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Entry version 90 (18 Sep 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Kappa-actitoxin-Bgr1a

Gene
N/A
Organism
Bunodosoma granuliferum (Red warty sea anemone)
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

Inhibits voltage-dependent potassium channels of the Kv1 family (Kv1.1/KCNA1 (Kd=6 nM), Kv1.2/KCNA2 (Kd=15 nM), Kv1.3/KCNA3 (Kd=10-39 nM), Kv1.6/KCNA6, and KCa3.1/KCNN4 (Kd=172 nM)).4 Publications

Miscellaneous

Does not act on Kv3.1 up to 125 nM of the toxin (PubMed:9063464). Does not show effect on crabs.1 Publication

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>Sitei6Key residue for binding Kv1.2 and Kv1.32 Publications1
Sitei7Key residue for binding Kv1.31 Publication1
Sitei12Important for binding Kv1.21 Publication1
Sitei13Important for binding Kv1.2 and Kv1.32 Publications1
Sitei17Important for binding Kv1.31 Publication1
Sitei19Key residue for binding Kv1.1 and Kv1.31 Publication1
Sitei22Important for binding Kv1.31 Publication1
Sitei23Key residue for binding Kv1.1, Kv1.2 and Kv1.32 Publications1
Sitei24Important for binding Kv1.1 and key residue for binding Kv1.31 Publication1
Sitei25Key residue for binding Kv1.1, Kv1.2 and Kv1.32 Publications1
Sitei26Important for binding Kv1.1, Kv1.2 and key residue for binding Kv1.32 Publications1
Sitei27Important for binding Kv1.31 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, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

Protein family/group databases

Transport Classification Database

More...
TCDBi
8.B.14.1.1 the sea anemone peptide toxin, class 1 (bgk) 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:
Kappa-actitoxin-Bgr1a1 Publication
Short name:
Kappa-AITX-Bgr1a1 Publication
Alternative name(s):
Potassium channel toxin Bgk2 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>OrganismiBunodosoma granuliferum (Red warty sea anemone)
<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 identifieri31164 [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 lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaActiniidaeBunodosoma

<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

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 <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the lethal dose (LD), paralytic dose (PD), effect dose (ED) or lethal concentration (LC) of a protein toxin.<p><a href='/help/toxic_dose' target='_top'>More...</a></p>Toxic dosei

LD50 is 4.5 µg/kg by intracerebroventricular injection into mice. Symptoms observed are trembling of tail, fasciculations, salivation, paralysis and death.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>Mutagenesisi1V → A: No change in affinity on Kv1.1 and on Kv1.3. Small increase in affinity on Kv1.2. 1 Publication1
Mutagenesisi3R → A: Small decrease in affinity on Kv1.1, Kv1.2 and Kv1.3. 1 Publication1
Mutagenesisi4D → A: Is not properly oxidized. 1 Publication1
Mutagenesisi5W → A: Small decrease in affinity on Kv1.1 and on Kv1.2. No change in affinity on Kv1.3. 1 Publication1
Mutagenesisi5W → Y: No change in affinity on Kv1.1, Kv1.2 and Kv1.6; when associated with F-26. Important decrease in affinity on Kv1.2, and no change in affinity on Kv1.1 and Kv1.6; when associated with A-6 and F-26. 1 Publication1
Mutagenesisi6F → A: No change in affinity on Kv1.1. >500-fold decrease in affinity on Kv1.2. 20-100-fold decrease in affinity on Kv1.3. 46-fold decrease in ability to compete with alpha-dendrotoxin. Important decrease in affinity on Kv1.2, and no change in affinity on Kv1.1 and Kv1.6; when associated with Y-5 and F-26. 3 Publications1
Mutagenesisi7K → A: Small decrease in affinity on Kv1.1 and on Kv1.2. 20-100-fold decrease in affinity on Kv1.3. 1 Publication1
Mutagenesisi8E → A: No change in affinity on Kv1.1. Small increase in affinity on Kv1.2. Small decrease in affinity on Kv1.3. 1 Publication1
Mutagenesisi9T → A: Small decrease in affinity on Kv1.1 and on Kv1.3. Small increase in affinity on Kv1.2. 1 Publication1
Mutagenesisi12R → A: Small decrease in affinity on Kv1.1 and on Kv1.3. 5-20-fold decrease in affinity on Kv1.2. 1 Publication1
Mutagenesisi13H → A: Small decrease in affinity on Kv1.1. 5-20-fold decrease in affinity on Kv1.2 and on Kv1.3. 5.6-fold decrease in ability to compete with alpha-dendrotoxin. 2 Publications1
Mutagenesisi15K → A: Small decrease in affinity on Kv1.1, Kv1.2 and Kv1.3. 1 Publication1
Mutagenesisi16S → A: Small decrease in affinity on Kv1.1 and on Kv1.3. No change in affinity on Kv1.2. 1 Publication1
Mutagenesisi17L → A: Small decrease in affinity on Kv1.1. No change in affinity on Kv1.2. 5-20-fold decrease in affinity on Kv1.3. 1 Publication1
Mutagenesisi19N → A: 20-fold decrease in affinity on Kv1.1. Small decrease in affinity on Kv1.2. 20-100-fold decrease in affinity on Kv1.3. 1 Publication1
Mutagenesisi21R → A: Small decrease in affinity on Kv1.1, Kv1.2 and Kv1.3. 1 Publication1
Mutagenesisi22T → A: Small decrease in affinity on Kv1.1. Small increase in affinity on Kv1.2. 5-20-fold decrease in affinity on Kv1.3. 1 Publication1
Mutagenesisi23S → A: 5-20-fold decrease in affinity on Kv1.1 and on Kv1.2. 20-100-fold decrease in affinity on Kv1.3. 8.3-fold decrease in ability to compete with alpha-dendrotoxin. 2 Publications1
Mutagenesisi24Q → A: 5-20-fold decrease in affinity on Kv1.1. No change in affinity on Kv1.2. 20-100-fold decrease in affinity on Kv1.3. 1 Publication1
Mutagenesisi25K → A: 60-fold decrease in affinity on Kv1.1. >500-fold decrease in affinity on Kv1.2. 20-100-fold decrease in affinity on Kv1.3. >80-fold decrease in ability to compete with alpha-dendrotoxin. 214-fold decrease in affinity on Kv1.1, 23000-fold affinity decrease on Kv1.2 and 1580-fold decrease in affinity on Kv1.3; when associated with A-26. 2 Publications1
Mutagenesisi26Y → A: 20-fold decrease in affinity on Kv1.1. >20-fold decrease in affinity on Kv1.2. 20-100-fold decrease in affinity on Kv1.3. 28-fold decrease in ability to compete with alpha-dendrotoxin. 214-fold decrease in affinity on Kv1.1, 23000-fold affinity decrease on Kv1.2 and 1580-fold decrease in affinity on Kv1.3; when associated with A-25. 2 Publications1
Mutagenesisi26Y → F: No change in affinity on Kv1.1, Kv1.2 and Kv1.6; when associated with Y-5. Important decrease in affinity on Kv1.2, and no change in affinity on Kv1.1 and Kv1.6; when associated with Y-5 and A-6. 1 Publication1
Mutagenesisi27R → A: Small decrease in affinity on Kv1.1 and on Kv1.2. 5-20-fold decrease in affinity on Kv1.3. 1 Publication1
Mutagenesisi29N → A: Shows distorsions in the dichroic spectrum. 5-20-fold decrease in affinity on Kv1.1 and on Kv1.3. Small decrease in affinity on Kv1.2. 1 Publication1
Mutagenesisi32K → A: Shows distorsions in the dichroic spectrum. Small decrease in affinity on Kv1.1 and on Kv1.3. No change in affinity on Kv1.2. 1 Publication1
Mutagenesisi33T → A: Shows distorsions in the dichroic spectrum. No change in affinity on Kv1.1. Small decrease in affinity on Kv1.2 and on Kv1.3. 1 Publication1
Mutagenesisi35E → A: Shows distorsions in the dichroic spectrum. No change in affinity on Kv1.1 and on Kv1.3. Small increase in affinity on Kv1.2. 1 Publication1
Mutagenesisi36L → A: Shows distorsions in the dichroic spectrum. Small decrease in affinity on Kv1.1 and on Kv1.2. 5-20-fold decrease in affinity on Kv1.3. 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_00000448641 – 37Kappa-actitoxin-Bgr1a2 PublicationsAdd BLAST37

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 ↔ 372 Publications
Disulfide bondi11 ↔ 302 Publications
Disulfide bondi20 ↔ 342 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PRoteomics IDEntifications database

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PRIDEi
P29186

<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

137
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P29186

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P29186

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 37ShKTPROSITE-ProRule annotationAdd BLAST36

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>Regioni25 – 26Crucial for binding to potassium channels2

<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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003582 ShKT_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01549 ShK, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51670 SHKT, 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>. 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.

P29186-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30 
VCRDWFKETA CRHAKSLGNC RTSQKYRANC AKTCELC
Length:37
Mass (Da):4,282
Last modified:November 1, 1997 - v2
<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:i1E1315690D28958F
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 4276.8 Da from positions 1 - 37. Determined by MALDI. 1 Publication
Molecular mass is 4272.4 Da from positions 1 - 37. Determined by PD. Monoisotopic mass.1 Publication

Sequence databases

Protein sequence database of the Protein Information Resource

More...
PIRi
S33268

<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

Sequence databases

PIRiS33268

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
1BGKNMR-A1-37[»]
SMRiP29186
ModBaseiSearch...

Protein family/group databases

TCDBi8.B.14.1.1 the sea anemone peptide toxin, class 1 (bgk) family

Proteomic databases

PRIDEiP29186

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP29186

Family and domain databases

InterProiView protein in InterPro
IPR003582 ShKT_dom
PfamiView protein in Pfam
PF01549 ShK, 1 hit
PROSITEiView protein in PROSITE
PS51670 SHKT, 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 nameiK1B_BUNGR
<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: P29186
<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: December 1, 1992
Last sequence update: November 1, 1997
Last modified: September 18, 2019
This is version 90 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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