213387 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Ecdysozoa › Arthropoda › Chelicerata › Arachnida › Araneae › Mygalomorphae › Theraphosidae › Thrixopelma

Organism-specific databases

ArachnoServer: Spider toxin database

More...ArachnoServeri		AS000413, beta/omega-theraphotoxin-Tp1a

<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 & Seán O’Donoghue; 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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

The amidated mutant G32A (ProTx-I-G32A-NH2) shows a decreased ability to inhibit all sodium channels tested, with a more pronounced reduction on Nav1.2/SCN2A and Nav1.5/SCN5A. As a consequence, this mutant shows an enhanced selectivity and potency for Nav1.7/SCN9A, and thus may provide a good starting point for second generation analogs to treat pain.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi3R → A: Reduced ability to inhibit sodium channel Nav1.2/SCN2A. 1 Publication1
Mutagenesisi5W → A: Reduced ability to inhibit sodium channel Nav1.2/SCN2A. 1 Publication1
Mutagenesisi6L → A: Decrease in ability to inhibit Nav1.7/SCN9A. 1 Publication1
Mutagenesisi13Q → A: Reduced ability to inhibit nociceptor cation channel TRPA1. 1 Publication1
Mutagenesisi17K → E: Decrease in ability to inhibit Nav1.2/SCN2A, Nav1.5/SCN5A, Nav1.6/SCN8A and Nav1.7/SCN9A. 1 Publication1
Mutagenesisi19L → A: Decrease in ability to inhibit the channels TRPA1, Nav1.2/SCN2A, and Nav1.7/SCN9A, probably due to improper folding. 2 Publications1
Mutagenesisi22S → A: Reduced ability to inhibit nociceptor cation channel TRPA1. Reduced ability to inhibit sodium channel Nav1.2/SCN2A. 1 Publication1
Mutagenesisi23R → A: Reduced ability to inhibit sodium channel Nav1.2/SCN2A. 1 Publication1
Mutagenesisi27W → A: Decrease in ability to inhibit Nav1.2/SCN2A and Nav1.7/SCN9A. 2 Publications1
Mutagenesisi29V → A: Decrease in ability to inhibit Nav1.2/SCN2A and Nav1.7/SCN9A. 2 Publications1
Mutagenesisi30W → A: Decrease in ability to inhibit the channels TRPA1, Nav1.2/SCN2A and Nav1.7/SCN9A. 2 Publications1
Mutagenesisi31D → A: Decrease in ability to inhibit Nav1.2/SCN2A and Nav1.7/SCN9A. 2 Publications1
Mutagenesisi32G → A: Reduced ability to inhibit sodium channel Nav1.2/SCN2A. 1 Publication1
Mutagenesisi34F → A: Reduced ability to inhibit nociceptor cation channel TRPA1. Reduced ability to inhibit sodium channel Nav1.2/SCN2A. 1 Publication1
Mutagenesisi35S → A: Reduced ability to inhibit nociceptor cation channel TRPA1. 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 position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_00000450291 – 35Beta/omega-theraphotoxin-Tp1a1 PublicationAdd BLAST35

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 ↔ 16Combined sources1 Publication
Disulfide bondi9 ↔ 21Combined sources1 Publication
Disulfide bondi15 ↔ 28Combined sources1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

An unnatural amidation at Ser-35 provokes a 14-fold increased toxin ability to inhibit Nav1.2/SCN2A and a ~2-fold decreased toxin ability to inhibit both Nav1.5/SCN5A and Nav1.6/SCN8A.1 Publication

Keywords - PTMi

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

Secondary structure

135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P83480

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

More...SMRi		P83480

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

<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

Belongs to the neurotoxin 10 (Hwtx-1) family. 54 (ProTx-1) subfamily.Curated

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

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P83480-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30 
ECRYWLGGCS AGQTCCKHLV CSRRHGWCVW DGTFS
Length:35
Mass (Da):3,994
Last modified:November 15, 2002 - 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:i13F35B2F3A59B2A5
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 3988.3 Da. Determined by ESI. 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:

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
2M9LNMR-A1-35[»]
BMRBiP83480
SMRiP83480
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

TCDBi8.B.5.1.1, the na(+)/k(+)/ca(2+) channel targeting tarantula huwentoxin (tht) family

Organism-specific databases

ArachnoServeriAS000413, beta/omega-theraphotoxin-Tp1a

Family and domain databases

InterProiView protein in InterPro
IPR011696, Huwentoxin-1
PfamiView protein in Pfam
PF07740, Toxin_12, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiTXPR1_THRPR
<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: P83480
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: December 2, 2020
This is version 75 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, Pharmaceutical

Documents

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