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Entry version 53 (22 Apr 2020)
Sequence version 2 (01 Sep 2009)
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Protein

DELTA-actitoxin-Afr1a

Gene
N/A
Organism
Actinia fragacea (Strawberry 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

Pore-forming toxin (PFT) that consists of a crown-shaped octamer or nonamer that forms cation-selective hydrophilic pores of about 1.5 nm (inside) and 13 nm (outside) (PubMed:21300287, PubMed:25716479). It causes cardiac stimulation and hemolysis (PubMed:19563820, PubMed:25759390). Interestingly, the Phe-16 is crucial for hemolysis (PubMed:25759390). Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers (PubMed:19563820, PubMed:25716479). It is probable that a dimeric form is an assembly intermediate before the complete oligomerization (PubMed:25716479). The formation of stable pores occurs only in vesicles composed of DOPC/SM (there is no oligomerization when the PFT is treated with vesicles of DOPC or SM alone) (PubMed:25716479). The transmembrane pore displays 8 lateral perforations, one at each subunit-subunit interface, partially occupied by the acyl-chain region of a bridging lipid (PubMed:25716479). Each pore contains 24 lipid molecules, firmly bound to each subunit, that is, 3 lipids (L1, L2, L3, L4 and/or L5) are associated to each subunit (PubMed:25716479). Lipid L1 bridges 2 subunits, whereas lipids L2 and L3 bind to sites at single subunit (PubMed:25716479).4 Publications

Miscellaneous

This protein has been found to bind carbohydrates, since it shows a substantial delay in elution profile in size-exclusion chromatography. The carbohydrate pocket ovelaps with the lipid-binding module of actinoporins.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>Sitei16Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B); essential in hemolysis, since it is critical for pore formation in cholesterol-rich membrane cells (such as red blood cells)3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei31Binds bridging lipid L1 (subunit A) (in oligomeric forms, only)1 Publication1
Binding sitei51Carbohydrate1 Publication1
Binding sitei53Binds lipid L2 and/or L4 (in monomeric and oligomeric forms)1 Publication1
Binding sitei53Carbohydrate1 Publication1
Binding sitei54Binds lipid L2 (in monomeric and oligomeric forms)1 Publication1
Sitei60Protrudes from one subunit (B) and inserts into the hydrophobic cavity from the adjacent subunit (A)2 Publications1
Binding sitei79Binds bridging lipid L1 (subunit B) (in oligomeric forms, only); via amide nitrogen1 Publication1
Binding sitei85Binds lipid L2 (in monomeric and oligomeric forms); via amide nitrogen1 Publication1
Binding sitei108Binds lipid L2 (in monomeric and oligomeric forms); via amide nitrogen1 Publication1
Binding sitei113Binds lipid L2 (in monomeric and oligomeric forms)1 Publication1
Binding sitei114Binds lipid L5 (in monomeric and oligomeric forms)1 Publication1
Binding sitei116Binds lipid L3 (in monomeric and oligomeric forms)1 Publication1
Binding sitei133Binds lipid L4 (in monomeric and oligomeric forms)1 Publication1
Binding sitei137Binds lipid L3 (in monomeric and oligomeric forms)1 Publication1
Binding sitei138Binds lipid L4 (in monomeric and oligomeric forms)1 Publication1
Binding sitei138Carbohydrate1 Publication1
Binding sitei144Binds lipid L5 (in monomeric and oligomeric forms)1 Publication1
Sitei149Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B)2 Publications1
Sitei163Part of the hydrophobic cavity (in subunit A) that receives Val-60 from the adjacent subunit (B)1 Publication1
Binding sitei168Binds bridging lipid L1 (subunit A) (in oligomeric forms, only); via amide nitrogen1 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 functionToxin
Biological processCytolysis, Hemolysis, Ion transport, Transport
LigandLipid-binding

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.C.38.1.8 the pore-forming equinatoxin (equinatoxin) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DELTA-actitoxin-Afr1a1 Publication
Short name:
DELTA-AITX-Afr1a1 Publication
Alternative name(s):
Alpha-helical pore-forming toxin3 Publications
Short name:
PFT3 Publications
Cytolysin1 Publication
Fragaceatoxin C4 Publications
Short name:
fraC4 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiActinia fragacea (Strawberry anemone)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri396334 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaActiniidaeActinia

<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

Membrane, Nematocyst, Secreted, Target cell membrane, Target membrane

<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 specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Has been engineered for DNA analysis in nanopore technology.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi8V → C in V8C/K69C; loss of ability to form stable pores after addition of a new disulfide bond. 1 Publication1
Mutagenesisi16F → A, G or P: Loss of pore formation ability in cholesterol-rich membranes, but does not change effect on membranes with low cholesterol content. 1 Publication1
Mutagenesisi60V → E: V60E/W149A; decrease in hemolytic activity, suggesting that this mutant forms functional but structurally weak pores. 1 Publication1
Mutagenesisi69K → C in V8C/K69C; loss of ability to form stable pores after addition of a new disulfide bond. 1 Publication1
Mutagenesisi112W → R in W112R/W116F; loss of ability to bind membranes. 1 Publication1
Mutagenesisi116W → F in W112R/W116F; loss of ability to bind membranes. 1 Publication1
Mutagenesisi149W → A in V60E/W149A; decrease in hemolytic activity, suggesting that this mutant forms functional but structurally weak pores. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003817301 – 179DELTA-actitoxin-Afr1a1 PublicationAdd BLAST179

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Octamer or nonamer in membranes (PubMed:21300287, PubMed:22728830, PubMed:25716479). Monomer in the soluble state (PubMed:21300287, PubMed:22728830, PubMed:25716479).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

B9W5G6
With#Exp.IntAct
itself2EBI-15910829,EBI-15910829

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-59108N

<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

1179
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

More...
SMRi
B9W5G6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
B9W5G6

<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 – 29N-terminal alpha-helix that contributes to the pore1 PublicationAdd BLAST29
Regioni105 – 120Trp-rich region, which is important for the binding to lipid membraneBy similarityAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi144 – 146Cell attachment siteSequence analysisBy similarity3

<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 N-terminal region, before the pore is formed, is bound to the lipid membrane. It partitions into the lipid-water interface and stabilizes the monomeric molecule on the membrane. Finally, it traverses the bilayer, thus forming the transmembrane pore.By similarity

<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

Keywords - Domaini

Transmembrane

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.270.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR009104 Anemon_actinoporin-like
IPR015926 Cytolysin/lectin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06369 Anemone_cytotox, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF63724 SSF63724, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

B9W5G6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
SADVAGAVID GAGLGFDVLK TVLEALGNVK RKIAVGIDNE SGKTWTAMNT
60 70 80 90 100
YFRSGTSDIV LPHKVAHGKA LLYNGQKNRG PVATGVVGVI AYSMSDGNTL
110 120 130 140 150
AVLFSVPYDY NWYSNWWNVR VYKGQKRADQ RMYEELYYHR SPFRGDNGWH
160 170
SRGLGYGLKS RGFMNSSGHA ILEIHVTKA
Length:179
Mass (Da):19,719
Last modified:September 1, 2009 - 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:i2BEBB150A05FFBEC
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 19719±3 Da. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
FM958450 mRNA Translation: CAX16792.1

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM958450 mRNA Translation: CAX16792.1

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
3LIMX-ray1.80A/B/C/D/E/F2-179[»]
3VWIX-ray1.70A/B/C/D1-179[»]
3W9PX-ray2.10A/B1-179[»]
3ZWGX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O1-179[»]
3ZWJX-ray2.37A/B/C/D/E/F/G/H/I1-179[»]
4TSLX-ray1.60A/B1-179[»]
4TSNX-ray1.57A/B/C/D1-179[»]
4TSOX-ray2.30A/B1-179[»]
4TSPX-ray2.15A/B1-179[»]
4TSQX-ray1.60A/B/C/D/E/F1-179[»]
4TSYX-ray3.14A/B/C/D1-179[»]
4WDCX-ray1.29A3-179[»]
5BPGX-ray2.14A/B/C/D1-179[»]
5GWFX-ray1.55A/B/C/D3-179[»]
SMRiB9W5G6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-59108N

Protein family/group databases

TCDBi1.C.38.1.8 the pore-forming equinatoxin (equinatoxin) family

Miscellaneous databases

EvolutionaryTraceiB9W5G6

Family and domain databases

Gene3Di2.60.270.20, 1 hit
InterProiView protein in InterPro
IPR009104 Anemon_actinoporin-like
IPR015926 Cytolysin/lectin
PfamiView protein in Pfam
PF06369 Anemone_cytotox, 1 hit
SUPFAMiSSF63724 SSF63724, 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 nameiACTPC_ACTFR
<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: B9W5G6
Secondary accession number(s): P86212
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: April 22, 2020
This is version 53 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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