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Protein

Peroxiredoxin-2

Gene

PRDX2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2.

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei52 – 521Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiR-BTA-3299685. Detoxification of Reactive Oxygen Species.
R-BTA-5628897. TP53 Regulates Metabolic Genes.

Protein family/group databases

PeroxiBasei4473. Bt2CysPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2 (EC:1.11.1.15)
Gene namesi
Name:PRDX2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Peroxiredoxin-2PRO_0000135079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 – 52Interchain (with C-173); in linked formBy similarity
Modified residuei113 – 1131PhosphoserineBy similarity
Disulfide bondi173 – 173Interchain (with C-52); in linked formBy similarity
Modified residuei183 – 1831PhosphothreonineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ9BGI3.
PeptideAtlasiQ9BGI3.
PRIDEiQ9BGI3.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015996.

Structurei

3D structure databases

ProteinModelPortaliQ9BGI3.
SMRiQ9BGI3. Positions 7-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 165159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ9BGI3.
KOiK03386.
OMAiLFAWPKD.
OrthoDBiEOG7T1RCD.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR033046. PRDX2.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10681:SF124. PTHR10681:SF124. 1 hit.
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BGI3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACVCKAHVG KPAPEFQATA VVDGAFKEVK LSDYKGKYVV LFFYPLDFTF
60 70 80 90 100
VCPTEIVAFS DRAAEFHKLN CEVLGVSVDS QFTHLAWINT PRKEGGLGPL
110 120 130 140 150
NIPLLADVTR KLSSDYGVLK EDEGIAYRGL FVIDGKGVLR QVTINDLPVG
160 170 180 190
RSVDEALRLV QAFQYTDEHG EVCPAGWTPG SDTIKPNVDD SKEYFSKHN
Length:199
Mass (Da):21,946
Last modified:June 1, 2001 - v1
Checksum:i5F256CE54090E2DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305562 mRNA. Translation: AAG53659.1.
BC102351 mRNA. Translation: AAI02352.1.
RefSeqiNP_777188.1. NM_174763.2.
XP_005208710.1. XM_005208653.1.
XP_010805021.1. XM_010806719.2.
UniGeneiBt.2689.

Genome annotation databases

EnsembliENSBTAT00000015996; ENSBTAP00000015996; ENSBTAG00000012062.
GeneIDi286793.
KEGGibta:286793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF305562 mRNA. Translation: AAG53659.1.
BC102351 mRNA. Translation: AAI02352.1.
RefSeqiNP_777188.1. NM_174763.2.
XP_005208710.1. XM_005208653.1.
XP_010805021.1. XM_010806719.2.
UniGeneiBt.2689.

3D structure databases

ProteinModelPortaliQ9BGI3.
SMRiQ9BGI3. Positions 7-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000015996.

Protein family/group databases

PeroxiBasei4473. Bt2CysPrx02.

Proteomic databases

PaxDbiQ9BGI3.
PeptideAtlasiQ9BGI3.
PRIDEiQ9BGI3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000015996; ENSBTAP00000015996; ENSBTAG00000012062.
GeneIDi286793.
KEGGibta:286793.

Organism-specific databases

CTDi7001.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ9BGI3.
KOiK03386.
OMAiLFAWPKD.
OrthoDBiEOG7T1RCD.
TreeFamiTF105181.

Enzyme and pathway databases

ReactomeiR-BTA-3299685. Detoxification of Reactive Oxygen Species.
R-BTA-5628897. TP53 Regulates Metabolic Genes.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR033046. PRDX2.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10681:SF124. PTHR10681:SF124. 1 hit.
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of 4 new bovine peroxiredoxins, and screening of the complete peroxiredoxin family in different bovine tissues."
    Leyens G., Donnay I., Knoops B.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiPRDX2_BOVIN
AccessioniPrimary (citable) accession number: Q9BGI3
Secondary accession number(s): Q3T0L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin (By similarity).By similarity
Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.