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Entry version 75 (02 Jun 2021)
Sequence version 1 (15 Nov 2002)
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Protein

Beta/omega-theraphotoxin-Tp2a

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

Gating-modifier toxin that targets voltage-gated sodium channels with a selective activity on Nav1.7/SCN9A (IC50=1-1.5 nM) (PubMed:25026046, PubMed:31234412).

It inhibits both activation and inactivation (PubMed:20855463).

For inhibition of activation, it is 100-fold more selective for Nav1.7/SCN9A (IC50=0.26-3) than for other sodium channels (Nav1.2/SCN2A (IC50=40-540 nM), Nav1.3/SCN3A (IC50=102 nM), Nav1.4/SCN4A (IC50=30-39 nM), Nav1.5/SCN5A (IC50=19-90 nM), Nav1.6/SCN8A (IC50=26 nM), and Nav1.8/SCN10A (IC50=146 nM)) (PubMed:12475222, PubMed:17087985, PubMed:18156314, PubMed:18728100, PubMed:20855463, PubMed:25658507, PubMed:27311819, PubMed:30661758).

For inhibition of inactivation, it is 20-fold more potent in inhibiting inactivation on Nav1.7/SCN9A (IC50=250 nM) than other channels (about 4.6 µM for all channels) (PubMed:20855463).

It also weakly inhibits Cav1.2/CACNA1C and Cav3.2/CACNA1H (29% block at 1 µM) (PubMed:17087985, PubMed:20600227, PubMed:24886690).

It inhibits Nav1.7/SCN9A activation by interacting with DII and impairs Nav1.7/SCN9A inactivation by interacting with DIV (PubMed:20855463).

It docks on top of the DII S3 helix Nav1.7/SCN9A (PubMed:30661758, PubMed:30765606).

It is about 60-fold less active on Nav1.7/SCN9A at depolarized potential (0 mV; IC50=15 nM), compared to -120 mV potential (IC50=0.26 nM) (PubMed:30661758).

This toxin binds to lipid membrane (PubMed:15632158, PubMed:27311819).

This ability correlates with hNav1.7/SCN9A inhibition, showing that membrane binding is the first step in the inhibitory mechanism of this toxin (PubMed:27311819).

It inhibits Nav1.2/SCN2A less potently when it is coexpressed with SCN2B or SCN4B than when it is expressed alone, showing that beta subunits (SCN2B and SCN4B) have a protective effect (PubMed:24297919, PubMed:26894959).

13 Publications

Miscellaneous

The ability to inhibit Nav1.7/SCN9A is greatly enhances by unatural modifications such as C-terminal amidation (5-fold) or C-terminal addition of -NHCH3 (25-fold). Such modifications also improve the ability to inhibit Nav1.2/SCN2A, but the selectivity for Nav1.7/SCN9A over Nav1.2/SCN2A is retained.1 Publication
Highly resistant to proteases, such as pepsin, trypsin, chymotrypsin and elastase. The toxin is not degraded in the plasma and shows fast clearance from the circulation.1 Publication
Does not inhibit Kv1.2/KCNA2, Kv1.3/KCNA3, Kv1.5/KCNA5, and Kv2.1/KCNB1 channels (PubMed:12475222). Weakly inhibits calcium channels hCav3.1/CACNA1G (9% inhibition at 1 µM or 81% at 5 µM) and hCav3.3/CACNA1I (8.9% inhibition at 1 µM) (PubMed:24886690).2 Publications

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>Sitei5Part of an aromatic-rich surface that anchors the toxin toward the membrane core relative to lipid headgroups bound along the pore module of Nav1.7/SCN9A1 Publication1
Sitei7Part of an aromatic-rich surface that anchors the toxin toward the membrane core relative to lipid headgroups bound along the pore module of Nav1.7/SCN9A1 Publication1
Sitei22Electrostatic gating-modifier of Nav1.7/SCN9A that antagonizes outward gating-charge movement through direct electrostatic repulsion; may also indirectly antagonize S4 gating-charge movement by neutralizing acidic side chains within the extracellular vestibule of VSD21 Publication1
Sitei24Part of an aromatic-rich surface that anchors the toxin toward the membrane core relative to lipid headgroups bound along the pore module of Nav1.7/SCN9A; it also stabilizes the toxin for productive receptor site engagement1 Publication1
Sitei26Antagonizes outward gating-charge movement of Nav1.7/SCN9A through direct electrostatic repulsion; may also indirectly antagonize S4 gating-charge movement by neutralizing acidic side chains within the extracellular vestibule of VSD21 Publication1
Sitei30Part of an aromatic-rich surface that anchors the toxin toward the membrane core relative to lipid headgroups bound along the pore module of 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

<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, Toxin, Voltage-gated calcium channel impairing toxin, Voltage-gated sodium channel impairing toxin
LigandLipid-binding

Protein family/group databases

Transport Classification Database

More...
TCDBi
8.B.5.2.1, 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_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/omega-theraphotoxin-Tp2aCurated
Short name:
Beta/omega-TRTX-Tp2aCurated
Alternative name(s):
Protoxin-2Curated
Short name:
ProTx-2Curated
Short name:
ProTx21 Publication
Protoxin-II1 Publication
Short name:
PT-II1 Publication
Short name:
ProTx-II2 Publications
<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>OrganismiThrixopelma pruriens (Peruvian green velvet tarantula)
<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 identifieri213387 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeTheraphosidaeThrixopelma

Organism-specific databases

ArachnoServer: Spider toxin database

More...
ArachnoServeri
AS000414, beta/omega-theraphotoxin-Tp2a

<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

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 derivative JNJ63955918 (Y1GPY; W7Q; W30L) is under preclinical trial by Janssen Pharmaceutica as a non-opioid alternative for the pharmacological treatment of severe pain.1 Publication

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>Mutagenesisi1Y → A: No change in binding affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi1Y → GPY: Important increase in selectivity for Nav1.7/SCN9A; derivative JNJ63955918. 1 Publication1
Mutagenesisi3Q → A: No change in binding affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi4K → R in K/R, 30-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. In K/R,E17K, 110-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. 1 Publication1
Mutagenesisi5W → A: At least 10-fold decrease in affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi5W → Y: 290-fold decrease in ability to inhibit Nav1.7/SCN9A, and decrease in ability to bind membranes. 1 Publication1
Mutagenesisi6M → A: At least 10-fold decrease in affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi7W → A: At least 10-fold decrease in affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi7W → Q: Important increase in selectivity for Nav1.7/SCN9A; derivative JNJ63955918. 1 Publication1
Mutagenesisi7W → Y: 111-fold decrease in ability to inhibit Nav1.7/SCN9A, and decrease in ability to bind membranes. 1 Publication1
Mutagenesisi8T → A: No change in binding affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi10D → A: No change in binding affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi11S → A: No change in binding affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi12E → A: No change in binding affinity with Nav1.5/SCN5A. 5-fold increase in ability to inhibit sodium channel Nav1.7/SCN9A. No change in activity towards Nav1.7/SCN9A; when associated with L-19. 2 Publications1
Mutagenesisi14K → R in K/R, 30-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. In K/R,E17K, 110-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. 1 Publication1
Mutagenesisi17E → K: No change in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. In K/R,E17K, 110-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. 1 Publication1
Mutagenesisi19M → L: 1.7-fold decrease in ability to inhibit sodium channel Nav1.7/SCN9A. No change in activity towards Nav1.7/SCN9A; when associated with A-12. 1 Publication1
Mutagenesisi22R → D or E: Important decrease in ability to inhibit human Nav1.7/SCN9A. 1 Publication1
Mutagenesisi22R → K: Small decrease in ability to inhibit human Nav1.7/SCN9A. 1 Publication1
Mutagenesisi22R → Q: Moderate decrease in ability to inhibit human Nav1.7/SCN9A. 1 Publication1
Mutagenesisi23L → A: No change in binding affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi24W → A: At least 10-fold decrease in affinity with Nav1.5/SCN5A. 1 Publication1
Mutagenesisi24W → Y: 180-fold decrease in ability to inhibit Nav1.7/SCN9A, and decrease in ability to bind membranes. 1 Publication1
Mutagenesisi26K → D: Important decrease in ability to inhibit human Nav1.7/SCN9A. 1 Publication1
Mutagenesisi26K → E: Almost complete loss in ability to inhibit human Nav1.7/SCN9A. 1 Publication1
Mutagenesisi26K → R: Small increase in ability to inhibit human Nav1.7/SCN9A. In K/R, 30-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. In K/R,E17K, 110-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. 2 Publications1
Mutagenesisi27K → R in K/R, 30-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. In K/R,E17K, 110-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. 1 Publication1
Mutagenesisi28K → R in K/R, 30-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. In K/R,E17K, 110-fold decrease in ability to inhibit Nav1.7/SCN9A, and change in ability to bind membranes. 1 Publication1
Mutagenesisi30W → L: Important increase in selectivity for Nav1.7/SCN9A; derivative JNJ63955918. 1 Publication1
Mutagenesisi30W → Y: 6-fold decrease in ability to inhibit Nav1.7/SCN9A, and decrease in ability to bind membranes. 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_00000445561 – 30Beta/omega-theraphotoxin-Tp2a1 PublicationAdd BLAST30

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 ↔ 163 PublicationsImported
Disulfide bondi9 ↔ 213 PublicationsImported
Disulfide bondi15 ↔ 253 PublicationsImported

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P83476

<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

130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P83476

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

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SMRi
P83476

Database of comparative protein structure models

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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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni26 – 30Flexible tail region important for ability to inhibit Nav channel1 Publication5
Regioni29 – 30Hydrophobic dyad that anchors the toxin into the membrane while positioning it over the S3 helix of Nav1.7/SCN9A1 Publication2

<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 30 (phrixotoxin) family.Curated

Keywords - Domaini

Knottin

<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>. 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_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.

P83476-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30
YCQKWMWTCD SERKCCEGMV CRLWCKKKLW
Length:30
Mass (Da):3,833
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:i5B8CF4C6338C1B9B
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 3827 Da. Determined by ESI. 1 Publication
Molecular mass is 3827 Da. Determined by MALDI. 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

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N9TNMR-A1-30[»]
5O0UX-ray0.99A1-30[»]
5TCZNMR-A1-29[»]
6MK4NMR-A1-30[»]
6N4IX-ray3.54E/F/G/H1-30[»]
6N4Qelectron microscopy3.60E/F/G/H1-30[»]
6N4Relectron microscopy4.20E/F/G/H1-30[»]
BMRBiP83476
SMRiP83476
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

TCDBi8.B.5.2.1, the na(+)/k(+)/ca(2+) channel targeting tarantula huwentoxin (tht) family

Proteomic databases

PRIDEiP83476

Organism-specific databases

ArachnoServeriAS000414, beta/omega-theraphotoxin-Tp2a

Family and domain databases

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 nameiTXPR2_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: P83476
<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: November 15, 2002
Last sequence update: November 15, 2002
Last modified: June 2, 2021
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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