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Q61171 (PRDX2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Prdx2
Synonyms:Tdpx1, Tpx
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity. Interacts with TIPIN. Ref.9

Subcellular location

Cytoplasm.

Tissue specificity

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.

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.

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.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell proliferation

Inferred from mutant phenotype PubMed 15259009. Source: MGI

activation of MAPK activity

Inferred from mutant phenotype PubMed 17325201. Source: MGI

homeostasis of number of cells

Inferred from mutant phenotype PubMed 15259009. Source: MGI

hydrogen peroxide catabolic process

Inferred from mutant phenotype PubMed 15902258. Source: MGI

hydrogen peroxide metabolic process

Inferred from mutant phenotype PubMed 15259009. Source: MGI

negative regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 17325201. Source: MGI

negative regulation of T cell differentiation

Inferred from mutant phenotype PubMed 16290204. Source: MGI

negative regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 15259009. Source: MGI

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from direct assay Ref.1. Source: MGI

negative regulation of lipopolysaccharide-mediated signaling pathway

Inferred from mutant phenotype PubMed 17325201. Source: MGI

negative regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 17325201. Source: MGI

positive regulation of blood coagulation

Inferred from mutant phenotype PubMed 20978343. Source: BHF-UCL

regulation of hydrogen peroxide metabolic process

Inferred from mutant phenotype PubMed 17325201. Source: MGI

removal of superoxide radicals

Inferred from mutant phenotype PubMed 20978343. Source: BHF-UCL

respiratory burst involved in inflammatory response

Inferred from mutant phenotype PubMed 17325201. Source: MGI

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 17325201. Source: MGI

response to oxidative stress

Traceable author statement Ref.1. Source: MGI

thymus development

Inferred from mutant phenotype PubMed 15259009. Source: MGI

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functionperoxidase activity

Traceable author statement Ref.1. Source: MGI

selenium binding

Traceable author statement PubMed 9792801. Source: MGI

thioredoxin peroxidase activity

Inferred from sequence or structural similarity Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 198197Peroxiredoxin-2
PRO_0000135081

Regions

Domain6 – 164159Thioredoxin

Sites

Active site511Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Disulfide bond51Interchain (with C-172); in linked form By similarity
Disulfide bond172Interchain (with C-51); in linked form By similarity

Experimental info

Sequence conflict381V → M in BAB27093. Ref.5
Sequence conflict391V → D in BAB23893. Ref.5
Sequence conflict691G → R in BAB23893. Ref.5
Sequence conflict971G → A in AAA69475. Ref.3
Sequence conflict1131Q → H in BAB23893. Ref.5
Sequence conflict1241I → V in BAB23893. Ref.5
Sequence conflict1351K → S in BAB23893. Ref.5
Sequence conflict1821T → N Ref.3
Sequence conflict1821T → N Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q61171 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FE216F5426F7174D

FASTA19821,779
        10         20         30         40         50         60 
MASGNAQIGK SAPDFTATAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD 

        70         80         90        100        110        120 
HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN 

       130        140        150        160        170        180 
DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS 

       190 
DTIKPNVDDS KEYFSKHN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51679 mRNA. Translation: AAB01941.1.
X82067 mRNA. Translation: CAA57566.1.
U20611 mRNA. Translation: AAA69475.1.
AF032722 expand/collapse EMBL AC list , 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.
RefSeqNP_035693.3. NM_011563.5.
XP_006530898.1. XM_006530835.1.
UniGeneMm.347009.
Mm.393373.

3D structure databases

ProteinModelPortalQ61171.
SMRQ61171. Positions 3-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204094. 1 interaction.
IntActQ61171. 13 interactions.
MINTMINT-1862390.

Protein family/group databases

PeroxiBase4474. Mm2CysPrx02.

PTM databases

PhosphoSiteQ61171.

2D gel databases

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

Proteomic databases

PaxDbQ61171.
PRIDEQ61171.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005292; ENSMUSP00000005292; ENSMUSG00000005161.
ENSMUST00000109733; ENSMUSP00000105355; ENSMUSG00000005161.
ENSMUST00000109734; ENSMUSP00000105356; ENSMUSG00000005161.
ENSMUST00000164807; ENSMUSP00000126451; ENSMUSG00000005161.
GeneID21672.
KEGGmmu:21672.
UCSCuc009mom.1. mouse.

Organism-specific databases

CTD7001.
MGIMGI:109486. Prdx2.

Phylogenomic databases

eggNOGCOG0450.
GeneTreeENSGT00390000004653.
HOGENOMHOG000022343.
HOVERGENHBG000286.
InParanoidQ61171.
KOK03386.
OMALQFTEEF.
OrthoDBEOG7T1RCD.
PhylomeDBQ61171.
TreeFamTF105181.

Gene expression databases

ArrayExpressQ61171.
BgeeQ61171.
CleanExMM_PRDX2.
GenevestigatorQ61171.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRDX2. mouse.
NextBio300952.
PROQ61171.
SOURCESearch...

Entry information

Entry namePRDX2_MOUSE
AccessionPrimary (citable) accession number: Q61171
Secondary accession number(s): O88376 expand/collapse secondary AC list , Q60796, Q9CWJ4, Q9DB49
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot