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Q61171

- PRDX2_MOUSE

UniProt

Q61171 - PRDX2_MOUSE

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Protein
Peroxiredoxin-2
Gene
Prdx2, Tdpx1, Tpx
Organism
Mus musculus (Mouse)
Status
Reviewed - 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) intermediate By similarity

GO - Molecular functioni

  1. peroxidase activity Source: MGI
  2. protein binding Source: MGI
  3. selenium binding Source: MGI
  4. thioredoxin peroxidase activity Source: MGI

GO - Biological processi

  1. T cell proliferation Source: MGI
  2. activation of MAPK activity Source: MGI
  3. homeostasis of number of cells Source: MGI
  4. hydrogen peroxide catabolic process Source: MGI
  5. hydrogen peroxide metabolic process Source: MGI
  6. negative regulation of NF-kappaB transcription factor activity Source: MGI
  7. negative regulation of T cell differentiation Source: MGI
  8. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  9. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  10. negative regulation of lipopolysaccharide-mediated signaling pathway Source: MGI
  11. negative regulation of reactive oxygen species metabolic process Source: MGI
  12. positive regulation of blood coagulation Source: BHF-UCL
  13. regulation of hydrogen peroxide metabolic process Source: MGI
  14. removal of superoxide radicals Source: BHF-UCL
  15. respiratory burst involved in inflammatory response Source: MGI
  16. response to lipopolysaccharide Source: MGI
  17. response to oxidative stress Source: MGI
  18. thymus development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

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: Chromosome 8

Organism-specific databases

MGIiMGI:109486. Prdx2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Disulfide bondi51 – 51Interchain (with C-172); in linked form By similarity
Disulfide bondi172 – 172Interchain (with C-51); in linked form By similarity

Keywords - PTMi

Acetylation, Disulfide bond

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

ArrayExpressiQ61171.
BgeeiQ61171.
CleanExiMM_PRDX2.
GenevestigatoriQ61171.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation By similarity. Interacts with TIPIN.1 Publication

Protein-protein interaction databases

BioGridi204094. 2 interactions.
IntActiQ61171. 13 interactions.
MINTiMINT-1862390.

Structurei

3D structure databases

ProteinModelPortaliQ61171.
SMRiQ61171. Positions 3-198.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 164159Thioredoxin
Add
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.
Contains 1 thioredoxin domain.

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ61171.
KOiK03386.
OMAiEGVIQHA.
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

MASGNAQIGK SAPDFTATAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV    50
CPTEIIAFSD HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN 100
IPLLADVTKS LSQNYGVLKN DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR 150
SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN 198
Length:198
Mass (Da):21,779
Last modified:January 23, 2007 - v3
Checksum:iFE216F5426F7174D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381V → M in BAB27093. 1 Publication
Sequence conflicti39 – 391V → D in BAB23893. 1 Publication
Sequence conflicti69 – 691G → R in BAB23893. 1 Publication
Sequence conflicti97 – 971G → A in AAA69475. 1 Publication
Sequence conflicti113 – 1131Q → H in BAB23893. 1 Publication
Sequence conflicti124 – 1241I → V in BAB23893. 1 Publication
Sequence conflicti135 – 1351K → S in BAB23893. 1 Publication
Sequence conflicti182 – 1821T → N1 Publication
Sequence conflicti182 – 1821T → N1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS40416.1.
RefSeqi NP_035693.3. NM_011563.5.
XP_006530898.1. XM_006530835.1.
UniGenei Mm.347009.
Mm.393373.

3D structure databases

ProteinModelPortali Q61171.
SMRi Q61171. Positions 3-198.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204094. 2 interactions.
IntActi Q61171. 13 interactions.
MINTi MINT-1862390.

Protein family/group databases

PeroxiBasei 4474. Mm2CysPrx02.

PTM databases

PhosphoSitei Q61171.

2D gel databases

REPRODUCTION-2DPAGE Q61171.
SWISS-2DPAGE Q61171.
UCD-2DPAGE Q61171.

Proteomic databases

MaxQBi Q61171.
PaxDbi Q61171.
PRIDEi Q61171.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005292 ; ENSMUSP00000005292 ; ENSMUSG00000005161 .
ENSMUST00000109733 ; ENSMUSP00000105355 ; ENSMUSG00000005161 .
ENSMUST00000109734 ; ENSMUSP00000105356 ; ENSMUSG00000005161 .
ENSMUST00000164807 ; ENSMUSP00000126451 ; ENSMUSG00000005161 .
GeneIDi 21672.
KEGGi mmu:21672.
UCSCi uc009mom.1. mouse.

Organism-specific databases

CTDi 7001.
MGIi MGI:109486. Prdx2.

Phylogenomic databases

eggNOGi COG0450.
GeneTreei ENSGT00390000004653.
HOGENOMi HOG000022343.
HOVERGENi HBG000286.
InParanoidi Q61171.
KOi K03386.
OMAi EGVIQHA.
OrthoDBi EOG7T1RCD.
PhylomeDBi Q61171.
TreeFami TF105181.

Enzyme and pathway databases

Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSi PRDX2. mouse.
NextBioi 300952.
PROi Q61171.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61171.
Bgeei Q61171.
CleanExi MM_PRDX2.
Genevestigatori Q61171.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000239. AHPC. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 146 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.
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.

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

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