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Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (24 kDa protein) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Liver 2D page spot 40) (Non-selenium glutathione peroxidase) (NSGPx) (Red blood cells page spot 12)

 PRDX6_HUMAN             Reviewed;         224 AA.
P30041; A8JZY7; P32077; Q5TAH4; Q5ZEZ8;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 192.
RecName: Full=Peroxiredoxin-6;
EC=1.11.1.15 {ECO:0000269|PubMed:10893423, ECO:0000269|PubMed:9497358};
AltName: Full=1-Cys peroxiredoxin;
Short=1-Cys PRX;
AltName: Full=24 kDa protein;
AltName: Full=Acidic calcium-independent phospholipase A2;
Short=aiPLA2;
EC=3.1.1.4 {ECO:0000269|PubMed:10893423};
AltName: Full=Antioxidant protein 2;
AltName: Full=Liver 2D page spot 40;
AltName: Full=Non-selenium glutathione peroxidase;
Short=NSGPx;
AltName: Full=Red blood cells page spot 12;
Name=PRDX6; Synonyms=AOP2, KIAA0106;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8999971; DOI=10.1074/jbc.272.4.2542;
Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R.,
Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.;
"Identification of a human cDNA clone for lysosomal type Ca2+-
independent phospholipase A2 and properties of the expressed
protein.";
J. Biol. Chem. 272:2542-2550(1997).
[2]
ERRATUM.
Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R.,
Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.;
J. Biol. Chem. 272:10981-10981(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9050990; DOI=10.1038/sj.onc.1200905;
Frank S., Munz B., Werner S.;
"The human homologue of a bovine non-selenium glutathione peroxidase
is a novel keratinocyte growth factor-regulated gene.";
Oncogene 14:915-921(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain, and Testis;
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).
[10]
PROTEIN SEQUENCE OF 2-22.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[11]
PROTEIN SEQUENCE OF 2-22; 25-53; 85-106; 133-142; 145-155; 163-173 AND
175-199, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
PROTEIN SEQUENCE OF 2-15.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[13]
PROTEIN SEQUENCE OF 2-13.
TISSUE=Erythrocyte;
PubMed=8313871; DOI=10.1002/elps.11501401183;
Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C.,
Balant L., Hochstrasser D.F.;
"Plasma and red blood cell protein maps: update 1993.";
Electrophoresis 14:1223-1231(1993).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-99.
Dominguez O., Lombardia L.;
"DNA probes built and sequenced for microarrays hybridisations.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[15]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
CYS-47.
PubMed=9497358; DOI=10.1074/jbc.273.11.6303;
Kang S.W., Baines I.C., Rhee S.G.;
"Characterization of a mammalian peroxiredoxin that contains one
conserved cysteine.";
J. Biol. Chem. 273:6303-6311(1998).
[16]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-32 AND CYS-47.
PubMed=10893423; DOI=10.1074/jbc.M005073200;
Chen J.-W., Dodia C., Feinstein S.I., Jain M.K., Fisher A.B.;
"1-Cys peroxiredoxin, a bifunctional enzyme with glutathione
peroxidase and phospholipase A2 activities.";
J. Biol. Chem. 275:28421-28427(2000).
[17]
OVEROXIDATION AT CYS-47.
PubMed=12059788; DOI=10.1042/BJ20020525;
Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A.,
Leize-Wagner E., Rabilloud T.;
"A method for detection of overoxidation of cysteines: peroxiredoxins
are oxidized in vivo at the active-site cysteine during oxidative
stress.";
Biochem. J. 366:777-785(2002).
[18]
SUBCELLULAR LOCATION, AND INTERACTION WITH STH.
PubMed=16186110; DOI=10.1074/jbc.M506116200;
Gao L., Tse S.-W., Conrad C., Andreadis A.;
"Saitohin, which is nested in the tau locus and confers allele-
specific susceptibility to several neurodegenerative diseases,
interacts with peroxiredoxin 6.";
J. Biol. Chem. 280:39268-39272(2005).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=19188445; DOI=10.1128/MCB.01337-08;
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
Quadrifoglio F., Tell G.;
"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in
the rRNA quality control process.";
Mol. Cell. Biol. 29:1834-1854(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63 AND LYS-209, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
INTERACTION WITH FAM168B.
PubMed=20716133; DOI=10.1111/j.1582-4934.2010.01134.x;
Mishra M., Akatsu H., Heese K.;
"The novel protein MANI modulates neurogenesis and neurite-cone
growth.";
J. Cell. Mol. Med. 15:1713-1725(2011).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[27]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), ACTIVE SITE, AND SUBUNIT.
PubMed=9587003; DOI=10.1038/nsb0598-400;
Choi H.-J., Kang S.W., Yang C.-H., Rhee S.G., Ryu S.-E.;
"Crystal structure of a novel human peroxidase enzyme at 2.0-A
resolution.";
Nat. Struct. Biol. 5:400-406(1998).
[33]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-224, AND SUBUNIT.
PubMed=27353378; DOI=10.1016/j.bbrc.2016.06.125;
Kim K.H., Lee W., Kim E.E.;
"Crystal structures of human peroxiredoxin 6 in different oxidation
states.";
Biochem. Biophys. Res. Commun. 477:717-722(2016).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Can reduce H(2)O(2) and short chain
organic, fatty acid, and phospholipid hydroperoxides. Also has
phospholipase activity, and can therefore either reduce the
oxidized sn-2 fatty acyl grup of phospholipids (peroxidase
activity) or hydrolyze the sn-2 ester bond of phospholipids
(phospholipase activity). These activities are dependent on
binding to phospholipids at acidic pH and to oxidized phospholipds
at cytosolic pH. Plays a role in cell protection against oxidative
stress by detoxifying peroxides and in phospholipid homeostasis.
{ECO:0000269|PubMed:10893423, ECO:0000269|PubMed:9497358}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:10893423, ECO:0000269|PubMed:9497358}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate.
{ECO:0000269|PubMed:10893423}.
-!- SUBUNIT: Homodimer (PubMed:9587003, PubMed:27353378). Interacts
with GSTP1; mediates PRDX6 glutathionylation and regeneration (By
similarity). Interacts with APEX1 (PubMed:19188445). Interacts
with STH (PubMed:16186110). May interact with FAM168B
(PubMed:20716133). May interact with HTR2A (By similarity).
{ECO:0000250|UniProtKB:O08709, ECO:0000250|UniProtKB:O77834,
ECO:0000269|PubMed:16186110, ECO:0000269|PubMed:19188445,
ECO:0000269|PubMed:20716133, ECO:0000269|PubMed:27353378,
ECO:0000269|PubMed:9587003}.
-!- INTERACTION:
P29991:- (xeno); NbExp=3; IntAct=EBI-2255129, EBI-8826747;
P09211:GSTP1; NbExp=2; IntAct=EBI-2255129, EBI-353467;
P54274:TERF1; NbExp=2; IntAct=EBI-2255129, EBI-710997;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16186110,
ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:9497358}. Lysosome
{ECO:0000250|UniProtKB:O35244}. Note=Also found in lung secretory
organelles (lamellar bodies). {ECO:0000250|UniProtKB:O35244}.
-!- PTM: Irreversibly inactivated by overoxidation of Cys-47 to
sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms
upon oxidative stress. {ECO:0000269|PubMed:12059788,
ECO:0000269|PubMed:27353378}.
-!- PTM: Phosphorylation at Thr-177 by MAP kinases increases the
phospholipase activity of the enzyme.
{ECO:0000250|UniProtKB:O35244}.
-!- 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 1-Cys peroxiredoxin, no C(R) is present and C(P)
instead forms a disulfide with a cysteine from another protein or
with a small thiol molecule. C(P) is reactivated by
glutathionylation mediated by glutathione S-transferase Pi,
followed by spontaneous reduction of the enzyme with glutathione.
{ECO:0000250|UniProtKB:O35244}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS SNPs;
URL="http://egp.gs.washington.edu/data/prdx6/";
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EMBL; D14662; BAA03496.1; -; mRNA.
EMBL; DQ230990; ABB02185.1; -; Genomic_DNA.
EMBL; AL139142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK289352; BAF82041.1; -; mRNA.
EMBL; CH471067; EAW90944.1; -; Genomic_DNA.
EMBL; BC035857; AAH35857.1; -; mRNA.
EMBL; BC053550; AAH53550.1; -; mRNA.
EMBL; AJ844621; CAH59743.1; -; mRNA.
CCDS; CCDS1307.1; -.
RefSeq; NP_004896.1; NM_004905.2.
UniGene; Hs.120; -.
UniGene; Hs.731505; -.
PDB; 1PRX; X-ray; 2.00 A; A/B=1-224.
PDB; 5B6M; X-ray; 2.50 A; A/B/C/D/E/F=1-224.
PDB; 5B6N; X-ray; 2.90 A; A/B/C/D/E/F=1-224.
PDBsum; 1PRX; -.
PDBsum; 5B6M; -.
PDBsum; 5B6N; -.
ProteinModelPortal; P30041; -.
SMR; P30041; -.
BioGrid; 114956; 83.
IntAct; P30041; 26.
MINT; MINT-4999165; -.
STRING; 9606.ENSP00000342026; -.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DrugBank; DB02325; Isopropyl Alcohol.
SwissLipids; SLP:000001691; -.
PeroxiBase; 4426; Hs1CysPrx01.
iPTMnet; P30041; -.
PhosphoSitePlus; P30041; -.
SwissPalm; P30041; -.
BioMuta; PRDX6; -.
DMDM; 1718024; -.
DOSAC-COBS-2DPAGE; P30041; -.
OGP; P30041; -.
REPRODUCTION-2DPAGE; IPI00220301; -.
REPRODUCTION-2DPAGE; P30041; -.
SWISS-2DPAGE; P30041; -.
EPD; P30041; -.
PaxDb; P30041; -.
PeptideAtlas; P30041; -.
PRIDE; P30041; -.
TopDownProteomics; P30041; -.
DNASU; 9588; -.
Ensembl; ENST00000340385; ENSP00000342026; ENSG00000117592.
GeneID; 9588; -.
KEGG; hsa:9588; -.
CTD; 9588; -.
DisGeNET; 9588; -.
EuPathDB; HostDB:ENSG00000117592.8; -.
GeneCards; PRDX6; -.
H-InvDB; HIX0028696; -.
HGNC; HGNC:16753; PRDX6.
HPA; CAB008663; -.
HPA; HPA006983; -.
MIM; 602316; gene.
neXtProt; NX_P30041; -.
OpenTargets; ENSG00000117592; -.
PharmGKB; PA134992760; -.
eggNOG; KOG0854; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00550000074794; -.
HOGENOM; HOG000022346; -.
HOVERGEN; HBG105234; -.
InParanoid; P30041; -.
KO; K11188; -.
OMA; YPIIADD; -.
OrthoDB; EOG091G0IWK; -.
PhylomeDB; P30041; -.
TreeFam; TF105183; -.
BRENDA; 1.11.1.15; 2681.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P30041; -.
ChiTaRS; PRDX6; human.
EvolutionaryTrace; P30041; -.
GeneWiki; PRDX6; -.
GenomeRNAi; 9588; -.
PRO; PR:P30041; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117592; -.
CleanEx; HS_PRDX6; -.
ExpressionAtlas; P30041; baseline and differential.
Genevisible; P30041; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IMP:CAFA.
GO; GO:0004602; F:glutathione peroxidase activity; IMP:CAFA.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0098869; P:cellular oxidant detoxification; IMP:CAFA.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0046475; P:glycerophospholipid catabolic process; IMP:CAFA.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IGI:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IMP:CAFA.
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;
3D-structure; Acetylation; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Lipid degradation;
Lipid metabolism; Lysosome; Multifunctional enzyme; Oxidoreductase;
Peroxidase; Phosphoprotein; Redox-active center; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:1286669,
ECO:0000269|PubMed:8313871,
ECO:0000269|Ref.11}.
CHAIN 2 224 Peroxiredoxin-6.
/FTId=PRO_0000135102.
DOMAIN 5 169 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
REGION 31 40 Required and sufficient for targeting to
lysosomes and lamellar bodies.
{ECO:0000250|UniProtKB:O35244}.
ACT_SITE 47 47 Cysteine sulfenic acid (-SOH)
intermediate; for peroxidase activity.
{ECO:0000269|PubMed:10893423,
ECO:0000269|PubMed:9497358,
ECO:0000269|PubMed:9587003}.
ACT_SITE 140 140 For phospholipase activity.
{ECO:0000250|UniProtKB:O35244}.
SITE 32 32 Important for phospholipase activity.
{ECO:0000305|PubMed:10893423}.
MOD_RES 44 44 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 63 63 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 89 89 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 177 177 Phosphothreonine; by MAPK.
{ECO:0000250|UniProtKB:O35244}.
MOD_RES 209 209 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 209 209 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08709}.
MUTAGEN 32 32 S->A: Loss of phospholipase activity, but
no effect on peroxidase activity.
{ECO:0000269|PubMed:9497358}.
MUTAGEN 47 47 C->S: Loss of peroxidase activity, but no
effect on phospholipase activity.
{ECO:0000269|PubMed:9497358}.
STRAND 15 18 {ECO:0000244|PDB:1PRX}.
STRAND 21 24 {ECO:0000244|PDB:1PRX}.
HELIX 25 29 {ECO:0000244|PDB:1PRX}.
STRAND 32 40 {ECO:0000244|PDB:1PRX}.
HELIX 45 62 {ECO:0000244|PDB:1PRX}.
TURN 63 65 {ECO:0000244|PDB:1PRX}.
STRAND 66 74 {ECO:0000244|PDB:1PRX}.
HELIX 76 89 {ECO:0000244|PDB:1PRX}.
STRAND 102 104 {ECO:0000244|PDB:1PRX}.
HELIX 109 113 {ECO:0000244|PDB:1PRX}.
STRAND 117 122 {ECO:0000244|PDB:5B6M}.
STRAND 124 126 {ECO:0000244|PDB:1PRX}.
STRAND 128 130 {ECO:0000244|PDB:5B6M}.
STRAND 133 137 {ECO:0000244|PDB:1PRX}.
STRAND 141 148 {ECO:0000244|PDB:1PRX}.
STRAND 151 153 {ECO:0000244|PDB:5B6N}.
HELIX 157 173 {ECO:0000244|PDB:1PRX}.
STRAND 175 177 {ECO:0000244|PDB:1PRX}.
STRAND 187 189 {ECO:0000244|PDB:1PRX}.
HELIX 195 201 {ECO:0000244|PDB:1PRX}.
STRAND 219 221 {ECO:0000244|PDB:1PRX}.
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


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