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Entry version 96 (20 Dec 2017)
Sequence version 1 (01 Jan 1988)
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Protein

Delta-actitoxin-Axm1b

Gene
N/A
Organism
Anthopleura xanthogrammica (Giant green sea anemone) (Actinia xanthogrammica)
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

Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation. This toxin has the highest affinity of all anemone toxins for the mammalian sodium channel, whereas its paralog Anthopleurin-A retains the greatest capacity to discriminate between cardiac (Nav1.5/SCN5A) and neuronal sodium channels (PubMed:8916901). When tested electrophysiologically, this toxin exhibits a high affinity for multiple sodium channels with a 50-fold preference for rat cardiac (Nav1.5/SCN5A) over neuronal channels (0.1 nM versus 5 nM). When tested by ion flux, the affinities are similar and appear to have higher affinity (9 nM versus 22 nM) (PubMed:8276803, PubMed:7612595). The residue Lys-37 of this toxin has been shown to interact with channel Nav1.5 (residue Asp-1612 in rat and Asp-1610 in human), which is located in the DIV S3-S4 linker (corresponding to channel site 3) (PubMed:9417050, PubMed:24898004). Selectively modifies sodium channel inactivation from the open state with little effect on channel activation or on inactivation from closed states (By similarity). Does not display phospholipid-binding activities, suggesting that the domain IV S3-S4 linker is located at the extracellular surface and not buried in the phospholipid bilayer (PubMed:15632158).By similarity7 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>Sitei7Structurally important1 Publication1
Sitei9Important for sodium channel affinity and for toxin structure1 Publication1
Sitei10Important for affinity to sodium channel, probably due to the flexibility this residue gives to the Arg-14 loop1 Publication1
Sitei12Key residue for binding both cardiac and neuronal sodium channels1 Publication1
Sitei13Important for sodium channel affinity1 Publication1
Sitei14Not essential for sodium channel affinity1 Publication1
Sitei15Important for affinity to sodium channel, probably due to the flexibility this residue gives to the Arg-14 loop1 Publication1
Sitei16Binds to sodium channel1 Publication1
Sitei17Has its side chain oriented away from the channel in the binary complex1 Publication1
Sitei18Important for high affinity to sodium channel1 Publication1
Sitei19Binds to sodium channel1 Publication1
Sitei20Structurally important1 Publication1
Sitei33Important for channel affinity1 Publication1
Sitei34Not important for channel affinity and toxin structure1 Publication1
Sitei37Important for channel affinity (interacts with rat Nav1.5 channel residue Asp-1612)2 Publications1
Sitei39Not important for channel affinity and toxin structure1 Publication1
Sitei43Structurally important1 Publication1
Sitei45Does not affect binding, but may affect the stabilization of the cardiac channel open conformation1 Publication1
Sitei48Binds to sodium channel1 Publication1
Sitei49Important for most of the cardiac specificity1 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

GO - Biological processi

<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 functionCardiotoxin, Ion channel impairing toxin, Neurotoxin, 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:
Delta-actitoxin-Axm1b1 Publication
Short name:
Delta-AITX-Axm1b1 Publication
Alternative name(s):
Anthopleurin-B1 Publication
Short name:
AP-B1 Publication
Short name:
ApB1 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 xanthogrammica (Giant green sea anemone) (Actinia xanthogrammica)
<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 identifieri6112 [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

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>Mutagenesisi3P → S: Minor decrease in affinity for sodium channels (4.7-fold on neuronal and 2-fold on cardiac (Nav1.5) channels). 1 Publication1
Mutagenesisi7D → A or N: Incorrect folding or very limited amount of mutant obtained. 1 Publication1
Mutagenesisi7D → K: Incorrect folding; when associated with D-37. 1 Publication1
Mutagenesisi7D → N: Small decrease in affinity (4-6-fold), and very limited amount of mutant obtained. 1 Publication1
Mutagenesisi9D → A: Major decrease in affinity for both cardiac (Nav1.5) (300-fold) and neuronal (100-fold) channels. 1 Publication1
Mutagenesisi9D → N: Decrease in affinity for both cardiac (Nav1.5) (10-fold) and neuronal (8-fold) channels. 1 Publication1
Mutagenesisi10G → A: Decrease in affinity for both cardiac (Nav1.5) (15-fold) and neuronal (450-fold) channels, as well as a 30-fold increase in discrimination for Nav1.5. Decrease in affinity for cardiac (Nav1.5) (600-fold); when associated with A-15. Not correctly folded; when associated with A-20. 1 Publication1
Mutagenesisi12R → A: Major decrease in affinity for both cardiac (Nav1.5) and neuronal sodium channels. 1 Publication1
Mutagenesisi12R → K: Minor effect on toxicity. 1 Publication1
Mutagenesisi12R → S: Minor effect on toxicity. Decrease in affinity for both cardiac (Nav1.5) (5-fold) and neuronal (37-fold) channels; when associated with Q-49 (tested by ion flux studies). Loss of discrimination between cardiac and neuronal channels; when associated with Val-13 and Q-49. 3 Publications1
Mutagenesisi13P → V: Decrease in affinity for both cardiac (Nav1.5) (9-fold) and neuronal channels (9-fold). Loss of discrimination between cardiac and neuronal channels; when associated with S-12 and Q-49. 1 Publication1
Mutagenesisi14R → A: Minor effect on toxicity. 1 Publication1
Mutagenesisi14R → K: Minor effect on toxicity. 1 Publication1
Mutagenesisi14R → Q: Minor effect on toxicity. Decrease in affinity for both cardiac (Nav1.5) (56-fold) and neuronal (72-fold) channels; when associated with S-12 (tested by ion flux studies). Decrease in affinity for both cardiac (Nav1.5) (13-fold) and neuronal (27-fold) channels; when associated with A-48 (tested by ion flux studies). 2 Publications1
Mutagenesisi15G → A: Decrease in affinity for both cardiac (Nav1.5) (13-fold) and neuronal (600-fold) channels, as well as a 50-fold increase in discrimination for Nav1.5. Decrease in affinity for cardiac (Nav1.5) (600-fold); when associated with A-10. 1 Publication1
Mutagenesisi16N → A: Decrease in affinity for cardiac (Nav1.5) (8-fold) channels. 1 Publication1
Mutagenesisi16N → D: Decrease in affinity for both cardiac (Nav1.5) (500-fold) and neuronal (3600-fold) channels. 1 Publication1
Mutagenesisi16N → R: Decrease in affinity for both cardiac (Nav1.5) (5-fold) and neuronal (56-fold) channels. 1 Publication1
Mutagenesisi17T → A or D: No change in activity. 1 Publication1
Mutagenesisi18L → A: Major decrease in affinity for both cardiac (Nav1.5) (330-fold) and neuronal (34-fold) channels, as well as a 9.5-fold decrease in discrimination for Nav1.5. 1 Publication1
Mutagenesisi18L → V: Decrease in affinity for both cardiac (Nav1.5) and neuronal channels. 1 Publication1
Mutagenesisi19S → A: Decrease in affinity for cardiac (Nav1.5) (5.6-fold) channels. 1 Publication1
Mutagenesisi19S → D: Major decrease in affinity for both cardiac (Nav1.5) (85-fold) and neuronal (653-fold) channels. 1 Publication1
Mutagenesisi19S → R: Decrease in affinity for both cardiac (Nav1.5) (5.7-fold) and neuronal (27-fold) channels. 1 Publication1
Mutagenesisi20G → A: Incorrect folding. Incorrect folding; when associated with A-10. 1 Publication1
Mutagenesisi21I → T: Minor decrease in affinity for sodium channels (2.2-fold on neuronal and 2.9-fold on cardiac (Nav1.5) channels). 1 Publication1
Mutagenesisi24F → L: Minor decrease in affinity for sodium channels (4.8-fold on neuronal and 2.4-fold on cardiac (Nav1.5) channels). 1 Publication1
Mutagenesisi33W → A: No mutant obtained. 1 Publication1
Mutagenesisi33W → F: Major decrease in affinity for both cardiac (Nav1.5) (31-fold) and neuronal (50-fold) channels (tested by ion flux studies). This mutant is the first ApB mutant that displays a significantly altered association rate (K(on)). 1 Publication1
Mutagenesisi33W → S: No mutant obtained. 1 Publication1
Mutagenesisi33W → Y: Minor decrease in affinity for both cardiac (Nav1.5) (5.6-fold) and neuronal (5-fold) channels. 1 Publication1
Mutagenesisi34H → A: Minor decrease in affinity. 1 Publication1
Mutagenesisi37K → A: Decrease in affinity for both cardiac (Nav1.5) (11-fold) and neuronal (7-fold) channels. 1 Publication1
Mutagenesisi37K → A: Decrease in affinity for cardiac (Nav1.5) channels (13-fold) (with decrease in K(on) and increase in K(off)). 1 Publication1
Mutagenesisi37K → D: Incorrect folding; when associated with K-7. 1 Publication1
Mutagenesisi39H → A: No change in activity. 1 Publication1
Mutagenesisi39H → A: Small decrease in affinity for cardiac (Nav1.5) channels (1.1-fold) (with increase in both K(on) and K(off)). 1 Publication1
Mutagenesisi42N → T: Minor decrease in affinity for sodium channels (1.1-fold on neuronal and 3.4-fold on cardiac (Nav1.5) channels). 1 Publication1
Mutagenesisi43I → A, G or F: Incorrect folding. 1 Publication1
Mutagenesisi43I → L or V: Small decrease in apparent binding affinity for both neuronal and cardiac (Nav1.5) channels (tested by ion flux studies). 1 Publication1
Mutagenesisi45W → A: Minor decrease in affinity for both cardiac (Nav1.5) (7.7-fold) and neuronal (4-fold) channels (tested by ion flux studies). 1 Publication1
Mutagenesisi45W → F: Minor decrease in affinity for both cardiac (Nav1.5) (2-4-fold) (with decrease in K(on) and increase in K(off)) and neuronal (5-fold) channels (tested by ion flux studies). 2 Publications1
Mutagenesisi45W → S: Minor decrease in affinity for both cardiac (Nav1.5) (3.3-fold) and neuronal (7-fold) channels (tested by ion flux studies). 1 Publication1
Mutagenesisi48K → A: Minor effect on toxicity. Decrease in affinity for both cardiac (Nav1.5) (13-fold) and neuronal (27-fold) channels; when associated with Q-14 (tested by ion flux studies). 2 Publications1
Mutagenesisi48K → Q: Minor effect on toxicity. 1 Publication1
Mutagenesisi48K → R: Minor effect on toxicity. 1 Publication1
Mutagenesisi49K → A: Minor effect on toxicity. 1 Publication1
Mutagenesisi49K → Q: Minor effect on toxicity. Decrease in affinity for both cardiac (Nav1.5) (5-fold) and neuronal (37-fold) channels; when associated with S-12 (tested by ion flux studies). Loss of discrimination between cardiac and neuronal channels; when associated with S-12 and V-13. 3 Publications1
Mutagenesisi49K → R: Minor effect on toxicity. 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_00002215161 – 49Delta-actitoxin-Axm1b1 PublicationAdd BLAST49

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 ↔ 461 Publication
Disulfide bondi6 ↔ 361 Publication
Disulfide bondi29 ↔ 471 Publication

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

149
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
1APFNMR-A1-49[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P01531

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

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SMRi
P01531

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
P01531

<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>Regioni1 – 7Well-structured region2 Publications7
Regioni8 – 17Arg-14 loop (non-well-structured region)2 Publications10
Regioni18 – 49Well-structured region2 PublicationsAdd BLAST32

<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

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InterProi
View protein in InterPro
IPR000693 Anenome_toxin
IPR023355 Myo_ane_neurotoxin_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00706 Toxin_4, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001905 Anenome_toxin, 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.

P01531-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40 
GVPCLCDSDG PRPRGNTLSG ILWFYPSGCP SGWHNCKAHG PNIGWCCKK
Length:49
Mass (Da):5,274
Last modified:January 1, 1988 - 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:i7BD237179065AE90
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA27737 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti12 – 13RP → PN AA sequence (PubMed:6108877).Curated2
Sequence conflicti25Y → A AA sequence (PubMed:6108877).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M90675 mRNA Translation: AAA27737.1 Different initiation.

Protein sequence database of the Protein Information Resource

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PIRi
A92547 NAXAB

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90675 mRNA Translation: AAA27737.1 Different initiation.
PIRiA92547 NAXAB

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APFNMR-A1-49[»]
ProteinModelPortaliP01531
SMRiP01531
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01531

Family and domain databases

Gene3Di2.20.20.10, 1 hit
InterProiView protein in InterPro
IPR000693 Anenome_toxin
IPR023355 Myo_ane_neurotoxin_sf
PfamiView protein in Pfam
PF00706 Toxin_4, 1 hit
PIRSFiPIRSF001905 Anenome_toxin, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiNA1B_ANTXA
<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: P01531
Secondary accession number(s): V9GZA1
<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: July 21, 1986
Last sequence update: January 1, 1988
Last modified: December 20, 2017
This is version 96 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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