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Entry version 39 (02 Jun 2021)
Sequence version 1 (11 Nov 2015)
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Protein

Peroxiredoxin prdx-2

Gene

prdx-2

Organism
Caenorhabditis elegans
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

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15099742).

In I2 pharyngeal neurons, required for the inhibition of feeding in response to light and hydrogen peroxide (PubMed:25640076).

In the intestine, plays a role in protecting cells against oxidative stress by detoxifying peroxides such as hydrogen peroxide (PubMed:15099742, PubMed:19064914, PubMed:20649472).

In addition, plays a role in the recovery from oxidative stress induced by hydrogen peroxide (PubMed:20649472).

In its hyperoxidized form (induced by hydrogen peroxide), confers protection against heat stress (PubMed:19064914).

However, has a low tendency for overoxidation during the normal lifespan (PubMed:20964547).

Increases sensitivity to cytotoxity caused by metalloids and heavy metals such as arsenic and cadmium by playing a role in inhibiting the expression of phase II detoxification genes such as gcs-1 in intestinal cells (PubMed:19064914, PubMed:25204677).

In addition, in response to arsenite, promotes the secretion of the insulin ligand daf-28 into the pseudocoelom, which negatively regulates the activities of daf-16 and skn-1 (PubMed:25808059).

Plays a role in promoting longevity (PubMed:19064914, PubMed:24889636).

Plays a role in the mitohormetic pathway by promoting the activation of pmk-1 in response to the drug metformin (PubMed:24889636).

8 Publications

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated following oxidation of the conserved redox-active cysteine residue, which subsequently allows for the oxidation and activation of substrates.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei55Cysteine sulfenic acid (-SOH) intermediateBy similarity1

<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

  • thioredoxin peroxidase activity Source: WormBase

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 functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.11.1.24, 1045

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-3299685, Detoxification of Reactive Oxygen Species
R-CEL-5628897, TP53 Regulates Metabolic Genes

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
4485, Cel2CysPrx02

<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:
Peroxiredoxin prdx-2Curated (EC:1.11.1.241 Publication)
Alternative name(s):
2-Cys peroxiredoxin 21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:prdx-2Imported
Synonyms:prx21 Publication, tag-56Imported
ORF Names:F09E5.15Imported
<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>OrganismiCaenorhabditis elegansImported
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome II

Organism-specific databases

WormBase

More...
WormBasei
F09E5.15a ; CE32361 ; WBGene00006434 ; prdx-2
F09E5.15b ; CE41559 ; WBGene00006434 ; prdx-2
F09E5.15c ; CE50863 ; WBGene00006434 ; prdx-2

<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

Keywords - Cellular componenti

Cytoplasm

<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 in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Reduced size, egg production and brood size (PubMed:15099742). Survival in response to heat and oxidative stress induced by peroxides is comparable to wild-type (PubMed:15099742). RNAi-mediated knockdown increases lifespan in response to the heavy metal arsenite (PubMed:25808059). RNAi-mediated knockdown increases expression of gcs-1 and further increases gcs-1 expression in response to the heavy metal arsenite (PubMed:19064914). RNAi-mediated knockdown increases the expression of isoform a of skn-1 in intestinal nuclei (PubMed:25808059).3 Publications

<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_00004508621 – 201Peroxiredoxin prdx-2Add BLAST201

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 bondi55Interchain (with C-176); in linked formBy similarity
Disulfide bondi176Interchain (with C-55); in linked formBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond.By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8IG31

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
H2KZL7

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0020:Q8IG31

<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 in the gonad, neurons and intestine (at protein level) (PubMed:19064914). Expressed in the pharyngeal inter-neuron I4 and the sensory interneuron I2 (PubMed:15099742, PubMed:25640076). Expressed in the intestine, pharyngeal muscle 1, vulval muscle, body wall muscle, epithelial cells e1 and e3, and neurons in the head and tail (PubMed:25640076).3 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed throughout embryonic, larval and adult stages (PubMed:15099742, PubMed:19064914). Highly expressed at the L3 larval stage at 25 degrees Celsius (PubMed:29055282).3 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in response to the drug metformin.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00006434, Expressed in multi-cellular organism and 5 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
A0A0K3AUJ9, baseline and differential

<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

Monomer and homodimer; disulfide-linked (PubMed:19064914). Under nonstress conditions, present in the reduced monomeric form (PubMed:19064914).

Forms active hyperoxidized monomers and disulfide-linked homodimers upon oxidation by hydrogen peroxide (PubMed:19064914).

Forms active oxidized homodimers in response to the drug metformin (PubMed:24889636).

2 Publications

<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

3D structure databases

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

More...
SMRi
A0A0K3AUJ9

Database of comparative protein structure models

More...
ModBasei
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini10 – 168ThioredoxinPROSITE-ProRule annotationAdd BLAST159

<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

Redox-active center

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0852, Eukaryota
COG0450, LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_042529_21_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
H2KZL7

Identification of Orthologs from Complete Genome Data

More...
OMAi
FWYPKDF

Database of Orthologous Groups

More...
OrthoDBi
1326484at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.30.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000866, AhpC/TSA
IPR024706, Peroxiredoxin_AhpC-typ
IPR019479, Peroxiredoxin_C
IPR036249, Thioredoxin-like_sf
IPR013766, Thioredoxin_domain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10417, 1-cysPrx_C, 1 hit
PF00578, AhpC-TSA, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000239, AHPC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52833, SSF52833, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51352, THIOREDOXIN_2, 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>Sequences (3)i

<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.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform cImported (identifier: A0A0K3AUJ9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSLAPKMSKA FIGKPAPQFK TQAVVDGEFV DVSLSDYKGK YVVLFFYPLD
60 70 80 90 100
FTFVCPTEII AFSDRAEEFK AINTVVLAAS TDSVFSHLAW INQPRKHGGL
110 120 130 140 150
GEMNIPVLAD TNHQISRDYG VLKEDEGIAF RGLFIIDPSQ NLRQITINDL
160 170 180 190 200
PVGRSVDETL RLVQAFQFVE KHGEVCPAGW TPGSDTIKPG VKESQEYFKK

H
Length:201
Mass (Da):22,413
Last modified:November 11, 2015 - 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:i3E0DD7ECF8C32FC4
GO
Isoform aImported (identifier: A0A0K3AUJ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.

Show »
Length:195
Mass (Da):21,785
Checksum:i493A2E078D016068
GO
Isoform bImported (identifier: A0A0K3AUJ9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MSLAPK → MYRQ

Show »
Length:199
Mass (Da):22,363
Checksum:iD0B8184DF01AA418
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0607341 – 6Missing in isoform a. Curated6
Alternative sequenceiVSP_0607351 – 6MSLAPK → MYRQ in isoform b. Curated6

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
BX284602 Genomic DNA Translation: CCD68767.1
BX284602 Genomic DNA Translation: CCD68770.1
BX284602 Genomic DNA Translation: CTQ86475.1

NCBI Reference Sequences

More...
RefSeqi
NP_001122604.1, NM_001129132.2
NP_001300536.1, NM_001313607.1 [A0A0K3AUJ9-1]
NP_872052.1, NM_182252.5

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
F09E5.15a.1; F09E5.15a.1; WBGene00006434 [A0A0K3AUJ9-2]
F09E5.15a.2; F09E5.15a.2; WBGene00006434 [A0A0K3AUJ9-2]
F09E5.15b.1; F09E5.15b.1; WBGene00006434 [A0A0K3AUJ9-3]
F09E5.15c.1; F09E5.15c.1; WBGene00006434 [A0A0K3AUJ9-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
266858

UCSC genome browser

More...
UCSCi
F09E5.15b.1, c. elegans

Keywords - Coding sequence diversityi

Alternative splicing

<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
BX284602 Genomic DNA Translation: CCD68767.1
BX284602 Genomic DNA Translation: CCD68770.1
BX284602 Genomic DNA Translation: CTQ86475.1
RefSeqiNP_001122604.1, NM_001129132.2
NP_001300536.1, NM_001313607.1 [A0A0K3AUJ9-1]
NP_872052.1, NM_182252.5

3D structure databases

SMRiA0A0K3AUJ9
ModBaseiSearch...

Protein family/group databases

PeroxiBasei4485, Cel2CysPrx02

2D gel databases

World-2DPAGEi0020:Q8IG31

Proteomic databases

EPDiQ8IG31
PaxDbiH2KZL7

Genome annotation databases

EnsemblMetazoaiF09E5.15a.1; F09E5.15a.1; WBGene00006434 [A0A0K3AUJ9-2]
F09E5.15a.2; F09E5.15a.2; WBGene00006434 [A0A0K3AUJ9-2]
F09E5.15b.1; F09E5.15b.1; WBGene00006434 [A0A0K3AUJ9-3]
F09E5.15c.1; F09E5.15c.1; WBGene00006434 [A0A0K3AUJ9-1]
GeneIDi266858
UCSCiF09E5.15b.1, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
266858
WormBaseiF09E5.15a ; CE32361 ; WBGene00006434 ; prdx-2
F09E5.15b ; CE41559 ; WBGene00006434 ; prdx-2
F09E5.15c ; CE50863 ; WBGene00006434 ; prdx-2

Phylogenomic databases

eggNOGiKOG0852, Eukaryota
COG0450, LUCA
HOGENOMiCLU_042529_21_1_1
InParanoidiH2KZL7
OMAiFWYPKDF
OrthoDBi1326484at2759

Enzyme and pathway databases

BRENDAi1.11.1.24, 1045
ReactomeiR-CEL-3299685, Detoxification of Reactive Oxygen Species
R-CEL-5628897, TP53 Regulates Metabolic Genes

Gene expression databases

BgeeiWBGene00006434, Expressed in multi-cellular organism and 5 other tissues
ExpressionAtlasiA0A0K3AUJ9, baseline and differential

Family and domain databases

Gene3Di3.40.30.10, 1 hit
InterProiView protein in InterPro
IPR000866, AhpC/TSA
IPR024706, Peroxiredoxin_AhpC-typ
IPR019479, Peroxiredoxin_C
IPR036249, Thioredoxin-like_sf
IPR013766, Thioredoxin_domain
PfamiView protein in Pfam
PF10417, 1-cysPrx_C, 1 hit
PF00578, AhpC-TSA, 1 hit
PIRSFiPIRSF000239, AHPC, 1 hit
SUPFAMiSSF52833, SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS51352, THIOREDOXIN_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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<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 nameiPRDX_CAEEL
<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: A0A0K3AUJ9
Secondary accession number(s): H2KZL7, Q8IG31
<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: October 7, 2020
Last sequence update: November 11, 2015
Last modified: June 2, 2021
This is version 39 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 programCaenorhabditis annotation project

<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

Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families
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