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Entry version 59 (20 Dec 2017)
Sequence version 1 (24 May 2004)
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Protein

Pi-actitoxin-Ael2b

Gene
N/A
Organism
Anthopleura elegantissima (Green aggregating anemone) (Actinia elegantissima)
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

This toxin potently blocks acid-sensing ion channel ASIC3 homotrimers and heterotrimers containing ASIC3 (composed with isoforms of ASIC1 and ASIC2) (PubMed:15044953). It also weakly inhibits potassium channels, and sodium channels (PubMed:15044953, PubMed:21943094, PubMed:22972919, PubMed:25337890). On homomeric ASIC3, this protein shows IC50=57-87 nM on rat, 37.3 nM on mouse and 175 nM on human channels (PubMed:15044953, PubMed:18923424, PubMed:19306891, PubMed:20813121, PubMed:21943094, PubMed:22851922, PubMed:22851929). The blockade is rapid and reversible (PubMed:15044953). On heterotrimeric forms, the toxin is less potent (IC50=117 nM on rat ASIC2b-ASIC3 channel, 900 nM on rat ASIC1b-ASIC3, and 2 µM on rat ASIC1a-ASIC3) (PubMed:15044953). It weakly inhibits Kv3.4/KCNC4 potassium channels (3 µM of the toxin inhibits 38% of Kv3.4 current) (PubMed:15044953). It reversibly and voltage-dependently inhibits hKv11.1/KCNH2/ERG1 potassium channels (IC50=1.21 µM), inhibiting both peak and tail currents without action on channel inactivation (PubMed:25337890). It weakly inhibits rNav1.2/SCN2A (EC(50)=114 nM), rNav1.6/SCN8A current (17% at 1 µM of the toxin) and Nav1.8/SCN10A (IC50=6.6 µM on human channels expressed in oocytes, EC(50)=55 nM on rat channels expressed in oocytes, and 2.6 µM on rat channels in DRG neurons) (PubMed:21943094, PubMed:22972919). It may act on sodium channels by binding at site 1 or close by, when the pore is in an open configuration (PubMed:22972919). In vivo, central injection does not induce neurotoxin symptoms in mice even after 24 hours (PubMed:15044953). However, it abolishes acid-induced pain in rats (PubMed:18923424).9 Publications

Miscellaneous

This protein does not block rat ASIC1a and ASIC1b (ASIC1 isoforms), ASIC2a (ASIC2 isoform), and the heteromeric ASIC2a-ASIC3 channels (PubMed:15044953, PubMed:18923424, PubMed:19306891). It also does not inhibit most of voltage-gated potassium channels tested (Kv1.4, Kv2.2, Kv3.1, Kv4.1, Kv4.2, Kv4.3) (PubMed:15044953). It does not inhibit Nav1.3, Nav1.4, Nav1.5 and Nav1.7 (PubMed:22972919). It shows a very weak inhibition on Nav1.6 (17% inhibition by 1 µM of the toxin) (PubMed:22972919).3 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>Sitei1Important in ability to inhibit ASIC31 Publication1
Sitei2Important in ability to inhibit ASIC31 Publication1
Sitei8Important in ability to inhibit Kv11.1/KCNH2/ERG11 Publication1
Sitei15Important in ability to inhibit ASIC31 Publication1 Publication1
Sitei16Important in ability to inhibit ASIC31 Publication1 Publication1
Sitei17Important in ability to inhibit ASIC31 Publication2 Publications1
Sitei18Important in ability to inhibit Kv11.1/KCNH2/ERG11 Publication1
Sitei24Probably important in ability to inhibit ASIC31 Publication1
Sitei31Interacts with ASIC31 Publication1
Sitei32Interacts with ASIC31 Publication1
Sitei33Important in ability to inhibit both ASIC3 and Kv11.1/KCNH2/ERG11 Publication1 Publication1
Sitei34Important in ability to inhibit both ASIC3 and Kv11.1/KCNH2/ERG11 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 functionIon channel impairing toxin, Potassium channel impairing toxin, Proton-gated sodium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin, Voltage-gated sodium channel impairing toxin

Protein family/group databases

Transport Classification Database

More...
TCDBi
8.B.11.1.2 the sea anemone peptide toxin (apetx) 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:
Pi-actitoxin-Ael2b1 Publication
Short name:
Pi-AITX-Ael2b1 Publication
Alternative name(s):
Toxin APETx21 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>OrganismiAnthopleura elegantissima (Green aggregating anemone) (Actinia elegantissima)
<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 identifieri6110 [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 lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaActiniidaeAnthopleura

<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

Nematocyst, 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

Is under preclinical studies as a novel analgesic for the treatment of chronic inflammatory 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>Mutagenesisi1 – 2Missing : 300-fold decrease in ability to inhibit rASIC3 and small decrease in ability to inhibit hKv11.1/KCNH2/ERG1. 2 Publications2
Mutagenesisi3A → P: 4.1-fold decrease in ability to inhibit rASIC3 and no change in ability to inhibit hKv11.1/KCNH2/ERG1. 1 Publication1
Mutagenesisi5S → A: 2.5-fold decrease in ability to inhibit rASIC3. 1 Publication1
Mutagenesisi8N → A: 1.2-fold increase in ability to inhibit rASIC3 and decrease in ability to inhibit hKv11.1/KCNH2/ERG1. 1 Publication1
Mutagenesisi10K → A: 1.8-fold decrease in ability to inhibit rASIC3. 1 Publication1
Mutagenesisi15F → A: >100-fold decrease in ability to inhibit rASIC3. 1 Publication1
Mutagenesisi16Y → A or F: Complete loss of ability to inhibit rASIC3. 1 Publication1
Mutagenesisi17R → A: 44-fold decrease in ability to inhibit rASIC3 and mASIC3. 2 Publications1
Mutagenesisi17R → E: Complete loss of ability to inhibit rASIC3. 1 Publication1
Mutagenesisi18P → A: 3-fold decrease in ability to inhibit rASIC3 and decrease in ability to inhibit hKv11.1/KCNH2/ERG1. 1 Publication1
Mutagenesisi23D → A: 1.1-fold decrease in ability to inhibit rASIC3. 1 Publication1
Mutagenesisi24R → A or Q: About 25-fold decrease in ability to inhibit rASIC3. 1 Publication1
Mutagenesisi31R → A: 2.1-fold decrease in ability to inhibit rASIC3. 1 Publication1
Mutagenesisi32Y → A: 2.5-fold decrease in ability to inhibit rASIC3, probably due to alterations in the orientation of the side chains of neighboring residues of functional importance. No change in ability to inhibit hKv11.1/KCNH2/ERG1. 1 Publication1
Mutagenesisi33F → A: Complete loss of ability to inhibit rASIC3 and hKv11.1/KCNH2/ERG1 (tail current only). 1 Publication1
Mutagenesisi34L → A: Complete loss of ability to inhibit rASIC3 and hKv11.1/KCNH2/ERG1. 1 Publication1
Mutagenesisi40 – 42Missing : 18-fold decrease in ability to inhibit rASIC3. 1 Publication3

<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_00002215401 – 42Pi-actitoxin-Ael2b1 PublicationAdd BLAST42

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 bondi4 ↔ 373 PublicationsImported
Disulfide bondi6 ↔ 303 PublicationsImported
Disulfide bondi20 ↔ 383 PublicationsImported

Keywords - PTMi

Disulfide bond

<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

142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WXNNMR-A1-42[»]
2MUBNMR-A1-42[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P61542

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

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SMRi
P61542

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P61542

<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>Regioni13 – 14Play an important role in the folding and structural integrity of APETx21 Publication2

<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

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.20.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012414 BDS_K_chnl_tox
IPR023355 Myo_ane_neurotoxin_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07936 Defensin_4, 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.

P61542-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40 
GTACSCGNSK GIYWFYRPSC PTDRGYTGSC RYFLGTCCTP AD
Length:42
Mass (Da):4,567
Last modified:May 24, 2004 - 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:i3E8B26BA8655781D
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 4557.96 Da from positions 1 - 42. Determined by MALDI. Monoisotopic 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
1WXNNMR-A1-42[»]
2MUBNMR-A1-42[»]
ProteinModelPortaliP61542
SMRiP61542
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi8.B.11.1.2 the sea anemone peptide toxin (apetx) family

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP61542

Family and domain databases

Gene3Di2.20.20.10, 1 hit
InterProiView protein in InterPro
IPR012414 BDS_K_chnl_tox
IPR023355 Myo_ane_neurotoxin_sf
PfamiView protein in Pfam
PF07936 Defensin_4, 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 nameiBDS2_ANTEL
<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: P61542
<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: May 24, 2004
Last sequence update: May 24, 2004
Last modified: December 20, 2017
This is version 59 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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