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Entry version 174 (29 Sep 2021)
Sequence version 1 (01 May 2000)
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Protein

Peroxiredoxin 1

Gene

Jafrac1

Organism
Drosophila melanogaster (Fruit fly)
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. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2 (By similarity).

Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).

By similarity

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). As a reducing substrate, thioredoxin 2 is preferred over thioredoxin 1 (PubMed:11877442).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei47Cysteine 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

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

Reactome - a knowledgebase of biological pathways and processes

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

<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:
Peroxiredoxin 1 (EC:1.11.1.241 Publication)
Alternative name(s):
Cytosolic thioredoxin peroxidase
Short name:
DPx-4783
Short name:
DmTPx-1
Thioredoxin peroxidase
Thioredoxin-dependent peroxiredoxin 1Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Jafrac1
Synonyms:TPX-1
ORF Names:CG1633
<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>OrganismiDrosophila melanogaster (Fruit fly)
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 X

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0040309, Jafrac1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
VectorBase:FBgn0040309

<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

Results in reduced resistance to oxidative stress (PubMed:26715182). Simultaneous knockout of Urm1 restores normal sensitivity to oxidative stress (PubMed:26715182).1 Publication

<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_00001350851 – 194Peroxiredoxin 1Add BLAST194

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 bondi47Interchain (with C-168); in linked formBy similarity
Disulfide bondi168Interchain (with C-47); in linked formBy similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei193Phosphothreonine1 Publication1
Modified residuei194Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.By similarity
Conjugated to URM1, a ubiquitin-like protein.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q9V3P0

PRoteomics IDEntifications database

More...
PRIDEi
Q9V3P0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9V3P0

<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 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

Highly expressed during embryogenesis, weakly expressed during larval stages.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0040309, Expressed in embryo and 51 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9V3P0, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9V3P0, DM

<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">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (By similarity).

Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity).

Interacts with SESN1 and SESN2 (By similarity).

By similarity

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
72802, 25 interactors

Database of interacting proteins

More...
DIPi
DIP-17916N

Protein interaction database and analysis system

More...
IntActi
Q9V3P0, 16 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0073594

<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
Q9V3P0

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_and_domains_section">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>Domaini2 – 160ThioredoxinPROSITE-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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_042529_21_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9V3P0

Identification of Orthologs from Complete Genome Data

More...
OMAi
CPLGWKP

Database of Orthologous Groups

More...
OrthoDBi
1326484at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9V3P0

Family and domain databases

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_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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9V3P0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPQLQKPAPA FAGTAVVNGV FKDIKLSDYK GKYLVLFFYP LDFTFVCPTE
60 70 80 90 100
IIAFSESAAE FRKINCEVIG CSTDSQFTHL AWINTPRKQG GLGSMDIPLL
110 120 130 140 150
ADKSMKVARD YGVLDEETGI PFRGLFIIDD KQNLRQITVN DLPVGRSVEE
160 170 180 190
TLRLVQAFQY TDKYGEVCPA NWKPGQKTMV ADPTKSKEYF ETTS
Length:194
Mass (Da):21,738
Last modified:May 1, 2000 - 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:i93ED319BE144E8D1
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
X2JF59X2JF59_DROME
Thioredoxin peroxidase 1, isoform C
Jafrac1 1633, cTPx, Dmel\CG1633, DmTPx-1, dPrx I
194Annotation score:

Annotation score:3 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF167098 mRNA Translation: AAF42985.1
AF321615 mRNA Translation: AAK06770.1
AF321616 mRNA Translation: AAK06771.1
AE014298 Genomic DNA Translation: AAF48253.1
AY070534 mRNA Translation: AAL48005.1
BT014630 mRNA Translation: AAT27254.1

NCBI Reference Sequences

More...
RefSeqi
NP_001285202.1, NM_001298273.1
NP_001285203.1, NM_001298274.1
NP_001285204.1, NM_001298275.1
NP_477510.1, NM_058162.3
NP_727689.1, NM_167359.2

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0073763; FBpp0073594; FBgn0040309
FBtr0073764; FBpp0073595; FBgn0040309
FBtr0339699; FBpp0308756; FBgn0040309
FBtr0339700; FBpp0308757; FBgn0040309
FBtr0345161; FBpp0311371; FBgn0040309

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
53578

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG1633

<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
AF167098 mRNA Translation: AAF42985.1
AF321615 mRNA Translation: AAK06770.1
AF321616 mRNA Translation: AAK06771.1
AE014298 Genomic DNA Translation: AAF48253.1
AY070534 mRNA Translation: AAL48005.1
BT014630 mRNA Translation: AAT27254.1
RefSeqiNP_001285202.1, NM_001298273.1
NP_001285203.1, NM_001298274.1
NP_001285204.1, NM_001298275.1
NP_477510.1, NM_058162.3
NP_727689.1, NM_167359.2

3D structure databases

SMRiQ9V3P0
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi72802, 25 interactors
DIPiDIP-17916N
IntActiQ9V3P0, 16 interactors
STRINGi7227.FBpp0073594

PTM databases

iPTMnetiQ9V3P0

Proteomic databases

PaxDbiQ9V3P0
PRIDEiQ9V3P0

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
53578

Genome annotation databases

EnsemblMetazoaiFBtr0073763; FBpp0073594; FBgn0040309
FBtr0073764; FBpp0073595; FBgn0040309
FBtr0339699; FBpp0308756; FBgn0040309
FBtr0339700; FBpp0308757; FBgn0040309
FBtr0345161; FBpp0311371; FBgn0040309
GeneIDi53578
KEGGidme:Dmel_CG1633

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
53578
FlyBaseiFBgn0040309, Jafrac1
VEuPathDBiVectorBase:FBgn0040309

Phylogenomic databases

eggNOGiKOG0852, Eukaryota
HOGENOMiCLU_042529_21_1_1
InParanoidiQ9V3P0
OMAiCPLGWKP
OrthoDBi1326484at2759
PhylomeDBiQ9V3P0

Enzyme and pathway databases

ReactomeiR-DME-3299685, Detoxification of Reactive Oxygen Species
R-DME-5628897, TP53 Regulates Metabolic Genes

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
53578, 0 hits in 3 CRISPR screens

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
53578

Protein Ontology

More...
PROi
PR:Q9V3P0

Gene expression databases

BgeeiFBgn0040309, Expressed in embryo and 51 other tissues
ExpressionAtlasiQ9V3P0, baseline and differential
GenevisibleiQ9V3P0, DM

Family and domain databases

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

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 nameiPRDX1_DROME
<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: Q9V3P0
Secondary accession number(s): Q0KHT0
<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: January 10, 2003
Last sequence update: May 1, 2000
Last modified: September 29, 2021
This is version 174 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 programDrosophila 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. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families
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