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Entry version 70 (08 May 2019)
Sequence version 1 (01 Mar 2004)
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Protein

Psalmotoxin-1

Gene
N/A
Organism
Psalmopoeus cambridgei (Trinidad chevron tarantula)
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

This toxin is a gating modifier that acts principally as an inhibitor on ASIC1a (ASIC isoform 2) and a potentiator on ASIC1b (ASIC isoform 3) (PubMed:10829030, PubMed:15955877, PubMed:21036899). This toxin potently and selectively inhibits rat, mouse and human ASIC1a (IC50=0.35-3.7 nM) (PubMed:10829030, PubMed:15955877, PubMed:21715637, PubMed:26248594, PubMed:21825095). The blockade is rapidly reversible (PubMed:10829030, PubMed:28320941). The toxin acts by shifting its steady-state desensitization to more alkaline pH (0.27 pH unit) (PubMed:15955877, PubMed:16505147). At higher concentrations, it potentiates rat and human ASIC1b and activates chicken ASIC1 by stabilizing the open state of these subtypes (PubMed:16505147, PubMed:21036899, PubMed:19185346, PubMed:24262969, PubMed:22842900). The toxin binds most tightly to the open and the desensitized states of ASIC1a (promoting desensitization), whereas it binds most tightly to the open state of ASIC1b (promoting opening) (PubMed:16505147). The toxin also inhibits mouse ASIC1a-ASIC2b (IC50=2.64 nM) and rat ASIC1a-ASIC2a (PubMed:21715637, PubMed:27277303). It binds to the extracellular domain at subunit interfaces in the acidic pocket with the majority of contacts on the thumb domain of the channel (PubMed:21825095, PubMed:22842900, PubMed:22760635). It is also noteworthy that calcium competes with the toxin, probably by inhibiting binding of the toxin to the channel (PubMed:15955877).13 Publications

Miscellaneous

This peptide is present at only 0.4% abundance in P.cambridgei venom.1 Publication
Does not act on rat and mouse ASIC1a-ASIC2a (PubMed:10829030, PubMed:21715637). Does not act on rat ASIC1a-ASIC3 (PubMed:10829030).2 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>Sitei7Key residue for interaction with ASIC1a3 Publications1
Sitei24Key residue for interaction with ASIC1a3 Publications1
Sitei26Key residue for interaction with ASIC1a3 Publications1
Sitei27Key residue for interaction with ASIC1a3 Publications1
Sitei28Key residue for interaction with ASIC1a3 Publications1
Sitei30Key residue for interaction with ASIC1a3 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel impairing toxin, Proton-gated sodium channel impairing toxin, Toxin

Protein family/group databases

Transport Classification Database

More...
TCDBi
8.B.10.1.1 the psalmotoxin-1 (pctx1) family

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Psalmotoxin-14 Publications
Alternative name(s):
PcTx12 Publications
Pi-theraphotoxin-Pc1a1 Publication
Short name:
Pi-TRTX-Pc1a1 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>OrganismiPsalmopoeus cambridgei (Trinidad chevron tarantula)
<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 identifieri179874 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeTheraphosidaePsalmopoeus

Organism-specific databases

ArachnoServer: Spider toxin database

More...
ArachnoServeri
AS000400 pi-theraphotoxin-Pc1a

<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

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 ‘Pathology and Biotech’ section describes the use of a protein as a pharmaceutical drug. It indicates the name of the drug, the name of the firm that commercializes it and explains in a few words in which context the drug is used. In some cases, drugs that are under development are also described.<p><a href='/help/pharmaceutical_use' target='_top'>More...</a></p>Pharmaceutical usei

This toxin has been shown to be neuroprotective in both rodent and porcine models of cerebral ischemia when administered 30 minutes prior to induction of stroke (PubMed:28457973). In addition, a single dose of this toxin (1 ng/kg, i.c.v. 2 h post stroke) does indeed provide substantial neuronal and functional protection in ischemic stroke in conscious hypertensive rats (PubMed:26320544).2 Publications

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>Mutagenesisi1 – 2Missing : 1.6-fold decrease in ability to inhibit rASIC1a channel. 1 Publication2
Mutagenesisi6K → A: 97.7-fold decrease in ability to inhibit rASIC1a channel, probably due to structural perturbations. 1 Publication1
Mutagenesisi7W → A: Complete loss in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi8K → A: 1.7-fold decrease in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi14H → A: No change in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi24W → A: 170-fold decrease in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi25K → A: No change in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi26R → A: Loss of ability to inhibit rASIC1a at low concentration and gain of function as a positive modulator at high concentrations (>100 nM), probably by stabilizing the open state of the channel. 1 Publication1
Mutagenesisi27R → A: 165-fold decrease in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi28R → A: 14.5-fold decrease in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi29S → A: Does not significantly modify the ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi30F → A: Loss of ability to inhibit rASIC1a at low concentration and gain of function as a positive modulator at high concentrations, probably by stabilizing the open state of the channel. 1 Publication1
Mutagenesisi31E → A: 2.2-fold decrease in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi32V → A: 17.9-fold decrease in ability to inhibit rASIC1a channel, probably due to structural perturbations. 1 Publication1
Mutagenesisi34V → A: 1.4-fold decrease in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi35P → A: 2.7-fold increase in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi36K → A: 1.8-fold increase in ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi37T → A: Does not significantly modify the ability to inhibit rASIC1a channel. 1 Publication1
Mutagenesisi38 – 40Missing : 4.1-fold decrease in ability to inhibit rASIC1a channel, probably due to the deletion of P-38. 1 Publication3
Mutagenesisi38P → A: 3.9-fold decrease in ability to inhibit rASIC1a channel. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_00000449651 – 40Psalmotoxin-11 PublicationAdd BLAST40

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 bondi3 ↔ 184 PublicationsImported
Disulfide bondi10 ↔ 234 PublicationsImported
Disulfide bondi17 ↔ 334 PublicationsImported

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>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_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ASIC1Q1XA762EBI-16002043,EBI-15659618From Gallus gallus.

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-59909N

Protein interaction database and analysis system

More...
IntActi
P60514, 1 interactor

<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

140
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P60514

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P60514

<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

<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 presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.4 Publications

<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 psalmotoxin-1 family.Curated

Keywords - Domaini

Knottin

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

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

P60514-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40
EDCIPKWKGC VNRHGDCCEG LECWKRRRSF EVCVPKTPKT
Length:40
Mass (Da):4,695
Last modified:March 1, 2004 - 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:iA52DC98962D9598C
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 4689.25 Da from positions 1 - 40. Determined by MALDI. 1 Publication
Molecular mass is 4690 Da from positions 1 - 40. Determined by MALDI. 1 Publication

<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

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

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LMMNMR-A1-40[»]
2KNINMR-A1-40[»]
3S3XX-ray2.99D/E/F2-38[»]
4FZ0X-ray2.80M/N/O1-40[»]
4FZ1X-ray3.36D1-40[»]
SMRiP60514
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-59909N
IntActiP60514, 1 interactor

Protein family/group databases

TCDBi8.B.10.1.1 the psalmotoxin-1 (pctx1) family

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ArachnoServeriAS000400 pi-theraphotoxin-Pc1a

Miscellaneous databases

EvolutionaryTraceiP60514

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 nameiTXP1_PSACA
<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: P60514
<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: March 1, 2004
Last sequence update: March 1, 2004
Last modified: May 8, 2019
This is version 70 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, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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