ID PRDX5_HUMAN Reviewed; 214 AA. AC P30044; A6NC19; A6NG06; B7ZLJ4; B7ZVW3; Q14CK0; Q6IAF2; Q9UBU5; Q9UJU4; AC Q9UKX4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 4. DT 17-JUN-2020, entry version 211. DE RecName: Full=Peroxiredoxin-5, mitochondrial; DE EC=1.11.1.24 {ECO:0000269|PubMed:10751410}; DE AltName: Full=Alu corepressor 1; DE AltName: Full=Antioxidant enzyme B166; DE Short=AOEB166; DE AltName: Full=Liver tissue 2D-page spot 71B; DE AltName: Full=PLP; DE AltName: Full=Peroxiredoxin V; DE Short=Prx-V; DE AltName: Full=Peroxisomal antioxidant enzyme; DE AltName: Full=TPx type VI; DE AltName: Full=Thioredoxin peroxidase PMP20; DE AltName: Full=Thioredoxin-dependent peroxiredoxin 5 {ECO:0000305}; DE Flags: Precursor; GN Name=PRDX5; Synonyms=ACR1; ORFNames=SBBI10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT CYS-33. RX PubMed=10095767; DOI=10.1046/j.1432-1327.1999.00162.x; RA Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A., Krutilina R., RA Oei S.L., Griesenbeck J., Buchlow G., Tomilin N.; RT "A novel human DNA-binding protein with sequence similarity to a subfamily RT of redox proteins which is able to repress RNA-polymerase-III-driven RT transcription of the Alu-family retroposons in vitro."; RL Eur. J. Biochem. 260:336-346(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=10514471; DOI=10.1074/jbc.274.42.29897; RA Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., RA Subramani S., Rogers R.A., Avraham H.; RT "Characterization of human and murine PMP20 peroxisomal proteins that RT exhibit antioxidant activity in vitro."; RL J. Biol. Chem. 274:29897-29904(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), PROTEIN SEQUENCE OF RP 54-90, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANT RP CYS-33. RC TISSUE=Lung; RX PubMed=10521424; DOI=10.1074/jbc.274.43.30451; RA Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., RA Duconseille E., Falmagne P., Bernard A.; RT "Cloning and characterization of AOEB166, a novel mammalian antioxidant RT enzyme of the peroxiredoxin family."; RL J. Biol. Chem. 274:30451-30458(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), AND VARIANT RP CYS-33. RX PubMed=10679306; DOI=10.1006/bbrc.2000.2231; RA Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., RA Fung P.C.W., Kung H.-F., Jin D.-Y.; RT "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53- RT induced apoptosis."; RL Biochem. Biophys. Res. Commun. 268:921-927(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF RP CYS-100; CYS-125 AND CYS-204, ACTIVE SITE, DISULFIDE BOND, AND SUBCELLULAR RP LOCATION. RX PubMed=10751410; DOI=10.1074/jbc.m001943200; RA Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G.; RT "Identification of a new type of mammalian peroxiredoxin that forms an RT intramolecular disulfide as a reaction intermediate."; RL J. Biol. Chem. 275:20346-20354(2000). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL). RA Kim I.H., Jeong W.; RT "A new type of human thiol peroxidase (Human TPx type VI)."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT CYS-33. RA Zhang W., Li N., Wan T., Cao X.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT RP CYS-33. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT CYS-33. RG NIEHS SNPs program; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MITOCHONDRIAL; 3 AND 4), RP AND VARIANT CYS-33. RC TISSUE=Brain, and Medulla oblongata; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [13] RP PROTEIN SEQUENCE OF 54-63. RC TISSUE=Liver; RX PubMed=1286669; DOI=10.1002/elps.11501301201; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RT "Human liver protein map: a reference database established by RT microsequencing and gel comparison."; RL Electrophoresis 13:992-1001(1992). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). RX PubMed=11518528; DOI=10.1006/jmbi.2001.4853; RA Declercq J.-P., Evrard C., Clippe A., Stricht D.V., Bernard A., Knoops B.; RT "Crystal structure of human peroxiredoxin 5, a novel type of mammalian RT peroxiredoxin at 1.5-A resolution."; RL J. Mol. Biol. 311:751-759(2001). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 54-214, AND DISULFIDE BOND. RX PubMed=18489898; DOI=10.1016/j.abb.2008.04.036; RA Smeets A., Marchand C., Linard D., Knoops B., Declercq J.P.; RT "The crystal structures of oxidized forms of human peroxiredoxin 5 with an RT intramolecular disulfide bond confirm the proposed enzymatic mechanism for RT atypical 2-Cys peroxiredoxins."; RL Arch. Biochem. Biophys. 477:98-104(2008). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 54-214 IN COMPLEX WITH RP DITHIOTHREITOL, AND ACTIVE SITE. RX PubMed=20643143; DOI=10.1016/j.jmb.2010.07.022; RA Hall A., Parsonage D., Poole L.B., Karplus P.A.; RT "Structural evidence that peroxiredoxin catalytic power is based on RT transition-state stabilization."; RL J. Mol. Biol. 402:194-209(2010). RN [21] RP VARIANT [LARGE SCALE ANALYSIS] LEU-157. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of CC hydrogen peroxide and organic hydroperoxides to water and alcohols, CC respectively. Plays a role in cell protection against oxidative stress CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated CC signaling events. {ECO:0000269|PubMed:10514471, CC ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]- CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA- CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, CC ChEBI:CHEBI:50058; EC=1.11.1.24; CC Evidence={ECO:0000269|PubMed:10751410}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20643143}. CC -!- INTERACTION: CC P30044; P55273: CDKN2D; NbExp=3; IntAct=EBI-722161, EBI-745859; CC P30044; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-722161, EBI-1210753; CC P30044; P49901: SMCP; NbExp=3; IntAct=EBI-722161, EBI-750494; CC P30044; P00441: SOD1; NbExp=10; IntAct=EBI-722161, EBI-990792; CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion CC {ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410}. CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm CC {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10751410}. Peroxisome CC matrix {ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10521424, CC ECO:0000269|PubMed:10751410}. Note=Imported into peroxisomes via CC peroxisomal targeting signal 1 receptor PEX5. CC {ECO:0000269|PubMed:10514471}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=4; CC Name=Mitochondrial; CC IsoId=P30044-1; Sequence=Displayed; CC Name=Cytoplasmic+peroxisomal; CC IsoId=P30044-2; Sequence=VSP_018829; CC Name=3; CC IsoId=P30044-3; Sequence=VSP_045783; CC Name=4; CC IsoId=P30044-4; Sequence=VSP_046682; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10521424}. CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide CC bridge. The disulfide is subsequently reduced by an appropriate CC electron donor to complete the catalytic cycle. In this atypical 2-Cys CC Prx, C(R) is present in the same subunit to form an intramolecular CC disulfide. The disulfide is subsequently reduced by thioredoxin. CC {ECO:0000305|PubMed:10751410, ECO:0000305|PubMed:18489898}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF17200.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/prdx5/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF231705; AAF78899.1; -; mRNA. DR EMBL; AF124993; AAF27531.1; -; mRNA. DR EMBL; AF110731; AAF03750.1; -; mRNA. DR EMBL; AF197952; AAF04856.1; -; mRNA. DR EMBL; AJ249483; CAB62210.1; -; mRNA. DR EMBL; AF242525; AAF99605.1; -; mRNA. DR EMBL; AF112212; AAF17200.1; ALT_FRAME; mRNA. DR EMBL; CR457203; CAG33484.1; -; mRNA. DR EMBL; DQ247769; ABB05181.1; -; Genomic_DNA. DR EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003774; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC110983; AAI10984.1; -; mRNA. DR EMBL; BC113723; AAI13724.1; -; mRNA. DR EMBL; BC113725; AAI13726.1; -; mRNA. DR EMBL; BC143849; AAI43850.1; -; mRNA. DR EMBL; BC171733; AAI71733.1; -; mRNA. DR CCDS; CCDS8069.1; -. [P30044-1] DR CCDS; CCDS8070.1; -. [P30044-3] DR CCDS; CCDS8071.1; -. [P30044-4] DR RefSeq; NP_036226.1; NM_012094.4. [P30044-1] DR RefSeq; NP_857634.1; NM_181651.2. [P30044-3] DR RefSeq; NP_857635.1; NM_181652.2. [P30044-4] DR PDB; 1H4O; X-ray; 1.95 A; A/B/C/D/E/F/G/H=54-214. DR PDB; 1HD2; X-ray; 1.50 A; A=54-214. DR PDB; 1OC3; X-ray; 2.00 A; A/B/C=54-214. DR PDB; 1URM; X-ray; 1.70 A; A=54-214. DR PDB; 2VL2; X-ray; 1.92 A; A/B/C=54-214. DR PDB; 2VL3; X-ray; 1.83 A; A/B/C=54-214. DR PDB; 2VL9; X-ray; 2.70 A; A/B/C/D=54-214. DR PDB; 3MNG; X-ray; 1.45 A; A=54-214. DR PDB; 4K7I; X-ray; 2.25 A; A/B/C=54-214. DR PDB; 4K7N; X-ray; 2.30 A; A/B/C=54-214. DR PDB; 4K7O; X-ray; 1.98 A; A/B/C=54-214. DR PDB; 4MMM; X-ray; 1.47 A; A/C/E/G=54-214. DR PDBsum; 1H4O; -. DR PDBsum; 1HD2; -. DR PDBsum; 1OC3; -. DR PDBsum; 1URM; -. DR PDBsum; 2VL2; -. DR PDBsum; 2VL3; -. DR PDBsum; 2VL9; -. DR PDBsum; 3MNG; -. DR PDBsum; 4K7I; -. DR PDBsum; 4K7N; -. DR PDBsum; 4K7O; -. DR PDBsum; 4MMM; -. DR SMR; P30044; -. DR BioGRID; 117352; 130. DR IntAct; P30044; 41. DR MINT; P30044; -. DR STRING; 9606.ENSP00000265462; -. DR ChEMBL; CHEMBL3627586; -. DR DrugBank; DB00995; Auranofin. DR DrugBank; DB03793; Benzoic acid. DR DrugBank; DB03608; Diminazene. DR DrugBank; DB09221; Polaprezinc. DR PeroxiBase; 4448; HsPrxV. DR iPTMnet; P30044; -. DR MetOSite; P30044; -. DR PhosphoSitePlus; P30044; -. DR SwissPalm; P30044; -. DR BioMuta; PRDX5; -. DR DMDM; 317373539; -. DR OGP; P30044; -. DR REPRODUCTION-2DPAGE; IPI00759663; -. DR SWISS-2DPAGE; P30044; -. DR UCD-2DPAGE; P30044; -. DR CPTAC; CPTAC-572; -. DR EPD; P30044; -. DR jPOST; P30044; -. DR MassIVE; P30044; -. DR MaxQB; P30044; -. DR PaxDb; P30044; -. DR PeptideAtlas; P30044; -. DR PRIDE; P30044; -. DR ProteomicsDB; 1092; -. DR ProteomicsDB; 54624; -. [P30044-1] DR ProteomicsDB; 54625; -. [P30044-2] DR ProteomicsDB; 797; -. DR TopDownProteomics; P30044-1; -. [P30044-1] DR TopDownProteomics; P30044-2; -. [P30044-2] DR Antibodypedia; 3276; 417 antibodies. DR DNASU; 25824; -. DR Ensembl; ENST00000265462; ENSP00000265462; ENSG00000126432. [P30044-1] DR Ensembl; ENST00000347941; ENSP00000335363; ENSG00000126432. [P30044-4] DR Ensembl; ENST00000352435; ENSP00000335334; ENSG00000126432. [P30044-3] DR GeneID; 25824; -. DR KEGG; hsa:25824; -. DR UCSC; uc001nzu.4; human. [P30044-1] DR CTD; 25824; -. DR DisGeNET; 25824; -. DR EuPathDB; HostDB:ENSG00000126432.13; -. DR GeneCards; PRDX5; -. DR HGNC; HGNC:9355; PRDX5. DR HPA; ENSG00000126432; Low tissue specificity. DR MIM; 606583; gene. DR neXtProt; NX_P30044; -. DR OpenTargets; ENSG00000126432; -. DR PharmGKB; PA33726; -. DR eggNOG; KOG0541; Eukaryota. DR eggNOG; COG0678; LUCA. DR GeneTree; ENSGT00390000018173; -. DR HOGENOM; CLU_072440_3_1_1; -. DR InParanoid; P30044; -. DR KO; K11187; -. DR OMA; GYINHPK; -. DR OrthoDB; 1281610at2759; -. DR PhylomeDB; P30044; -. DR TreeFam; TF105182; -. DR BRENDA; 1.11.1.15; 2681. DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. [P30044-2] DR SIGNOR; P30044; -. DR BioGRID-ORCS; 25824; 6 hits in 793 CRISPR screens. DR ChiTaRS; PRDX5; human. DR EvolutionaryTrace; P30044; -. DR GeneWiki; PRDX5; -. DR GenomeRNAi; 25824; -. DR Pharos; P30044; Tbio. DR PRO; PR:P30044; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P30044; protein. DR Bgee; ENSG00000126432; Expressed in bronchial epithelial cell and 190 other tissues. DR Genevisible; P30044; HS. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB. DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB. DR GO; GO:0051920; F:peroxiredoxin activity; IDA:UniProtKB. DR GO; GO:0072541; F:peroxynitrite reductase activity; IDA:UniProtKB. DR GO; GO:0001016; F:RNA polymerase III regulatory region DNA binding; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0008379; F:thioredoxin peroxidase activity; EXP:Reactome. DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central. DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB. DR GO; GO:0070995; P:NADPH oxidation; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB. DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IDA:UniProtKB. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB. DR GO; GO:2001057; P:reactive nitrogen species metabolic process; IDA:UniProtKB. DR GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IDA:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB. DR CDD; cd03013; PRX5_like; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR037944; PRX5-like. DR InterPro; IPR013740; Redoxin. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10430; PTHR10430; 1. DR Pfam; PF08534; Redoxin; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing; KW Antioxidant; Cytoplasm; Direct protein sequencing; Disulfide bond; KW Mitochondrion; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein; KW Polymorphism; Redox-active center; Reference proteome; Transit peptide. FT TRANSIT 1..52 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 53..214 FT /note="Peroxiredoxin-5, mitochondrial" FT /id="PRO_0000023793" FT DOMAIN 56..214 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT MOTIF 212..214 FT /note="Microbody targeting signal" FT /evidence="ECO:0000305|PubMed:10514471" FT ACT_SITE 100 FT /note="Cysteine sulfenic acid (-SOH) intermediate" FT /evidence="ECO:0000305|PubMed:10751410, FT ECO:0000305|PubMed:20643143" FT MOD_RES 75 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P99029" FT MOD_RES 83 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000244|PubMed:19608861" FT MOD_RES 83 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P99029" FT MOD_RES 116 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P99029" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R063" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P99029" FT DISULFID 100..204 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691, FT ECO:0000269|PubMed:10751410, ECO:0000269|PubMed:18489898" FT VAR_SEQ 1..52 FT /note="Missing (in isoform Cytoplasmic+peroxisomal)" FT /evidence="ECO:0000303|PubMed:10514471, FT ECO:0000303|PubMed:10679306, ECO:0000303|PubMed:10931946, FT ECO:0000303|Ref.6" FT /id="VSP_018829" FT VAR_SEQ 57..145 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046682" FT VAR_SEQ 102..145 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045783" FT VARIANT 33 FT /note="Y -> C (in dbSNP:rs7938623)" FT /evidence="ECO:0000269|PubMed:10095767, FT ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10679306, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.10, FT ECO:0000269|Ref.7, ECO:0000269|Ref.9" FT /id="VAR_025049" FT VARIANT 157 FT /note="F -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036406" FT MUTAGEN 100 FT /note="C->S: Complete loss of activity." FT /evidence="ECO:0000269|PubMed:10751410" FT MUTAGEN 125 FT /note="C->S: No change in activity." FT /evidence="ECO:0000269|PubMed:10751410" FT MUTAGEN 204 FT /note="C->S: Complete loss of activity." FT /evidence="ECO:0000269|PubMed:10751410" FT CONFLICT 141 FT /note="H -> T (in Ref. 4; AAF04856)" FT /evidence="ECO:0000305" FT STRAND 66..68 FT /evidence="ECO:0000244|PDB:3MNG" FT HELIX 72..74 FT /evidence="ECO:0000244|PDB:2VL9" FT STRAND 75..77 FT /evidence="ECO:0000244|PDB:3MNG" FT HELIX 78..81 FT /evidence="ECO:0000244|PDB:3MNG" FT TURN 82..84 FT /evidence="ECO:0000244|PDB:3MNG" FT STRAND 85..91 FT /evidence="ECO:0000244|PDB:3MNG" FT HELIX 98..102 FT /evidence="ECO:0000244|PDB:3MNG" FT HELIX 104..110 FT /evidence="ECO:0000244|PDB:3MNG" FT HELIX 112..116 FT /evidence="ECO:0000244|PDB:3MNG" FT TURN 117..119 FT /evidence="ECO:0000244|PDB:3MNG" FT STRAND 122..129 FT /evidence="ECO:0000244|PDB:3MNG" FT HELIX 131..140 FT /evidence="ECO:0000244|PDB:3MNG" FT TURN 144..146 FT /evidence="ECO:0000244|PDB:3MNG" FT STRAND 148..151 FT /evidence="ECO:0000244|PDB:3MNG" FT HELIX 156..161 FT /evidence="ECO:0000244|PDB:3MNG" FT HELIX 167..169 FT /evidence="ECO:0000244|PDB:4MMM" FT HELIX 170..173 FT /evidence="ECO:0000244|PDB:3MNG" FT STRAND 181..186 FT /evidence="ECO:0000244|PDB:3MNG" FT STRAND 189..195 FT /evidence="ECO:0000244|PDB:3MNG" FT STRAND 199..203 FT /evidence="ECO:0000244|PDB:4MMM" FT HELIX 207..213 FT /evidence="ECO:0000244|PDB:3MNG" SQ SEQUENCE 214 AA; 22086 MW; DA1DEB21120254EE CRC64; MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS GGVRSFSRAA AAMAPIKVGD AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL //