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Entry version 149 (10 Feb 2021)
Sequence version 1 (01 Nov 1998)
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Protein

Peroxiredoxin tpx1

Gene

tpx1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
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 (PubMed:17409354, PubMed:20356456). Relays hydrogen peroxide as a signal to the transcription factor pap1 by inducing the formation of intramolecular disulfide bonds in pap1, which causes its nuclear accumulation and activation (PubMed:15824112, PubMed:24316080). Reduced by srx1 and this regulation acts as a molecular switch controlling the transcriptional response to hydrogen peroxide (PubMed:15956211).5 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 the typical 2-Cys AhpC/Prx1 family, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication

<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

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 sitei48Cysteine sulfenic acid (-SOH) intermediate1 Publication1

<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-SPO-3299685, Detoxification of Reactive Oxygen Species
R-SPO-5628897, TP53 Regulates Metabolic Genes
R-SPO-6798695, Neutrophil degranulation

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
4483, Spom2CysPrx

<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 tpx11 Publication (EC:1.11.1.241 Publication)
Alternative name(s):
Thioredoxin peroxidase1 Publication
Short name:
TPx1 Publication
Thioredoxin-dependent peroxiredoxin tpx1Curated
<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:tpx1
Synonyms:tsa1
ORF Names:SPCC576.03c
<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>OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
<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 identifieri284812 [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 lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
<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
  • UP000002485 <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 III

Organism-specific databases

Schizosaccharomyces pombe database

More...
PomBasei
SPCC576.03c, tpx1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:SPCC576.03c

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi48C → S: No nuclear accumulation of pap1. 1 Publication1
Mutagenesisi169C → S: No nuclear accumulation of pap1. 1 Publication1
Mutagenesisi191K → D: Peroxide reduction reduced. 1 Publication1
Mutagenesisi191K → R: Inactivated by 1 mM H(2)O(2). 1 Publication1
Mutagenesisi192H → E, G, K, L, Q or Y: Peroxide reduction reduced. 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 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_00003510761 – 192Peroxiredoxin tpx1Add BLAST192

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 bondi48Interchain (with C-169); in linked form1 Publication
<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 residuei105Phosphoserine1 Publication1
Modified residuei148Phosphoserine1 Publication1
Disulfide bondi169Interchain (with C-30 in TRX1); transient1 Publication
Disulfide bondi169Interchain (with C-48); in linked form1 Publication

<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. It can be reactivated by forming a transient disulfide bond with sulfiredoxin srx1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.2 Publications

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O74887

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

More...
PaxDbi
O74887

PRoteomics IDEntifications database

More...
PRIDEi
O74887

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O74887

<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

Homodimer; disulfide-linked, upon oxidation (PubMed:11795888, PubMed:20356456, PubMed:24316080).

Interacts with srx1 in response to oxidative stress (PubMed:15824112).

Interacts with pap1 via transient disulfide linkages (PubMed:24316080).

4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
276132, 19 interactors

Protein interaction database and analysis system

More...
IntActi
O74887, 3 interactors

Molecular INTeraction database

More...
MINTi
O74887

STRING: functional protein association networks

More...
STRINGi
4896.SPCC576.03c.1

<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
O74887

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>Domaini3 – 161ThioredoxinPROSITE-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_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O74887

Identification of Orthologs from Complete Genome Data

More...
OMAi
FWYPKDF

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O74887

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>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.

O74887-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLQIGKPAP DFKGTAVVNG AFEEIKLADY KGKWVFLGFY PLDFTFVCPT
60 70 80 90 100
EIVAFSEAAS KFAERNAQVI LTSTDSEYSH LAFINTPRKE GGLGGINIPL
110 120 130 140 150
LADPSHKVSR DYGVLIEDAG VAFRGLFLID PKGVLRQITI NDLPVGRSVD
160 170 180 190
EALRLLDAFQ FVEEHGEVCP ANWHKGSDTI DTKNPEKYFS KH
Length:192
Mass (Da):21,191
Last modified:November 1, 1998 - 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:i0DFE0C757C09A96B
GO

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
AF083335 mRNA Translation: AAC71013.1
CU329672 Genomic DNA Translation: CAA21182.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T41413

NCBI Reference Sequences

More...
RefSeqi
NP_588430.1, NM_001023421.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPCC576.03c.1; SPCC576.03c.1:pep; SPCC576.03c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2539572

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPCC576.03c

<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
AF083335 mRNA Translation: AAC71013.1
CU329672 Genomic DNA Translation: CAA21182.1
PIRiT41413
RefSeqiNP_588430.1, NM_001023421.2

3D structure databases

SMRiO74887
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi276132, 19 interactors
IntActiO74887, 3 interactors
MINTiO74887
STRINGi4896.SPCC576.03c.1

Protein family/group databases

PeroxiBasei4483, Spom2CysPrx

PTM databases

iPTMnetiO74887

Proteomic databases

MaxQBiO74887
PaxDbiO74887
PRIDEiO74887

Genome annotation databases

EnsemblFungiiSPCC576.03c.1; SPCC576.03c.1:pep; SPCC576.03c
GeneIDi2539572
KEGGispo:SPCC576.03c

Organism-specific databases

PomBaseiSPCC576.03c, tpx1
VEuPathDBiFungiDB:SPCC576.03c

Phylogenomic databases

eggNOGiKOG0852, Eukaryota
HOGENOMiCLU_042529_21_0_1
InParanoidiO74887
OMAiFWYPKDF
PhylomeDBiO74887

Enzyme and pathway databases

ReactomeiR-SPO-3299685, Detoxification of Reactive Oxygen Species
R-SPO-5628897, TP53 Regulates Metabolic Genes
R-SPO-6798695, Neutrophil degranulation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O74887

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

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 nameiTPX1_SCHPO
<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: O74887
<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: September 23, 2008
Last sequence update: November 1, 1998
Last modified: February 10, 2021
This is version 149 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 programFungal Protein 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

Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families
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