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Entry version 144 (12 Aug 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Peroxiredoxin-6

Gene

PRDX6

Organism
Bos taurus (Bovine)
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. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis.3 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 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. C(P) is reactivated by glutathionylation mediated by glutathione S-transferase Pi, followed by spontaneous reduction of the enzyme with glutathione.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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Note: Does not need Ca2+ as cofactor.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=25 µM for H2O21 Publication
  2. KM=180 µM for H2O21 Publication
  3. KM=22 µM for tert-butyl hydroperoxide1 Publication
  4. KM=142 µM for tert-butyl hydroperoxide1 Publication
  5. KM=170 µM for cumene hydroperoxide1 Publication
  6. KM=120 µM for cumene hydroperoxide1 Publication
  7. KM=12 µM for triphenylcarbinyl hydroperoxide1 Publication
  8. KM=34 µM for linoleic hydroperoxide1 Publication
  9. KM=141 µM for linolenoyl hydroperoxide1 Publication
  10. KM=135 µM for arachidonoyl hydroperoxide1 Publication
  11. KM=120 µM for PLCP hydroperoxide1 Publication
  12. KM=129 µM for PACP hydroperoxide1 Publication
  13. KM=22 µM for 5-phenyl-3-pentenyl hydroperoxide1 Publication
  14. KM=350 µM for dipalmitoyl phosphatidylcholine (at pH 4)1 Publication
  1. Vmax=5.07 µmol/min/mg enzyme for H2O21 Publication
  2. Vmax=1810 nmol/min/mg enzyme for H2O21 Publication
  3. Vmax=8.56 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
  4. Vmax=1270 nmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
  5. Vmax=9.18 µmol/min/mg enzyme for cumene hydroperoxide1 Publication
  6. Vmax=1120 nmol/min/mg enzyme for cumene hydroperoxide1 Publication
  7. Vmax=2.57 µmol/min/mg enzyme for triphenylcarbinyl hydroperoxide1 Publication
  8. Vmax=9.88 µmol/min/mg enzyme for linoleic hydroperoxide1 Publication
  9. Vmax=1390 nmol/min/mg enzyme for linolenoyl hydroperoxide1 Publication
  10. Vmax=7.34 µmol/min/mg enzyme for 5-phenyl-3-pentenyl hydroperoxide1 Publication
  11. Vmax=1380 nmol/min/mg enzyme for arachidonoyl hydroperoxide1 Publication
  12. Vmax=1500 nmol/min/mg enzyme for PLCP hydroperoxide1 Publication
  13. Vmax=1640 nmol/min/mg enzyme for PACP hydroperoxide1 Publication
  14. Vmax=4225 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine (at pH 4)1 Publication

pH dependencei

Optimum pH is 7-8.1 Publication

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>Sitei32Important for phospholipase activityBy similarity1
<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 sitei47Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activityBy similarity1
Active sitei140For phospholipase activityBy 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, Hydrolase, Multifunctional enzyme, Oxidoreductase, Peroxidase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.11.1.15, 908

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-BTA-3299685, Detoxification of Reactive Oxygen Species
R-BTA-6798695, Neutrophil degranulation

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
4423, Bt1CysPrx

<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-6 (EC:1.11.1.272 Publications)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
Acidic calcium-independent phospholipase A21 Publication (EC:3.1.1.41 Publication)
Short name:
aiPLA2
Antioxidant protein 2
Ciliary body glutathione peroxidase
Glutathione-dependent peroxiredoxinCurated
Non-selenium glutathione peroxidase
Short name:
NSGPx
PHGPx
<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:PRDX6
Synonyms:AOP2, GPX, PHGPX
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<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
  • UP000009136 <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 16

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:33304, PRDX6

<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

Cytoplasm, Lysosome

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00001351012 – 224Peroxiredoxin-6Add BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei44PhosphothreonineBy similarity1
Modified residuei63N6-acetyllysineBy similarity1
Modified residuei89PhosphotyrosineBy similarity1
Modified residuei177Phosphothreonine; by MAPKBy similarity1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateBy similarity1

<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

Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO2H) and sulfonic acid (Cys-SO3H) forms upon oxidative stress.By similarity
Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
O77834

PeptideAtlas

More...
PeptideAtlasi
O77834

PRoteomics IDEntifications database

More...
PRIDEi
O77834

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000004855, Expressed in lung and 18 other tissues

<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 (By similarity).

Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration (PubMed:15004285).

Interacts with APEX1.

Interacts with STH. May interact with FAM168B (By similarity). May interact with HTR2A (By similarity).

By similarity1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000006383

<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
O77834

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>Domaini5 – 169ThioredoxinPROSITE-ProRule annotationAdd BLAST165

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni31 – 40Required and sufficient for targeting to lysosomes and lamellar bodiesBy similarity10

<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 peroxiredoxin family. Prx6 subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0854, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074794

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_042529_4_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O77834

KEGG Orthology (KO)

More...
KOi
K11188

Identification of Orthologs from Complete Genome Data

More...
OMAi
IPLTCRA

Database of Orthologous Groups

More...
OrthoDBi
1129256at2759

TreeFam database of animal gene trees

More...
TreeFami
TF105183

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

O77834-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPGGLLLGDE APNFEANTTI GRIRFHDYLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKMIA LSIDSVEDHL AWSKDINAYN GEEPTEKLPF
110 120 130 140 150
PIIDDKNRDL AIQLGMLDPA EKDEKGMPVT ARVVFIFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVIISLQLT AEKRVATPVD WKNGDSVMVL PTIPEEEAKK
210 220
LFPKGVFTKE LPSGKKYLRY TPQP
Length:224
Mass (Da):25,067
Last modified:January 23, 2007 - v3
<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:i4013D59C4D9FC05E
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
AF080228 mRNA Translation: AAC63016.1
AF090194 mRNA Translation: AAC84043.1
AJ243848 mRNA Translation: CAB64802.1
BT020967 mRNA Translation: AAX08984.1
BC102172 mRNA Translation: AAI02173.1

NCBI Reference Sequences

More...
RefSeqi
NP_777068.1, NM_174643.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000006383; ENSBTAP00000006383; ENSBTAG00000004855

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
282438

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:282438

<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
AF080228 mRNA Translation: AAC63016.1
AF090194 mRNA Translation: AAC84043.1
AJ243848 mRNA Translation: CAB64802.1
BT020967 mRNA Translation: AAX08984.1
BC102172 mRNA Translation: AAI02173.1
RefSeqiNP_777068.1, NM_174643.1

3D structure databases

SMRiO77834
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006383

Protein family/group databases

PeroxiBasei4423, Bt1CysPrx

Proteomic databases

PaxDbiO77834
PeptideAtlasiO77834
PRIDEiO77834

Genome annotation databases

EnsembliENSBTAT00000006383; ENSBTAP00000006383; ENSBTAG00000004855
GeneIDi282438
KEGGibta:282438

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
9588
VGNCiVGNC:33304, PRDX6

Phylogenomic databases

eggNOGiKOG0854, Eukaryota
GeneTreeiENSGT00550000074794
HOGENOMiCLU_042529_4_1_1
InParanoidiO77834
KOiK11188
OMAiIPLTCRA
OrthoDBi1129256at2759
TreeFamiTF105183

Enzyme and pathway databases

BRENDAi1.11.1.15, 908
ReactomeiR-BTA-3299685, Detoxification of Reactive Oxygen Species
R-BTA-6798695, Neutrophil degranulation

Gene expression databases

BgeeiENSBTAG00000004855, Expressed in lung and 18 other tissues

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 nameiPRDX6_BOVIN
<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: O77834
Secondary accession number(s): Q5E9F3
<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: July 15, 1999
Last sequence update: January 23, 2007
Last modified: August 12, 2020
This is version 144 of the entry and version 3 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 programChordata 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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