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Peroxiredoxin-5, mitochondrial (EC 1.11.1.15) (Antioxidant enzyme B166) (AOEB166) (Liver tissue 2D-page spot 2D-0014IV) (PLP) (Peroxiredoxin V) (Prx-V) (Peroxisomal antioxidant enzyme) (Thioredoxin peroxidase PMP20) (Thioredoxin reductase)

 PRDX5_MOUSE             Reviewed;         210 AA.
P99029; Q9QX45; Q9QZ75;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
21-FEB-2002, sequence version 2.
30-AUG-2017, entry version 157.
RecName: Full=Peroxiredoxin-5, mitochondrial;
EC=1.11.1.15 {ECO:0000269|PubMed:10679306};
AltName: Full=Antioxidant enzyme B166;
Short=AOEB166;
AltName: Full=Liver tissue 2D-page spot 2D-0014IV;
AltName: Full=PLP;
AltName: Full=Peroxiredoxin V;
Short=Prx-V;
AltName: Full=Peroxisomal antioxidant enzyme;
AltName: Full=Thioredoxin peroxidase PMP20;
Flags: Precursor;
Name=Prdx5; Synonyms=Prdx6;
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], FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=10679306; DOI=10.1006/bbrc.2000.2231;
Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M.,
Fung P.C.W., Kung H.-F., Jin D.-Y.;
"Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-
induced apoptosis.";
Biochem. Biophys. Res. Commun. 268:921-927(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10514471; DOI=10.1074/jbc.274.42.29897;
Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P.,
Subramani S., Rogers R.A., Avraham H.;
"Characterization of human and murine PMP20 peroxisomal proteins that
exhibit antioxidant activity in vitro.";
J. Biol. Chem. 274:29897-29904(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeJ; TISSUE=Lung;
PubMed=10521424; DOI=10.1074/jbc.274.43.30451;
Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C.,
Duconseille E., Falmagne P., Bernard A.;
"Cloning and characterization of AOEB166, a novel mammalian
antioxidant enzyme of the peroxiredoxin family.";
J. Biol. Chem. 274:30451-30458(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10753630; DOI=10.1006/bbrc.2000.2430;
Lee T.H., Kim S.J., Kang S.W., Lee K.K., Rhee S.G., Yu D.Y.;
"Molecular cloning and characterization of the mouse Peroxiredoxin V
gene.";
Biochem. Biophys. Res. Commun. 270:356-362(2000).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
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 50-61.
TISSUE=Liver;
Sanchez J.-C., Rouge V., Frutiger S., Hughes G.J., Yan J.X.,
Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
Submitted (AUG-1998) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 72-79; 83-112 AND 145-172, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, 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).
[10]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-79 AND LYS-112,
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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-71 AND LYS-79, 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 and as sensor of
hydrogen peroxide-mediated signaling events.
{ECO:0000269|PubMed:10679306}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:10679306}.
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30044}.
-!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion
{ECO:0000250|UniProtKB:P30044}.
-!- SUBCELLULAR LOCATION: Isoform Cytoplasmic+peroxisomal: Cytoplasm
{ECO:0000250|UniProtKB:P30044}. Peroxisome matrix
{ECO:0000250|UniProtKB:P30044}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Mitochondrial;
IsoId=P99029-1; Sequence=Displayed;
Name=Cytoplasmic+peroxisomal;
IsoId=P99029-2; Sequence=VSP_018830;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- 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 atypical 2-Cys Prx, C(R) is present in the same
subunit to form an intramolecular disulfide. The disulfide is
subsequently reduced by thioredoxin.
{ECO:0000250|UniProtKB:P30044}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
{ECO:0000305}.
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EMBL; AF197951; AAF04855.1; -; mRNA.
EMBL; AF124994; AAF27532.1; -; mRNA.
EMBL; AF110733; AAG13450.1; -; mRNA.
EMBL; AF208730; AAF21016.1; -; Genomic_DNA.
EMBL; AF208729; AAF21016.1; JOINED; Genomic_DNA.
EMBL; AK002383; BAB22058.1; -; mRNA.
EMBL; AK003332; BAB22720.1; -; mRNA.
EMBL; BC008174; AAH08174.1; -; mRNA.
CCDS; CCDS29507.1; -. [P99029-1]
PIR; JC7239; JC7239.
RefSeq; NP_036151.1; NM_012021.2. [P99029-1]
UniGene; Mm.279782; -.
ProteinModelPortal; P99029; -.
SMR; P99029; -.
BioGrid; 207718; 3.
IntAct; P99029; 5.
MINT; MINT-1859227; -.
STRING; 10090.ENSMUSP00000025904; -.
PeroxiBase; 4453; MmPrxV.
iPTMnet; P99029; -.
PhosphoSitePlus; P99029; -.
SwissPalm; P99029; -.
REPRODUCTION-2DPAGE; P99029; -.
SWISS-2DPAGE; P99029; -.
MaxQB; P99029; -.
PaxDb; P99029; -.
PeptideAtlas; P99029; -.
PRIDE; P99029; -.
Ensembl; ENSMUST00000025904; ENSMUSP00000025904; ENSMUSG00000024953. [P99029-1]
GeneID; 54683; -.
KEGG; mmu:54683; -.
UCSC; uc008gjc.1; mouse. [P99029-1]
CTD; 25824; -.
MGI; MGI:1859821; Prdx5.
eggNOG; KOG0541; Eukaryota.
eggNOG; COG0678; LUCA.
GeneTree; ENSGT00390000018173; -.
HOGENOM; HOG000255884; -.
HOVERGEN; HBG053675; -.
InParanoid; P99029; -.
KO; K11187; -.
OMA; QRYAMVV; -.
PhylomeDB; P99029; -.
TreeFam; TF105182; -.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
PRO; PR:P99029; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024953; -.
CleanEx; MM_PRDX5; -.
CleanEx; MM_PRDX6; -.
ExpressionAtlas; P99029; baseline and differential.
Genevisible; P99029; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
GO; GO:0005777; C:peroxisome; ISO:MGI.
GO; GO:0016209; F:antioxidant activity; ISS:UniProtKB.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
GO; GO:0004601; F:peroxidase activity; ISO:MGI.
GO; GO:0051920; F:peroxiredoxin activity; ISO:MGI.
GO; GO:0072541; F:peroxynitrite reductase activity; ISO:MGI.
GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISS:UniProtKB.
GO; GO:0001016; F:RNA polymerase III regulatory region DNA binding; ISO:MGI.
GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:MGI.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0042744; P:hydrogen peroxide catabolic process; ISS:UniProtKB.
GO; GO:0070995; P:NADPH oxidation; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0051354; P:negative regulation of oxidoreductase activity; ISO:MGI.
GO; GO:0016480; P:negative regulation of transcription from RNA polymerase III promoter; ISO:MGI.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
GO; GO:2001057; P:reactive nitrogen species metabolic process; ISO:MGI.
GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; ISO:MGI.
GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
InterPro; IPR013740; Redoxin.
InterPro; IPR012336; Thioredoxin-like_fold.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF08534; Redoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Acetylation; Alternative initiation; Antioxidant; Complete proteome;
Cytoplasm; Direct protein sequencing; Disulfide bond; Mitochondrion;
Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein;
Redox-active center; Reference proteome; Transit peptide.
TRANSIT 1 48 Mitochondrion. {ECO:0000255}.
CHAIN 49 210 Peroxiredoxin-5, mitochondrial.
/FTId=PRO_0000023795.
DOMAIN 52 210 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 208 210 Microbody targeting signal.
{ECO:0000250|UniProtKB:P30044}.
ACT_SITE 96 96 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:P30044}.
MOD_RES 70 70 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 70 70 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 71 71 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 79 79 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 79 79 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 112 112 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R063}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
DISULFID 96 200 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VAR_SEQ 1 48 Missing (in isoform
Cytoplasmic+peroxisomal). {ECO:0000305}.
/FTId=VSP_018830.
CONFLICT 55 55 G -> D (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 83 102 GVLFGVPGAFTPGCSKTHLP -> VFCLESLGHLHLAVLRP
TA (in Ref. 4; AAF21016). {ECO:0000305}.
SEQUENCE 210 AA; 21897 MW; E944104CC468BDD8 CRC64;
MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA PIKVGDAIPS
VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH LPGFVEQAGA LKAKGAQVVA
CLSVNDVFVI EEWGRAHQAE GKVRLLADPT GAFGKATDLL LDDSLVSLFG NRRLKRFSMV
IDNGIVKALN VEPDGTGLTC SLAPNILSQL


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