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UniProtKB/Swiss-Prot entry P30041


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRDX6_HUMAN
Primary accession number P30041
Secondary accession numbers P32077 Q5TAH4 Q5ZEZ8
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 97)
Name and origin of the protein
Protein name Peroxiredoxin-6
Synonyms EC 1.11.1.15
Antioxidant protein 2
1-Cys peroxiredoxin
1-Cys PRX
Acidic calcium-independent phospholipase A2
aiPLA2
EC 3.1.1.-
Non-selenium glutathione peroxidase
NSGPx
EC 1.11.1.7
24 kDa protein
Liver 2D page spot 40
Red blood cells page spot 12
Gene name
Name: PRDX6
Synonyms: AOP2, KIAA0106
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.272.4.2542; PubMed=8999971 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/sj.onc.1200905; PubMed=9050990 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1093/dnares/2.1.37; PubMed=7788527 [NCBI, ExPASy, EBI, Israel, Japan]
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 [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PROTEIN SEQUENCE OF 2-22.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
PROTEIN SEQUENCE OF 2-22 AND 98-106, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[10]
PARTIAL PROTEIN SEQUENCE OF 2-15.
TISSUE=Liver;
DOI=10.1002/elps.11501301201; PubMed=1286669 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
PARTIAL PROTEIN SEQUENCE OF 2-13.
TISSUE=Erythrocyte;
PubMed=8313871 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-99.
Dominguez O., Lombardia L.;
"DNA probes built and sequenced for microrrays hybridisations.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[13]
CHARACTERIZATION, AND MUTAGENESIS.
DOI=10.1074/jbc.273.11.6303; PubMed=9497358 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
CHARACTERIZATION, AND MUTAGENESIS.
DOI=10.1074/jbc.M005073200; PubMed=10893423 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
OVEROXIDATION AT CYS-47.
DOI=10.1042/BJ20020525; PubMed=12059788 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
SUBCELLULAR LOCATION, AND INTERACTION WITH STH.
DOI=10.1074/jbc.M506116200; PubMed=16186110 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1038/nsb0598-400; PubMed=9587003 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D14662; BAA03496.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ230990; ABB02185.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139142; CAI20936.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC035857; AAH35857.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053550; AAH53550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ844621; CAH59743.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_004896.1; -.
UniGene Hs.573688
3D structure databases
PDB
1PRX; X-ray; 2.00 A; A/B=1-224.[ExPASy / RCSB / EBI]
PDBsum 1PRX; -.
ModBase P30041.
Protein family/group databases
PeroxiBase 4426; Hs1CysPrx.
PTM databases
PhosphoSite P30041; -.
2D gel databases
SWISS-2DPAGE P30041; -.
Cornea-2DPAGE P30041; -.
DOSAC-COBS-2DPAGE P30041; -.
OGP P30041; -.
REPRODUCTION-2DPAGE IPI00220301; -.
P30041; -.
Siena-2DPAGE P30041; -.
Organism-specific databases
H-InvDB HIX0001339; -.
HIX0028696; -.
HGNC HGNC:16753; PRDX6.
GenAtlas PRDX6.
HPA CAB008663; -.
HPA006983; -.
MIM 602316; gene. [NCBI / EBI]
PharmGKB PA134992760; -.
GeneCards P30041.
HUGE KIAA0106.
Gene expression databases
ArrayExpress P30041; -.
CleanEx HS_PRDX6; -.
GermOnline ENSG00000117592; Homo sapiens.
Ontologies
GO
GO:0031410; Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0005829; Cellular component: cytosol (non-traceable author statement from UniProtKB).
GO:0005764; Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0004623; Molecular function: phospholipase A2 activity (inferred from direct assay from UniProtKB).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009395; Biological process: phospholipid catabolic process (inferred from direct assay from UniProtKB).
GO:0006979; Biological process: response to oxidative stress (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P30041.
ProtoNet P30041.
Proteomic databases
PeptideAtlas P30041; -.
Genome annotation databases
Ensembl ENSG00000117592; Homo sapiens. [Contig view]
GeneID 9588; -.
KEGG hsa:9588; -.
Phylogenomic databases
HOGENOM P30041; -.
HOVERGEN P30041; -.
Other
LinkHub P30041; -.
NextBio 35979; -.
SOURCE PRDX6; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Antioxidant; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Hydrolase; Lipid degradation; Lysosome; Multifunctional enzyme; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   224  223     Peroxiredoxin-6. PRO_0000135102
DOMAIN   5   169  165     Thioredoxin. 
ACT_SITE   32    32        For phospholipase activity. 
ACT_SITE   47    47        Cysteine sulfenic acid (-SOH) intermediate. 
MOD_RES   44    44        Phosphothreonine. 
MOD_RES   89    89        Phosphotyrosine. 
DISULFID   47    47        Interchain; in linked form (By similarity). 
MUTAGEN   32    32        S->A: Loss of AIPLA2 activity, but no effect on NSGPX activity. 
MUTAGEN   47    47        C->S: Loss of NSGPX activity, but no effect on AIPLA2 activity. 
STRAND   15    18  4      
STRAND   21    24  4      
HELIX   25    29  5      
STRAND   32    40  9      
HELIX   45    62  18      
TURN   63    65  3      
STRAND   66    74  9      
HELIX   76    89  14      
STRAND   102   104  3      
HELIX   109   113  5      
STRAND   124   126  3      
STRAND   133   137  5      
STRAND   141   148  8      
HELIX   157   173  17      
STRAND   175   177  3      
STRAND   187   189  3      
HELIX   195   201  7      
STRAND   219   221  3      
Sequence information
Length: 224 AA [This is the length of the unprocessed precursor] Molecular weight: 25035 Da [This is the MW of the unprocessed precursor] CRC64: 017D955F0FEEDFBC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE 

        70         80         90        100        110        120 
FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF PIIDDRNREL AILLGMLDPA 

       130        140        150        160        170        180 
EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD 

       190        200        210        220 
WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP 

P30041 in FASTA format

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View entry in raw text format (no links)
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