UniProtKB - P61914 (ACTP2_ACTEQ)

>sp|P61914|ACTP2_ACTEQ DELTA-actitoxin-Aeq1a OS=Actinia equina OX=6106 PE=1 SV=1
MSRLIIVFIVVTMICSATALPSKKIIDEDEEDEKRSADVAGAVIDGASLSFDILKTVLEA
LGNVKRKIAVGVDNESGKTWTALNTYFRSGTSDIVLPHKVPHGKALLYNGQKDRGPVATG
AVGVLAYLMSDGNTLAVLFSVPYDYNWYSNWWNVRIYKGKRRADQRMYEELYYNLSPFRG
DNGWHTRNLGYGLKSRGFMNSSGHAILEIHVSKA

Entry version 85 (20 Dec 2017)
Sequence version 1 (07 Jun 2004)
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Protein

DELTA-actitoxin-Aeq1a

Gene

N/A

Organism

Actinia equina (Beadlet anemone)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. 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 several monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.

Miscellaneous

The discrimination between sphingomyelin and phosphatidylcholine occurs in the region directly below the phosphorylcholine headgroup.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	89	PhosphocholineBy similarity	1
Binding siteⁱ	122	PhosphocholineBy similarity	1
Binding siteⁱ	140	PhosphocholineBy similarity	1
Binding siteⁱ	142	PhosphocholineBy similarity	1
Siteⁱ	147	Important in the initial contact with the lipid membrane	1
Siteⁱ	148	Important in the initial contact with the lipid membrane	1
Binding siteⁱ	168	PhosphocholineBy similarity	1
Binding siteⁱ	172	PhosphocholineBy similarity	1
Binding siteⁱ	173	PhosphocholineBy similarity	1
Siteⁱ	179	Interacts with the lipid membrane	1
Siteⁱ	195	Interacts with the lipid membrane	1

GO - Molecular functionⁱ

channel activity Source: InterPro
toxin activity Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cation transport Source: InterPro
hemolysis in other organism involved in symbiotic interaction Source: InterPro
pore complex assembly Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Toxin
Biological process	Cytolysis, Hemolysis, Ion transport, Transport

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DELTA-actitoxin-Aeq1a1 Publication Short name: DELTA-AITX-Aeq1a1 Publication Alternative name(s): Equinatoxin II1 Publication Short name: EqT II1 Publication Short name: EqTII1 Publication Equinatoxin-2Curated
Organismⁱ	Actinia equina (Beadlet anemone)
Taxonomic identifierⁱ	6106 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Cnidaria › Anthozoa › Hexacorallia › Actiniaria › Actiniidae › Actinia

Keywords - Cellular componentⁱ

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

Pathology & Biotechⁱ

Toxic doseⁱ

LD₅₀ is 35 µg/kg by intravenous injection into mice.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	80	W → F: Expressed only 7% of the wild-type hemolytic activity. 1 Publication	1
Mutagenesisⁱ	147	W → A: Inhibition of direct binding of sphingomyelin. 1 Publication	1
Mutagenesisⁱ	148	Y → A: Inhibition of direct binding of sphingomyelin. 1 Publication	1
Mutagenesisⁱ	151 – 152	WW → FF: Expressed only 31% of the wild-type hemolytic activity. 1 Publication	2
Mutagenesisⁱ	184	W → F: Expressed only 2% of the wild-type hemolytic activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 19	Sequence analysisAdd BLAST	19
PropeptideⁱPRO_0000034830	20 – 35	2 PublicationsAdd BLAST	16
ChainⁱPRO_0000034831	36 – 214	DELTA-actitoxin-Aeq1a1 PublicationAdd BLAST	179

Keywords - PTMⁱ

Cleavage on pair of basic residues

Interactionⁱ

Subunit structureⁱ

Tetramer in the presence of a lipidic interface. Monomer, in soluble state.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	43 – 45	Combined sources	3
Helixⁱ	46 – 48	Combined sources	3
Helixⁱ	51 – 60	Combined sources	10
Beta strandⁱ	65 – 78	Combined sources	14
Beta strandⁱ	80 – 89	Combined sources	10
Beta strandⁱ	98 – 100	Combined sources	3
Beta strandⁱ	104 – 111	Combined sources	8
Beta strandⁱ	114 – 116	Combined sources	3
Beta strandⁱ	121 – 129	Combined sources	9
Beta strandⁱ	134 – 141	Combined sources	8
Turnⁱ	145 – 147	Combined sources	3
Beta strandⁱ	151 – 159	Combined sources	9
Helixⁱ	165 – 173	Combined sources	9
Beta strandⁱ	181 – 190	Combined sources	10
Beta strandⁱ	193 – 199	Combined sources	7
Beta strandⁱ	201 – 213	Combined sources	13

Show more details

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1IAZ	X-ray	1.90	A/B	36-214	[»]
	1KD6	NMR	-	A	36-214	[»]
	1TZQ	X-ray	2.30	A	40-214	[»]
ProteinModelPortalⁱ	P61914
SMRⁱ	P61914
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P61914

EvolutionaryTraceⁱ

P61914

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	38 – 47	Plays an important role in the hemolytic activityBy similarity	10
Regionⁱ	46 – 65	N-terminal regionAdd BLAST	20
Regionⁱ	140 – 155	Trp-rich regionAdd BLAST	16

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	179 – 181	Cell attachment siteSequence analysis		3

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.1 Publication

The Trp-rich region is important for the binding to lipid membrane.1 Publication

Sequence similaritiesⁱ

Belongs to the actinoporin family. Sea anemone subfamily.Curated

Keywords - Domainⁱ

Signal, Transmembrane

Family and domain databases

Gene3Dⁱ	2.60.270.20, 1 hit
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
SUPFAMⁱ	SSF63724 SSF63724, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P61914-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSRLIIVFIV VTMICSATAL PSKKIIDEDE EDEKRSADVA GAVIDGASLS 
        60         70         80         90        100
FDILKTVLEA LGNVKRKIAV GVDNESGKTW TALNTYFRSG TSDIVLPHKV 
       110        120        130        140        150
PHGKALLYNG QKDRGPVATG AVGVLAYLMS DGNTLAVLFS VPYDYNWYSN 
       160        170        180        190        200
WWNVRIYKGK RRADQRMYEE LYYNLSPFRG DNGWHTRNLG YGLKSRGFMN 
       210 
SSGHAILEIH VSKA

Length:214

Mass (Da):23,796

Last modified:June 7, 2004 - v1

Checksum:ⁱ182AD60801E41DF4

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱ	116	P → D.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U41661 mRNA Translation: AAC47005.1
PIRⁱ	JC4682

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P61914	DELTA-actitoxin-Ate1a		ACTTE		179	UniRef100_P61914

Protein	Similar proteins		Species	Score	Length	Source
P61914	DELTA-actitoxin-Ate1a		ACTTE		179	UniRef90_P61914
UPI0000112132		ACTEQ		179
UPI0000441F76		ACTEQ		175

Protein	Similar proteins		Species	Score	Length	Source
P61914	DELTA-actitoxin-Ate1a		ACTTE		179	UniRef50_P61914
DELTA-actitoxin-Ucs1a		URTCR		221
Cytolysin		ANESU		203
Actinoporin (Fragment)		EPIJA		225
Actinoporin (Fragment)		HETCR		225
+90

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U41661 mRNA Translation: AAC47005.1
PIRⁱ	JC4682

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1IAZ	X-ray	1.90	A/B	36-214	[»]
	1KD6	NMR	-	A	36-214	[»]
	1TZQ	X-ray	2.30	A	40-214	[»]
ProteinModelPortalⁱ	P61914
SMRⁱ	P61914
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P61914

EvolutionaryTraceⁱ

P61914

Family and domain databases

Gene3Dⁱ	2.60.270.20, 1 hit
InterProⁱ	View protein in InterPro IPR009104 Anemon_actinoporin-like IPR015926 Cytolysin/lectin
Pfamⁱ	View protein in Pfam PF06369 Anemone_cytotox, 1 hit
SUPFAMⁱ	SSF63724 SSF63724, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACTP2_ACTEQ
Accessionⁱ	P61914Primary (citable) accession number: P61914 Secondary accession number(s): P17723 , Q16993, Q9TWV2, Q9TWV3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
	Last sequence update:	June 7, 2004
	Last modified:	December 20, 2017
	This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Animal Toxin Annotation Program

UniProtKB

UniParc

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Annotation systems

Supporting data

UniProtKB - P61914 (ACTP2_ACTEQ)

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DELTA-actitoxin-Aeq1a

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<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

Miscellaneous

Sites

<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>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 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

Other locations

Extracellular region or secreted

Other locations

Keywords - Cellular componenti

<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

<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

Keywords - PTMi

<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 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

3D structure databases

Miscellaneous databases

<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

Motif

<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

Family and domain databases

Natural variant

Sequence databases

<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

3D structure databases

Protocols and materials databases

Miscellaneous databases

Family and domain databases

<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 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ