Full text data of PRDX6
PRDX6
(AOP2, KIAA0106)
[Confidence: high (present in two of the MS resources)]
Peroxiredoxin-6; 1.11.1.15 (1-Cys peroxiredoxin; 1-Cys PRX; 24 kDa protein; Acidic calcium-independent phospholipase A2; aiPLA2; 3.1.1.-; Antioxidant protein 2; Liver 2D page spot 40; Non-selenium glutathione peroxidase; NSGPx; 1.11.1.9; Red blood cells page spot 12)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Peroxiredoxin-6; 1.11.1.15 (1-Cys peroxiredoxin; 1-Cys PRX; 24 kDa protein; Acidic calcium-independent phospholipase A2; aiPLA2; 3.1.1.-; Antioxidant protein 2; Liver 2D page spot 40; Non-selenium glutathione peroxidase; NSGPx; 1.11.1.9; Red blood cells page spot 12)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00220301
IPI00220301 Antioxidant protein 2 Peroxiredoxin 6, Involved in redox regulation of the cell, red blood cell protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00220301 Antioxidant protein 2 Peroxiredoxin 6, Involved in redox regulation of the cell, red blood cell protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P30041
ID PRDX6_HUMAN Reviewed; 224 AA.
AC P30041; A8JZY7; P32077; Q5TAH4; Q5ZEZ8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 152.
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 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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=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 [27]
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.
CC -!- INTERACTION:
CC P29991:- (xeno); NbExp=3; IntAct=EBI-2255129, EBI-8826747;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome (By similarity).
CC Cytoplasmic vesicle (By similarity). Note=Also found in lung
CC secretory organelles (By similarity).
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 -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -!- WEB RESOURCE: Name=NIEHS SNPs;
CC URL="http://egp.gs.washington.edu/data/prdx6/";
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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 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 IntAct; P30041; 17.
DR MINT; MINT-4999165; -.
DR STRING; 9606.ENSP00000342026; -.
DR PeroxiBase; 4426; Hs1CysPrx01.
DR PhosphoSite; P30041; -.
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; GC01P173446; -.
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; COG0450; -.
DR HOGENOM; HOG000022346; -.
DR HOVERGEN; HBG105234; -.
DR InParanoid; P30041; -.
DR KO; K11188; -.
DR OMA; HPNANDT; -.
DR OrthoDB; EOG7CNZGP; -.
DR PhylomeDB; P30041; -.
DR BRENDA; 1.11.1.15; 2681.
DR ChiTaRS; PRDX6; human.
DR EvolutionaryTrace; P30041; -.
DR GeneWiki; PRDX6; -.
DR GenomeRNAi; 9588; -.
DR NextBio; 35979; -.
DR PRO; PR:P30041; -.
DR Bgee; P30041; -.
DR CleanEx; HS_PRDX6; -.
DR Genevestigator; P30041; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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: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 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.
FT CHAIN 2 224 Peroxiredoxin-6.
FT /FTId=PRO_0000135102.
FT DOMAIN 5 169 Thioredoxin.
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 MOD_RES 63 63 N6-acetyllysine.
FT MOD_RES 89 89 Phosphotyrosine.
FT MOD_RES 209 209 N6-acetyllysine.
FT DISULFID 47 47 Interchain; in linked form (By
FT similarity).
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
FT STRAND 21 24
FT HELIX 25 29
FT STRAND 32 40
FT HELIX 45 62
FT TURN 63 65
FT STRAND 66 74
FT HELIX 76 89
FT STRAND 102 104
FT HELIX 109 113
FT STRAND 124 126
FT STRAND 133 137
FT STRAND 141 148
FT HELIX 157 173
FT STRAND 175 177
FT STRAND 187 189
FT HELIX 195 201
FT STRAND 219 221
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
//
ID PRDX6_HUMAN Reviewed; 224 AA.
AC P30041; A8JZY7; P32077; Q5TAH4; Q5ZEZ8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 152.
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 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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=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 [27]
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.
CC -!- INTERACTION:
CC P29991:- (xeno); NbExp=3; IntAct=EBI-2255129, EBI-8826747;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome (By similarity).
CC Cytoplasmic vesicle (By similarity). Note=Also found in lung
CC secretory organelles (By similarity).
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 -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -!- WEB RESOURCE: Name=NIEHS SNPs;
CC URL="http://egp.gs.washington.edu/data/prdx6/";
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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 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 IntAct; P30041; 17.
DR MINT; MINT-4999165; -.
DR STRING; 9606.ENSP00000342026; -.
DR PeroxiBase; 4426; Hs1CysPrx01.
DR PhosphoSite; P30041; -.
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; GC01P173446; -.
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; COG0450; -.
DR HOGENOM; HOG000022346; -.
DR HOVERGEN; HBG105234; -.
DR InParanoid; P30041; -.
DR KO; K11188; -.
DR OMA; HPNANDT; -.
DR OrthoDB; EOG7CNZGP; -.
DR PhylomeDB; P30041; -.
DR BRENDA; 1.11.1.15; 2681.
DR ChiTaRS; PRDX6; human.
DR EvolutionaryTrace; P30041; -.
DR GeneWiki; PRDX6; -.
DR GenomeRNAi; 9588; -.
DR NextBio; 35979; -.
DR PRO; PR:P30041; -.
DR Bgee; P30041; -.
DR CleanEx; HS_PRDX6; -.
DR Genevestigator; P30041; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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: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 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.
FT CHAIN 2 224 Peroxiredoxin-6.
FT /FTId=PRO_0000135102.
FT DOMAIN 5 169 Thioredoxin.
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 MOD_RES 63 63 N6-acetyllysine.
FT MOD_RES 89 89 Phosphotyrosine.
FT MOD_RES 209 209 N6-acetyllysine.
FT DISULFID 47 47 Interchain; in linked form (By
FT similarity).
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
FT STRAND 21 24
FT HELIX 25 29
FT STRAND 32 40
FT HELIX 45 62
FT TURN 63 65
FT STRAND 66 74
FT HELIX 76 89
FT STRAND 102 104
FT HELIX 109 113
FT STRAND 124 126
FT STRAND 133 137
FT STRAND 141 148
FT HELIX 157 173
FT STRAND 175 177
FT STRAND 187 189
FT HELIX 195 201
FT STRAND 219 221
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
//
MIM
602316
*RECORD*
*FIELD* NO
602316
*FIELD* TI
*602316 PEROXIREDOXIN 6; PRDX6
;;PHOSPHOLIPASE A2, LYSOSOMAL
*FIELD* TX
DESCRIPTION
read more
Phospholipase A2 (PLA2) represents a diverse family of enzymes that
hydrolyze the fatty acyl or alkyl bonds of membrane phospholipids. The
PLA2 family has been divided into several groups of related enzymes,
including secreted and cytosolic forms; see 600522.
CLONING
Kim et al. (1997) isolated a calcium-independent lysosomal PLA2 from a
human myeloblast cell line. The predicted 224-amino acid protein
contained the PLA2 catalytic motif, but no other significant homology to
known phospholipases. Expressed protein had significant PLA2 activity on
several substrates.
*FIELD* RF
1. 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 Ca(2+)-independent phospholipase A2 and properties of the expressed
protein. J. Biol. Chem. 272: 2542-2550, 1997. Note: Erratum: J.
Biol. Chem. 272: 10981 only, 1997.
*FIELD* CD
Jennifer P. Macke: 2/3/1998
*FIELD* ED
terry: 03/28/2013
carol: 7/17/2009
carol: 2/10/1998
*RECORD*
*FIELD* NO
602316
*FIELD* TI
*602316 PEROXIREDOXIN 6; PRDX6
;;PHOSPHOLIPASE A2, LYSOSOMAL
*FIELD* TX
DESCRIPTION
read more
Phospholipase A2 (PLA2) represents a diverse family of enzymes that
hydrolyze the fatty acyl or alkyl bonds of membrane phospholipids. The
PLA2 family has been divided into several groups of related enzymes,
including secreted and cytosolic forms; see 600522.
CLONING
Kim et al. (1997) isolated a calcium-independent lysosomal PLA2 from a
human myeloblast cell line. The predicted 224-amino acid protein
contained the PLA2 catalytic motif, but no other significant homology to
known phospholipases. Expressed protein had significant PLA2 activity on
several substrates.
*FIELD* RF
1. 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 Ca(2+)-independent phospholipase A2 and properties of the expressed
protein. J. Biol. Chem. 272: 2542-2550, 1997. Note: Erratum: J.
Biol. Chem. 272: 10981 only, 1997.
*FIELD* CD
Jennifer P. Macke: 2/3/1998
*FIELD* ED
terry: 03/28/2013
carol: 7/17/2009
carol: 2/10/1998