UniProtKB - A0A2L0ART2 (TXF1A_SCOSU)
(max 400 entries)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
>sp|A0A2L0ART2|TXF1A_SCOSU Mu-scoloptoxin(15)-Ssm1a OS=Scolopendra subspinipes OX=55038 PE=1 SV=1 MEKKIIFLVFLVALLALPGFISTEVIKKDTPYKKRKFPYKSECLKACATSFTGGDESRIQ EGKPGFFKCTCYFTTGCommunity curation ()Add a publicationFeedback
Protein
Mu-scoloptoxin(15)-Ssm1a
Gene
N/A
Organism
Scolopendra subspinipes (Vietnamese centipede)
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>Select a section on the left to see content.
<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
Blocks voltage-gated potassium channels Kv7.4/KCNQ4 (IC50=2.5 µM), Kv7.1/KCNQ1 (IC50=2.8 µM), Kv7.2/KCNQ2 (IC50=2.7 µM) and Kv7.5/KCNQ5 (IC50=2.7 µM). Targets the pore domain, in particular negatively charged residues 'Asp-266' and 'Asp-288', of KCNQ4 and probably other KCNQ channel family members where these residues are conserved. In vivo, shows vasoconstrictive activity resulting in acute hypertension when injected intravenously in mice. Also induces coronary vasospasms ultimately leading to heart failure. Induces seizures when injected into the hippocampus of mice. Decreases respiratory rate while increasing respiratory amplitude, probably by triggering a contraction of the bronchial ring.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
Miscellaneous
Does not inhibit channels TRPV1 and TRPV2, voltage-gated potassium channels Kv2.1/KCNB1 and Kv4.1/KCND1, hERG, tetrodotoxin (TTX)-sensitive and TTX-insensitive sodium channels in DRG neurons or voltage-gated calcium channels in DRG neurons.1 Publication
Manual assertion based on experiment ini
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Sitei | 27 | Important for inhibition of KCNQ41 Publication Manual assertion based on experiment ini
| 1 | |
| Sitei | 68 | Important for inhibition of KCNQ41 Publication Manual assertion based on experiment ini
| 1 |
<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
- toxin activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
GO - Biological processi
- envenomation resulting in positive regulation of blood pressure in other organism Source: UniProtKBInferred from direct assayi
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
- negative regulation of voltage-gated potassium channel activity Source: UniProtKBInferred from direct assayi
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
- positive regulation of vasoconstriction Source: UniProtKBInferred from direct assayi
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
<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 function | Ion channel impairing toxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium 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%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: Mu-scoloptoxin(15)-Ssm1aCuratedShort name: Mu-SLPTX(15)-Ssm1aCurated Alternative name(s): Potassium channel toxin SsTx1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Ssm spooky toxin1 Publication Manual assertion based on opinion ini
|
| <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>Organismi | Scolopendra subspinipes (Vietnamese centipede) |
| <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 identifieri | 55038 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Myriapoda › Chilopoda › Pleurostigmophora › Epimorpha › Scolopendromorpha › Scolopendridae › Scolopendra |
<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
- Secreted 1 Publication
Manual assertion based on experiment ini
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKBInferred from direct assayi
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
- extracellular region Source: UniProtKBInferred from direct assayi
Keywords - Cellular componenti
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%5Fand%5Fbiotech%5Fsection">'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 0.85 mg/kg when injected intravenously in mice.1 Publication
Manual assertion based on experiment ini
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 27 | K → A: Reduced inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 28 | K → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 29 | D → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 33 | K → A: Reduced inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 34 | K → A: Reduced inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 35 | R → A: Severely reduced inhibition of KCNQ4 (IC(50)=104.7 uM). 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 35 | R → K: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 36 | K → A: Severaly reduced inhibition of KCNQ4 (IC(50)=117.5 uM). 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 36 | K → R: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 40 | K → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 42 | E → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 45 | K → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 55 | D → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 56 | E → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 58 | R → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 61 | E → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 63 | K → A: No effect on inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 68 | K → A: Reduced inhibition of KCNQ4. 1 Publication Manual assertion based on experiment ini
| 1 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 23 | 1 Publication Manual assertion based on experiment ini
| 23 | |
| <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_0000444563 | 24 – 76 | Mu-scoloptoxin(15)-Ssm1a1 Publication Manual assertion based on experiment ini
| 53 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bondi | 43 ↔ 69 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 47 ↔ 71 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
|
Keywords - PTMi
Disulfide bond<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Expressed by the venom gland.1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 27 – 31 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 41 – 49 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 53 – 56 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 60 – 62 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 68 – 73 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | A0A2L0ART2 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 33 – 36 | Important for inhibition of KCNQ41 Publication Manual assertion based on experiment ini
| 4 |
<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
Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta). Since the toxin contains only 2 disulfide bonds, it is called 2ds-CSalpha/beta.1 Publication
Manual assertion based on experiment ini
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
<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
Belongs to the scoloptoxin-15 family.Curated
Keywords - Domaini
Signal<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.
<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
A0A2L0ART2-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MEKKIIFLVF LVALLALPGF ISTEVIKKDT PYKKRKFPYK SECLKACATS
60 70
FTGGDESRIQ EGKPGFFKCT CYFTTG
Length:76
Mass (Da):8,568
Last modified:April 25, 2018 - 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:i92484A9A32ADECB2
<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 6017.5 Da. Determined by MALDI. 1 Publication
Manual assertion based on experiment ini
- Ref.1"Centipedes subdue giant prey by blocking KCNQ channels."
Luo L., Li B., Wang S., Wu F., Wang X., Liang P., Ombati R., Chen J., Lu X., Cui J., Lu Q., Zhang L., Zhou M., Tian C., Yang S., Lai R.
Proc. Natl. Acad. Sci. U.S.A. 115:1646-1651(2018) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-76, STRUCTURE BY NMR OF 24-76, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, TOXIC DOSE, DISULFIDE BONDS, MUTAGENESIS OF LYS-27; LYS-28; ASP-29; LYS-33; LYS-34; ARG-35; LYS-36; LYS-40; GLU-42; LYS-45; ASP-55; GLU-56; ARG-58; GLU-61; LYS-63 AND LYS-68.
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | MG585384 mRNA Translation: AUW64492.1 |
<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
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| A0A2L0ART2 | Omega-scoloptoxin(15)-Ssd3c | 76 | UniRef50_A0A2L0ART2 | |||
| U-scoloptoxin(15)-Sm3a | 73 | |||||
| U-scoloptoxin(15)-Ssd3b | 76 | |||||
| Kappa-scoloptoxin(15)-Ssd3a | 76 | |||||
| +1 | ||||||
<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 | MG585384 mRNA Translation: AUW64492.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 5X0S | NMR | - | A | 24-76 | [»] | |
| SMRi | A0A2L0ART2 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Family and domain databases
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 namei | TXF1A_SCOSU | |
| <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>Accessioni | A0A2L0ART2Primary (citable) accession number: A0A2L0ART2 Secondary accession number(s): A0A2R2JFU4, C0HKE0 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | June 20, 2018 |
| Last sequence update: | April 25, 2018 | |
| Last modified: | April 22, 2020 | |
| This is version 10 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Animal 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 sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
