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Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (PRX III) (Perioredoxin-3) (Protein MER5)

 PRDX3_MOUSE             Reviewed;         257 AA.
P20108;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
25-OCT-2017, entry version 171.
RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial;
EC=1.11.1.15 {ECO:0000269|PubMed:9497357};
AltName: Full=Antioxidant protein 1;
Short=AOP-1;
AltName: Full=PRX III;
AltName: Full=Perioredoxin-3;
AltName: Full=Protein MER5;
Flags: Precursor;
Name=Prdx3; Synonyms=Aop1, Mer5;
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].
PubMed=2583515; DOI=10.1016/0378-1119(89)90297-7;
Yamamoto T., Matsui Y., Natori S., Obinata M.;
"Cloning of a housekeeping-type gene (MER5) preferentially expressed
in murine erythroleukemia cells.";
Gene 80:337-343(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Lee T.-H., Rhee S.G., Lee K.-K., Yu D.-Y.;
"Characterization of mouse peroxiredoxin III genomic DNA and its
expression.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=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).
[5]
PROTEIN SEQUENCE OF 85-92; 151-167 AND 172-215, 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.
[6]
CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=9497357; DOI=10.1074/jbc.273.11.6297;
Kang S.W., Chae H.Z., Seo M.S., Kim K., Baines I.C., Rhee S.G.;
"Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide
generated in response to growth factors and tumor necrosis factor-
alpha.";
J. Biol. Chem. 273:6297-6302(1998).
[7]
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).
[8]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-84 AND LYS-92, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- 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.
{ECO:0000250|UniProtKB:P30048}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:9497357}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers
assemble to form a ring-like dodecamer. Interacts with NEK6.
Interacts with LRRK2. {ECO:0000250|UniProtKB:P30048}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9497357}.
-!- TISSUE SPECIFICITY: Housekeeping-type gene preferentially
expressed in murine erythroleukemia (MEL) cells.
-!- INDUCTION: Expression is increased after induction of MEL cells to
differentiation by DMSO.
-!- PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase
activity. {ECO:0000250|UniProtKB:P30048}.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
and sulphonic acid (C(P)-SO3H) instead of its condensation to a
disulfide bond. {ECO:0000250|UniProtKB:P30048}.
-!- 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:0000305|PubMed:9497357}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M28723; AAA39524.1; -; mRNA.
EMBL; AF211938; AAF63705.1; -; Genomic_DNA.
EMBL; AF211933; AAF63705.1; JOINED; Genomic_DNA.
EMBL; AF211934; AAF63705.1; JOINED; Genomic_DNA.
EMBL; AF211935; AAF63705.1; JOINED; Genomic_DNA.
EMBL; AF211936; AAF63705.1; JOINED; Genomic_DNA.
EMBL; AF211937; AAF63705.1; JOINED; Genomic_DNA.
EMBL; AK002448; BAB22108.1; -; mRNA.
EMBL; BC005626; AAH05626.1; -; mRNA.
CCDS; CCDS29944.1; -.
PIR; JQ0064; JQ0064.
RefSeq; NP_031478.1; NM_007452.2.
UniGene; Mm.29821; -.
ProteinModelPortal; P20108; -.
SMR; P20108; -.
BioGrid; 198117; 1.
IntAct; P20108; 5.
MINT; MINT-217585; -.
STRING; 10090.ENSMUSP00000025961; -.
PeroxiBase; 4499; Mm2CysPrx03.
iPTMnet; P20108; -.
PhosphoSitePlus; P20108; -.
SwissPalm; P20108; -.
REPRODUCTION-2DPAGE; IPI00116192; -.
REPRODUCTION-2DPAGE; P20108; -.
EPD; P20108; -.
MaxQB; P20108; -.
PaxDb; P20108; -.
PeptideAtlas; P20108; -.
PRIDE; P20108; -.
TopDownProteomics; P20108; -.
Ensembl; ENSMUST00000025961; ENSMUSP00000025961; ENSMUSG00000024997.
GeneID; 11757; -.
KEGG; mmu:11757; -.
UCSC; uc008icd.1; mouse.
CTD; 10935; -.
MGI; MGI:88034; Prdx3.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00390000004653; -.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; P20108; -.
KO; K20011; -.
OMA; TAVHNGE; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; P20108; -.
TreeFam; TF105181; -.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:P20108; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024997; -.
CleanEx; MM_PRDX3; -.
Genevisible; P20108; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0008385; C:IkappaB kinase complex; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:MGI.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:MGI.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
GO; GO:0001893; P:maternal placenta development; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0033673; P:negative regulation of kinase activity; ISO:MGI.
GO; GO:0018171; P:peptidyl-cysteine oxidation; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI.
GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
GO; GO:0006979; P:response to oxidative stress; 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;
Direct protein sequencing; Disulfide bond; Mitochondrion;
Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
Reference proteome; Transit peptide.
TRANSIT 1 62 Mitochondrion.
{ECO:0000250|UniProtKB:P30048}.
CHAIN 63 257 Thioredoxin-dependent peroxide reductase,
mitochondrial.
/FTId=PRO_0000023783.
DOMAIN 64 222 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 109 109 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:P35705}.
MOD_RES 84 84 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 92 92 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 92 92 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
DISULFID 109 109 Interchain (with C-230); in linked form.
{ECO:0000250|UniProtKB:P35705}.
DISULFID 230 230 Interchain (with C-109); in linked form.
{ECO:0000250|UniProtKB:P35705}.
SEQUENCE 257 AA; 28127 MW; 66513F2C5F1D56C0 CRC64;
MAAAAGRLLW SSVARHASAI SRSISASTVL RPVASRRTCL TDILWSASAQ GKSAFSTSSS
FHTPAVTQHA PYFKGTAVVN GEFKELSLDD FKGKYLVLFF YPLDFTFVCP TEIVAFSDKA
NEFHDVNCEV VAVSVDSHFS HLAWINTPRK NGGLGHMNIT LLSDITKQIS RDYGVLLESA
GIALRGLFII DPNGVVKHLS VNDLPVGRSV EETLRLVKAF QFVETHGEVC PANWTPESPT
IKPSPTASKE YFEKVHQ


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