ID PRDX6_HUMAN Reviewed; 224 AA. AC P30041; A8JZY7; P32077; Q5TAH4; Q5ZEZ8; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-NOV-2015, entry version 172. DE RecName: Full=Peroxiredoxin-6; DE EC=1.11.1.15; DE AltName: Full=1-Cys peroxiredoxin; DE Short=1-Cys PRX; DE AltName: Full=24 kDa protein; DE AltName: Full=Acidic calcium-independent phospholipase A2; DE Short=aiPLA2; DE EC=3.1.1.-; DE AltName: Full=Antioxidant protein 2; DE AltName: Full=Liver 2D page spot 40; DE AltName: Full=Non-selenium glutathione peroxidase; DE Short=NSGPx; DE EC=1.11.1.9; DE AltName: Full=Red blood cells page spot 12; GN Name=PRDX6; Synonyms=AOP2, KIAA0106; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8999971; DOI=10.1074/jbc.272.4.2542; RA Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., RA Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.; RT "Identification of a human cDNA clone for lysosomal type Ca2+- RT independent phospholipase A2 and properties of the expressed RT protein."; RL J. Biol. Chem. 272:2542-2550(1997). RN [2] RP ERRATUM. RA Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., RA Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.; RL J. Biol. Chem. 272:10981-10981(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9050990; DOI=10.1038/sj.onc.1200905; RA Frank S., Munz B., Werner S.; RT "The human homologue of a bovine non-selenium glutathione peroxidase RT is a novel keratinocyte growth factor-regulated gene."; RL Oncogene 14:915-921(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; RX PubMed=7788527; DOI=10.1093/dnares/2.1.37; RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. III. RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 2:37-43(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal brain, and Testis; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PROTEIN SEQUENCE OF 2-22. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [11] RP PROTEIN SEQUENCE OF 2-22; 25-53; 85-106; 133-142; 145-155; 163-173 AND RP 175-199, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [12] RP PROTEIN SEQUENCE OF 2-15. 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 [13] RP PROTEIN SEQUENCE OF 2-13. RC TISSUE=Erythrocyte; RX PubMed=8313871; DOI=10.1002/elps.11501401183; RA Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., RA Balant L., Hochstrasser D.F.; RT "Plasma and red blood cell protein maps: update 1993."; RL Electrophoresis 14:1223-1231(1993). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-99. RA Dominguez O., Lombardia L.; RT "DNA probes built and sequenced for microarrays hybridisations."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [15] RP CHARACTERIZATION, AND MUTAGENESIS. RX PubMed=9497358; DOI=10.1074/jbc.273.11.6303; RA Kang S.W., Baines I.C., Rhee S.G.; RT "Characterization of a mammalian peroxiredoxin that contains one RT conserved cysteine."; RL J. Biol. Chem. 273:6303-6311(1998). RN [16] RP CHARACTERIZATION, AND MUTAGENESIS. RX PubMed=10893423; DOI=10.1074/jbc.M005073200; RA Chen J.-W., Dodia C., Feinstein S.I., Jain M.K., Fisher A.B.; RT "1-Cys peroxiredoxin, a bifunctional enzyme with glutathione RT peroxidase and phospholipase A2 activities."; RL J. Biol. Chem. 275:28421-28427(2000). RN [17] RP OVEROXIDATION AT CYS-47. RX PubMed=12059788; DOI=10.1042/BJ20020525; RA Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., RA Leize-Wagner E., Rabilloud T.; RT "A method for detection of overoxidation of cysteines: peroxiredoxins RT are oxidized in vivo at the active-site cysteine during oxidative RT stress."; RL Biochem. J. 366:777-785(2002). RN [18] RP SUBCELLULAR LOCATION, AND INTERACTION WITH STH. RX PubMed=16186110; DOI=10.1074/jbc.M506116200; RA Gao L., Tse S.-W., Conrad C., Andreadis A.; RT "Saitohin, which is nested in the tau locus and confers allele- RT specific susceptibility to several neurodegenerative diseases, RT interacts with peroxiredoxin 6."; RL J. Biol. Chem. 280:39268-39272(2005). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [21] RP INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND RP SUBCELLULAR LOCATION. RX PubMed=19188445; DOI=10.1128/MCB.01337-08; RA Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., RA Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., RA Quadrifoglio F., Tell G.; RT "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in RT the rRNA quality control process."; RL Mol. Cell. Biol. 29:1834-1854(2009). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63 AND LYS-209, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [24] 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., RA Buerckstuemmer T., 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 [25] RP INTERACTION WITH FAM168B. RX PubMed=20716133; DOI=10.1111/j.1582-4934.2010.01134.x; RA Mishra M., Akatsu H., Heese K.; RT "The novel protein MANI modulates neurogenesis and neurite-cone RT growth."; RL J. Cell. Mol. Med. 15:1713-1725(2011). RN [26] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., RA Fischer-Posovszky P., Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion RT profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [27] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [29] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [30] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND 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., RA Ayoub D., 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 [31] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=9587003; DOI=10.1038/nsb0598-400; RA Choi H.-J., Kang S.W., Yang C.-H., Rhee S.G., Ryu S.-E.; RT "Crystal structure of a novel human peroxidase enzyme at 2.0-A RT resolution."; RL Nat. Struct. Biol. 5:400-406(1998). CC -!- FUNCTION: Involved in redox regulation of the cell. Can reduce CC H(2)O(2) and short chain organic, fatty acid, and phospholipid CC hydroperoxides. May play a role in the regulation of phospholipid CC turnover as well as in protection against oxidative injury. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione CC disulfide + 2 H(2)O. CC -!- SUBUNIT: Homotetramer. Interacts with GSTP1; mediates PRDX6 CC glutathionylation and regeneration. May interact with HTR2A (By CC similarity). Interacts with APEX1 and STH. May interact with CC FAM168B. {ECO:0000250, ECO:0000269|PubMed:16186110, CC ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20716133}. CC -!- INTERACTION: CC P29991:- (xeno); NbExp=3; IntAct=EBI-2255129, EBI-8826747; CC P09211:GSTP1; NbExp=2; IntAct=EBI-2255129, EBI-353467; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16186110, CC ECO:0000269|PubMed:19188445}. Lysosome {ECO:0000250}. Cytoplasmic CC vesicle {ECO:0000250}. Note=Also found in lung secretory CC organelles. {ECO:0000250}. CC -!- MISCELLANEOUS: The active site is the redox-active Cys-47 oxidized CC to Cys-SOH. Unlike 2-Cys peroxiredoxins, PRDX6 conserves only this CC peroxidatic cysteine. To regenerate and activate the enzyme, the CC oxidized form is directly reduced to cysteine by glutathione and CC not thioredoxin. CC -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-47 CC (to Cys-SO(3)H) upon oxidative stress. CC -!- SIMILARITY: Belongs to the AhpC/TSA family. Rehydrin subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00691}. CC -!- WEB RESOURCE: Name=NIEHS SNPs; CC URL="http://egp.gs.washington.edu/data/prdx6/"; 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; D14662; BAA03496.1; -; mRNA. DR EMBL; DQ230990; ABB02185.1; -; Genomic_DNA. DR EMBL; AL139142; CAI20936.1; -; Genomic_DNA. DR EMBL; AK289352; BAF82041.1; -; mRNA. DR EMBL; CH471067; EAW90944.1; -; Genomic_DNA. DR EMBL; BC035857; AAH35857.1; -; mRNA. DR EMBL; BC053550; AAH53550.1; -; mRNA. DR EMBL; AJ844621; CAH59743.1; -; mRNA. DR CCDS; CCDS1307.1; -. DR RefSeq; NP_004896.1; NM_004905.2. DR UniGene; Hs.120; -. DR UniGene; Hs.731505; -. DR PDB; 1PRX; X-ray; 2.00 A; A/B=1-224. DR PDBsum; 1PRX; -. DR ProteinModelPortal; P30041; -. DR SMR; P30041; 5-224. DR BioGrid; 114956; 51. DR IntAct; P30041; 19. DR MINT; MINT-4999165; -. DR STRING; 9606.ENSP00000342026; -. DR PeroxiBase; 4426; Hs1CysPrx01. DR PhosphoSite; P30041; -. DR BioMuta; PRDX6; -. DR DMDM; 1718024; -. DR DOSAC-COBS-2DPAGE; P30041; -. DR OGP; P30041; -. DR REPRODUCTION-2DPAGE; IPI00220301; -. DR REPRODUCTION-2DPAGE; P30041; -. DR SWISS-2DPAGE; P30041; -. DR PaxDb; P30041; -. DR PeptideAtlas; P30041; -. DR PRIDE; P30041; -. DR DNASU; 9588; -. DR Ensembl; ENST00000340385; ENSP00000342026; ENSG00000117592. DR GeneID; 9588; -. DR KEGG; hsa:9588; -. DR UCSC; uc001giy.1; human. DR CTD; 9588; -. DR GeneCards; PRDX6; -. DR H-InvDB; HIX0028696; -. DR HGNC; HGNC:16753; PRDX6. DR HPA; CAB008663; -. DR HPA; HPA006983; -. DR MIM; 602316; gene. DR neXtProt; NX_P30041; -. DR PharmGKB; PA134992760; -. DR eggNOG; KOG0854; Eukaryota. DR eggNOG; COG0450; LUCA. DR HOGENOM; HOG000022346; -. DR HOVERGEN; HBG105234; -. DR InParanoid; P30041; -. DR KO; K11188; -. DR OMA; IRFHDYL; -. DR OrthoDB; EOG7CNZGP; -. DR PhylomeDB; P30041; -. DR TreeFam; TF105183; -. DR BRENDA; 1.11.1.15; 2681. DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species. DR ChiTaRS; PRDX6; human. DR EvolutionaryTrace; P30041; -. DR GeneWiki; PRDX6; -. DR GenomeRNAi; 9588; -. DR NextBio; 35979; -. DR PRO; PR:P30041; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P30041; -. DR CleanEx; HS_PRDX6; -. DR ExpressionAtlas; P30041; baseline and differential. DR Genevisible; P30041; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; NAS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0016209; F:antioxidant activity; NAS:UniProtKB. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC. DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl. DR GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB. DR GO; GO:0000302; P:response to reactive oxygen species; TAS:Reactome. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Antioxidant; Complete proteome; Cytoplasm; KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; KW Hydrolase; Lipid degradation; Lipid metabolism; Lysosome; KW Multifunctional enzyme; Oxidoreductase; Peroxidase; Phosphoprotein; KW Redox-active center; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:25944712, FT ECO:0000269|PubMed:12665801, FT ECO:0000269|PubMed:1286669, FT ECO:0000269|PubMed:8313871, FT ECO:0000269|Ref.11}. FT CHAIN 2 224 Peroxiredoxin-6. FT /FTId=PRO_0000135102. FT DOMAIN 5 169 Thioredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00691}. FT ACT_SITE 32 32 For phospholipase activity. FT ACT_SITE 47 47 Cysteine sulfenic acid (-SOH) FT intermediate. FT MOD_RES 44 44 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 63 63 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 89 89 Phosphotyrosine. FT {ECO:0000244|PubMed:15592455}. FT MOD_RES 209 209 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 209 209 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:O08709}. FT DISULFID 47 47 Interchain; in linked form. FT {ECO:0000250}. FT MUTAGEN 32 32 S->A: Loss of AIPLA2 activity, but no FT effect on NSGPX activity. FT MUTAGEN 47 47 C->S: Loss of NSGPX activity, but no FT effect on AIPLA2 activity. FT STRAND 15 18 {ECO:0000244|PDB:1PRX}. FT STRAND 21 24 {ECO:0000244|PDB:1PRX}. FT HELIX 25 29 {ECO:0000244|PDB:1PRX}. FT STRAND 32 40 {ECO:0000244|PDB:1PRX}. FT HELIX 45 62 {ECO:0000244|PDB:1PRX}. FT TURN 63 65 {ECO:0000244|PDB:1PRX}. FT STRAND 66 74 {ECO:0000244|PDB:1PRX}. FT HELIX 76 89 {ECO:0000244|PDB:1PRX}. FT STRAND 102 104 {ECO:0000244|PDB:1PRX}. FT HELIX 109 113 {ECO:0000244|PDB:1PRX}. FT STRAND 124 126 {ECO:0000244|PDB:1PRX}. FT STRAND 133 137 {ECO:0000244|PDB:1PRX}. FT STRAND 141 148 {ECO:0000244|PDB:1PRX}. FT HELIX 157 173 {ECO:0000244|PDB:1PRX}. FT STRAND 175 177 {ECO:0000244|PDB:1PRX}. FT STRAND 187 189 {ECO:0000244|PDB:1PRX}. FT HELIX 195 201 {ECO:0000244|PDB:1PRX}. FT STRAND 219 221 {ECO:0000244|PDB:1PRX}. SQ SEQUENCE 224 AA; 25035 MW; 017D955F0FEEDFBC CRC64; MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF PIIDDRNREL AILLGMLDPA EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP //