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Peroxiredoxin-2 (EC 1.11.1.15) (Thiol-specific antioxidant protein) (TSA) (Thioredoxin peroxidase 1) (Thioredoxin-dependent peroxide reductase 1)

 PRDX2_MOUSE             Reviewed;         198 AA.
Q61171; O88376; Q60796; Q9CWJ4; Q9DB49;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 174.
RecName: Full=Peroxiredoxin-2;
EC=1.11.1.15;
AltName: Full=Thiol-specific antioxidant protein;
Short=TSA;
AltName: Full=Thioredoxin peroxidase 1;
AltName: Full=Thioredoxin-dependent peroxide reductase 1;
Name=Prdx2; Synonyms=Tdpx1, Tpx;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=9115640; DOI=10.1089/dna.1997.16.311;
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/6J;
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;
PubMed=9714804; DOI=10.1016/S0378-1119(98)00290-X;
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;
PubMed=16141072; DOI=10.1126/science.1112014;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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 IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Liver;
Bienvenut W.V.;
Submitted (JUL-2005) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 11-26; 92-109; 120-127 AND 140-150, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[9]
INTERACTION WITH TIPIN.
PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097;
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events. Might participate in
the signaling cascades of growth factors and tumor necrosis
factor-alpha by regulating the intracellular concentrations of
H(2)O(2). {ECO:0000250|UniProtKB:P32119}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000250|UniProtKB:P32119}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
assemble to form a ring-like decamer (By similarity). Interacts
with TIPIN (PubMed:17141802). {ECO:0000250|UniProtKB:P32119,
ECO:0000269|PubMed:17141802}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}.
-!- 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.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
instead of its condensation to a disulfide bond. It can be
reactivated by forming a transient disulfide bond with
sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an
ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:P32119,
ECO:0000250|UniProtKB:Q06830}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by thioredoxin.
{ECO:0000250|UniProtKB:P32119}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U51679; AAB01941.1; -; mRNA.
EMBL; X82067; CAA57566.1; -; mRNA.
EMBL; U20611; AAA69475.1; -; mRNA.
EMBL; AF032722; AAC35744.1; -; Genomic_DNA.
EMBL; AF032718; AAC35744.1; JOINED; Genomic_DNA.
EMBL; AF032719; AAC35744.1; JOINED; Genomic_DNA.
EMBL; AF032720; AAC35744.1; JOINED; Genomic_DNA.
EMBL; AF032721; AAC35744.1; JOINED; Genomic_DNA.
EMBL; AK005225; BAB23893.1; -; mRNA.
EMBL; AK008433; BAB25666.1; -; mRNA.
EMBL; AK010653; BAB27093.1; -; mRNA.
EMBL; AK088280; BAC40255.1; -; mRNA.
EMBL; BC002034; AAH02034.1; -; mRNA.
EMBL; BC081454; AAH81454.1; -; mRNA.
CCDS; CCDS40416.1; -.
RefSeq; NP_001304314.1; NM_001317385.1.
RefSeq; NP_035693.3; NM_011563.6.
UniGene; Mm.347009; -.
UniGene; Mm.393373; -.
ProteinModelPortal; Q61171; -.
SMR; Q61171; -.
BioGrid; 204094; 6.
IntAct; Q61171; 14.
MINT; MINT-1862390; -.
STRING; 10090.ENSMUSP00000005292; -.
PeroxiBase; 4474; Mm2CysPrx02.
iPTMnet; Q61171; -.
PhosphoSitePlus; Q61171; -.
SwissPalm; Q61171; -.
REPRODUCTION-2DPAGE; Q61171; -.
SWISS-2DPAGE; Q61171; -.
UCD-2DPAGE; Q61171; -.
EPD; Q61171; -.
MaxQB; Q61171; -.
PaxDb; Q61171; -.
PeptideAtlas; Q61171; -.
PRIDE; Q61171; -.
TopDownProteomics; Q61171; -.
Ensembl; ENSMUST00000005292; ENSMUSP00000005292; ENSMUSG00000005161.
Ensembl; ENSMUST00000109733; ENSMUSP00000105355; ENSMUSG00000005161.
Ensembl; ENSMUST00000109734; ENSMUSP00000105356; ENSMUSG00000005161.
Ensembl; ENSMUST00000164807; ENSMUSP00000126451; ENSMUSG00000005161.
GeneID; 21672; -.
KEGG; mmu:21672; -.
UCSC; uc009mom.1; mouse.
CTD; 7001; -.
MGI; MGI:109486; Prdx2.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; Q61171; -.
KO; K03386; -.
OMA; FKEVKLC; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; Q61171; -.
TreeFam; TF105181; -.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-MMU-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
ChiTaRS; Prdx2; mouse.
PRO; PR:Q61171; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000005161; -.
CleanEx; MM_PRDX2; -.
ExpressionAtlas; Q61171; baseline and differential.
Genevisible; Q61171; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0016209; F:antioxidant activity; ISO:MGI.
GO; GO:0004601; F:peroxidase activity; TAS:MGI.
GO; GO:0008430; F:selenium binding; TAS:MGI.
GO; GO:0008379; F:thioredoxin peroxidase activity; ISS:MGI.
GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:MGI.
GO; GO:0042743; P:hydrogen peroxide metabolic process; IMP:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IMP:MGI.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:MGI.
GO; GO:0045581; P:negative regulation of T cell differentiation; IMP:MGI.
GO; GO:0030194; P:positive regulation of blood coagulation; IMP:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:MGI.
GO; GO:0019430; P:removal of superoxide radicals; IMP:BHF-UCL.
GO; GO:0002536; P:respiratory burst involved in inflammatory response; IMP:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
GO; GO:0042098; P:T cell proliferation; IMP:MGI.
GO; GO:0048538; P:thymus development; IMP:MGI.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Acetylation; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase;
Phosphoprotein; Redox-active center; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.7}.
CHAIN 2 198 Peroxiredoxin-2.
/FTId=PRO_0000135081.
DOMAIN 6 164 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 51 51 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:P32119}.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.7}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000250|UniProtKB:P32119}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000250|UniProtKB:P32119}.
DISULFID 51 51 Interchain (with C-172); in linked form.
{ECO:0000250|UniProtKB:P32119}.
DISULFID 172 172 Interchain (with C-51); in linked form.
{ECO:0000250|UniProtKB:P32119}.
CONFLICT 38 38 V -> M (in Ref. 5; BAB27093).
{ECO:0000305}.
CONFLICT 39 39 V -> D (in Ref. 5; BAB23893).
{ECO:0000305}.
CONFLICT 69 69 G -> R (in Ref. 5; BAB23893).
{ECO:0000305}.
CONFLICT 97 97 G -> A (in Ref. 3; AAA69475).
{ECO:0000305}.
CONFLICT 113 113 Q -> H (in Ref. 5; BAB23893).
{ECO:0000305}.
CONFLICT 124 124 I -> V (in Ref. 5; BAB23893).
{ECO:0000305}.
CONFLICT 135 135 K -> S (in Ref. 5; BAB23893).
{ECO:0000305}.
CONFLICT 182 182 T -> N (in Ref. 3 and 4). {ECO:0000305}.
SEQUENCE 198 AA; 21779 MW; FE216F5426F7174D CRC64;
MASGNAQIGK SAPDFTATAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD
HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN
DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
DTIKPNVDDS KEYFSKHN


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