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UniProtKB/Swiss-Prot entry Q61171


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRDX2_MOUSE
Primary accession number Q61171
Secondary accession numbers O88376 Q60796 Q9CWJ4 Q9DB49
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 88)
Name and origin of the protein
Protein name Peroxiredoxin-2
Synonyms EC 1.11.1.15
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1
Thiol-specific antioxidant protein
TSA
Gene name
Name: Prdx2
Synonyms: Tdpx1, Tpx
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Brain;
PubMed=9115640 [NCBI, ExPASy, EBI, Israel, Japan]
Ichimiya S., Davis J.G., O'Rourke D.M., Katsumata M., Greene M.I.;
"Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed in areas of the brain most susceptible to hypoxic and ischemic injury.";
DNA Cell Biol. 16:311-321(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129;
Oberbaeumer I.;
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6;
Chae H.Z., Kim H., Rhee S.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/SvJ;
DOI=10.1016/S0378-1119(98)00290-X; PubMed=9714804 [NCBI, ExPASy, EBI, Israel, Japan]
Lim M.J., Chae H.Z., Rhee S.G., Yu D.-Y., Lee K.-K., Yeom Y.I.;
"The type II peroxiredoxin gene family of the mouse: molecular structure, expression and evolution.";
Gene 216:197-205(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
TISSUE=Cerebellum, Small intestine, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Brain, and Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-10 AND 120-135, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Liver;
Bienvenut W.V.;
Submitted (JUL-2005) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 11-26; 93-109 AND 140-150, AND MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 11-26; 92-109 AND 120-127, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[10]
INTERACTION WITH TIPIN.
DOI=10.1016/j.jmb.2006.10.097; PubMed=17141802 [NCBI, ExPASy, EBI, Israel, Japan]
Gotter A.L., Suppa C., Emanuel B.S.;
"Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors.";
J. Mol. Biol. 366:36-52(2007).
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 H(2)O(2).
  • CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
  • SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity). Interacts with TIPIN.
  • 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).
  • MISCELLANEOUS: Inactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized (By similarity).
  • SIMILARITY: Belongs to the ahpC/TSA family.
  • SIMILARITY: Contains 1 thioredoxin domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U51679; AAB01941.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X82067; CAA57566.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U20611; AAA69475.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032722; AAC35744.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032718; AAC35744.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032719; AAC35744.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032720; AAC35744.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032721; AAC35744.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005225; BAB23893.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008433; BAB25666.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK010653; BAB27093.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK088280; BAC40255.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002034; AAH02034.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081454; AAH81454.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_035693.3; -.
UniGene Mm.347009
3D structure databases
HSSP P32119; 1QMV. [HSSP ENTRY / PDB]
SMR Q61171; 2-197, 3-198.
ModBase Q61171.
Protein family/group databases
PeroxiBase 4474; Mm2CysPrx02.
PTM databases
PhosphoSite Q61171; -.
2D gel databases
SWISS-2DPAGE Q61171; -.
REPRODUCTION-2DPAGE Q61171; -.
Organism-specific databases
MGI MGI:109486; Prdx2.
Gene expression databases
ArrayExpress Q61171; -.
CleanEx MM_PRDX2; -.
GermOnline ENSMUSG00000005161; Mus musculus.
Ontologies
GO
GO:0008430; Molecular function: selenium binding (traceable author statement from MGI).
GO:0008379; Molecular function: thioredoxin peroxidase activity (traceable author statement from MGI).
GO:0006916; Biological process: anti-apoptosis (inferred from direct assay from MGI).
GO:0048872; Biological process: homeostasis of number of cells (inferred from mutant phenotype from MGI).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from mutant phenotype from MGI).
GO:0042098; Biological process: T cell proliferation (inferred from mutant phenotype from MGI).
GO:0048538; Biological process: thymus development (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q61171.
Genome annotation databases
Ensembl ENSMUSG00000005161; Mus musculus. [Contig view]
GeneID 21672; -.
KEGG mmu:21672; -.
NMPDR fig|10090.3.peg.18891; -.
Phylogenomic databases
HOGENOM Q61171; -.
HOVERGEN Q61171; -.
Other
LinkHub Q61171; -.
SOURCE Prdx2; Mus musculus.
ProtoNet Q61171.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing; Oxidoreductase; Peroxidase; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   198  197     Peroxiredoxin-2. PRO_0000135081
DOMAIN   6   164  159     Thioredoxin. 
ACT_SITE   51    51        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
DISULFID   51    51        Interchain (with C-172); in linked form (By similarity). 
DISULFID   172   172        Interchain (with C-51); in linked form (By similarity). 
CONFLICT   38    38        V -> M (in Ref. 5; BAB27093). 
CONFLICT   39    39        V -> D (in Ref. 5; BAB23893). 
CONFLICT   69    69        G -> R (in Ref. 5; BAB23893). 
CONFLICT   97    97        G -> A (in Ref. 3; AAA69475). 
CONFLICT   113   113        Q -> H (in Ref. 5; BAB23893). 
CONFLICT   124   124        I -> V (in Ref. 5; BAB23893). 
CONFLICT   135   135        K -> S (in Ref. 5; BAB23893). 
CONFLICT   182   182        T -> N (in Ref. 3 and 4). 
Sequence information
Length: 198 AA [This is the length of the unprocessed precursor] Molecular weight: 21779 Da [This is the MW of the unprocessed precursor] CRC64: FE216F5426F7174D [This is a checksum on the sequence]
        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 

Q61171 in FASTA format

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