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Protein

Peroxiredoxin-2

Gene

Prdx2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 sitei51 – 511Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  • antioxidant activity Source: MGI
  • peroxidase activity Source: MGI
  • selenium binding Source: MGI
  • thioredoxin peroxidase activity Source: MGI

GO - Biological processi

  • activation of MAPK activity Source: MGI
  • cellular response to oxidative stress Source: MGI
  • homeostasis of number of cells Source: MGI
  • hydrogen peroxide catabolic process Source: MGI
  • hydrogen peroxide metabolic process Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • negative regulation of lipopolysaccharide-mediated signaling pathway Source: MGI
  • negative regulation of NF-kappaB transcription factor activity Source: MGI
  • negative regulation of reactive oxygen species metabolic process Source: MGI
  • negative regulation of T cell differentiation Source: MGI
  • positive regulation of blood coagulation Source: BHF-UCL
  • regulation of apoptotic process Source: MGI
  • regulation of hydrogen peroxide metabolic process Source: MGI
  • removal of superoxide radicals Source: BHF-UCL
  • respiratory burst involved in inflammatory response Source: MGI
  • response to lipopolysaccharide Source: MGI
  • response to oxidative stress Source: MGI
  • T cell proliferation Source: MGI
  • thymus development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_308972. Detoxification of Reactive Oxygen Species.
REACT_360191. TP53 Regulates Metabolic Genes.

Protein family/group databases

PeroxiBasei4474. Mm2CysPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2 (EC:1.11.1.15)
Alternative name(s):
Thiol-specific antioxidant protein
Short name:
TSA
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1
Gene namesi
Name:Prdx2
Synonyms:Tdpx1, Tpx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:109486. Prdx2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 198197Peroxiredoxin-2PRO_0000135081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Disulfide bondi51 – 51Interchain (with C-172); in linked formBy similarity
Modified residuei112 – 1121PhosphoserineBy similarity
Disulfide bondi172 – 172Interchain (with C-51); in linked formBy similarity
Modified residuei182 – 1821PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ61171.
PaxDbiQ61171.
PRIDEiQ61171.

2D gel databases

REPRODUCTION-2DPAGEQ61171.
SWISS-2DPAGEQ61171.
UCD-2DPAGEQ61171.

PTM databases

PhosphoSiteiQ61171.

Expressioni

Tissue specificityi

Widely expressed with highest levels in bone marrow. High levels also found in heart, brain, kidney and skeletal muscle. Lower levels in liver, lung and thymus.

Gene expression databases

BgeeiQ61171.
CleanExiMM_PRDX2.
ExpressionAtlasiQ61171. baseline and differential.
GenevisibleiQ61171. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation (By similarity). Interacts with TIPIN.By similarity1 Publication

Protein-protein interaction databases

BioGridi204094. 3 interactions.
IntActiQ61171. 14 interactions.
MINTiMINT-1862390.
STRINGi10090.ENSMUSP00000005292.

Structurei

3D structure databases

ProteinModelPortaliQ61171.
SMRiQ61171. Positions 3-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 164159ThioredoxinPROSITE-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

eggNOGiCOG0450.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ61171.
KOiK03386.
OMAiMAACCSS.
OrthoDBiEOG7T1RCD.
PhylomeDBiQ61171.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGNAQIGK SAPDFTATAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV
60 70 80 90 100
CPTEIIAFSD HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN
110 120 130 140 150
IPLLADVTKS LSQNYGVLKN DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR
160 170 180 190
SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN
Length:198
Mass (Da):21,779
Last modified:January 23, 2007 - v3
Checksum:iFE216F5426F7174D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381V → M in BAB27093 (PubMed:16141072).Curated
Sequence conflicti39 – 391V → D in BAB23893 (PubMed:16141072).Curated
Sequence conflicti69 – 691G → R in BAB23893 (PubMed:16141072).Curated
Sequence conflicti97 – 971G → A in AAA69475 (Ref. 3) Curated
Sequence conflicti113 – 1131Q → H in BAB23893 (PubMed:16141072).Curated
Sequence conflicti124 – 1241I → V in BAB23893 (PubMed:16141072).Curated
Sequence conflicti135 – 1351K → S in BAB23893 (PubMed:16141072).Curated
Sequence conflicti182 – 1821T → N (Ref. 3) Curated
Sequence conflicti182 – 1821T → N (PubMed:9714804).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51679 mRNA. Translation: AAB01941.1.
X82067 mRNA. Translation: CAA57566.1.
U20611 mRNA. Translation: AAA69475.1.
AF032722
, AF032718, AF032719, AF032720, AF032721 Genomic DNA. Translation: AAC35744.1.
AK005225 mRNA. Translation: BAB23893.1.
AK008433 mRNA. Translation: BAB25666.1.
AK010653 mRNA. Translation: BAB27093.1.
AK088280 mRNA. Translation: BAC40255.1.
BC002034 mRNA. Translation: AAH02034.1.
BC081454 mRNA. Translation: AAH81454.1.
CCDSiCCDS40416.1.
RefSeqiNP_035693.3. NM_011563.5.
XP_006530898.1. XM_006530835.1.
UniGeneiMm.347009.
Mm.393373.

Genome annotation databases

EnsembliENSMUST00000005292; ENSMUSP00000005292; ENSMUSG00000005161.
ENSMUST00000109733; ENSMUSP00000105355; ENSMUSG00000005161.
ENSMUST00000109734; ENSMUSP00000105356; ENSMUSG00000005161.
ENSMUST00000164807; ENSMUSP00000126451; ENSMUSG00000005161.
GeneIDi21672.
KEGGimmu:21672.
UCSCiuc009mom.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51679 mRNA. Translation: AAB01941.1.
X82067 mRNA. Translation: CAA57566.1.
U20611 mRNA. Translation: AAA69475.1.
AF032722
, AF032718, AF032719, AF032720, AF032721 Genomic DNA. Translation: AAC35744.1.
AK005225 mRNA. Translation: BAB23893.1.
AK008433 mRNA. Translation: BAB25666.1.
AK010653 mRNA. Translation: BAB27093.1.
AK088280 mRNA. Translation: BAC40255.1.
BC002034 mRNA. Translation: AAH02034.1.
BC081454 mRNA. Translation: AAH81454.1.
CCDSiCCDS40416.1.
RefSeqiNP_035693.3. NM_011563.5.
XP_006530898.1. XM_006530835.1.
UniGeneiMm.347009.
Mm.393373.

3D structure databases

ProteinModelPortaliQ61171.
SMRiQ61171. Positions 3-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204094. 3 interactions.
IntActiQ61171. 14 interactions.
MINTiMINT-1862390.
STRINGi10090.ENSMUSP00000005292.

Protein family/group databases

PeroxiBasei4474. Mm2CysPrx02.

PTM databases

PhosphoSiteiQ61171.

2D gel databases

REPRODUCTION-2DPAGEQ61171.
SWISS-2DPAGEQ61171.
UCD-2DPAGEQ61171.

Proteomic databases

MaxQBiQ61171.
PaxDbiQ61171.
PRIDEiQ61171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005292; ENSMUSP00000005292; ENSMUSG00000005161.
ENSMUST00000109733; ENSMUSP00000105355; ENSMUSG00000005161.
ENSMUST00000109734; ENSMUSP00000105356; ENSMUSG00000005161.
ENSMUST00000164807; ENSMUSP00000126451; ENSMUSG00000005161.
GeneIDi21672.
KEGGimmu:21672.
UCSCiuc009mom.1. mouse.

Organism-specific databases

CTDi7001.
MGIiMGI:109486. Prdx2.

Phylogenomic databases

eggNOGiCOG0450.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ61171.
KOiK03386.
OMAiMAACCSS.
OrthoDBiEOG7T1RCD.
PhylomeDBiQ61171.
TreeFamiTF105181.

Enzyme and pathway databases

ReactomeiREACT_308972. Detoxification of Reactive Oxygen Species.
REACT_360191. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiPrdx2. mouse.
NextBioi300952.
PROiQ61171.
SOURCEiSearch...

Gene expression databases

BgeeiQ61171.
CleanExiMM_PRDX2.
ExpressionAtlasiQ61171. baseline and differential.
GenevisibleiQ61171. MM.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
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. "Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed in areas of the brain most susceptible to hypoxic and ischemic injury."
    Ichimiya S., Davis J.G., O'Rourke D.M., Katsumata M., Greene M.I.
    DNA Cell Biol. 16:311-321(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  2. Oberbaeumer I.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129.
  3. Chae H.Z., Kim H., Rhee S.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  4. "The type II peroxiredoxin gene family of the mouse: molecular structure, expression and evolution."
    Lim M.J., Chae H.Z., Rhee S.G., Yu D.-Y., Lee K.-K., Yeom Y.I.
    Gene 216:197-205(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/SvJ.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Cerebellum, Small intestine and Thymus.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Mammary gland.
  7. Bienvenut W.V.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10 AND 120-135, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Liver.
  8. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 11-26; 92-109; 120-127 AND 140-150, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  9. "Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors."
    Gotter A.L., Suppa C., Emanuel B.S.
    J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIPIN.

Entry informationi

Entry nameiPRDX2_MOUSE
AccessioniPrimary (citable) accession number: Q61171
Secondary accession number(s): O88376
, Q60796, Q9CWJ4, Q9DB49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 155 of the entry and version 3 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-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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-51 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.