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UniProtKB/Swiss-Prot entry O08709


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

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Entry information
Entry name PRDX6_MOUSE
Primary accession number O08709
Secondary accession numbers Q91WT2 Q9QWP4 Q9QWW0
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 81)
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
Gene name
Name: Prdx6
Synonyms: Aop2, Ltw4, Prdx5
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-26.
STRAIN=C3H/FEJ, C57BL/6J, and DBA/2J;
TISSUE=Kidney, and Liver;
DOI=10.1006/geno.1997.4762; PubMed=9205120 [NCBI, ExPASy, EBI, Israel, Japan]
Iakoubova O.A., Pacella L.A., Her H., Beier D.R.;
"LTW4 protein on mouse chromosome 1 is a member of a family of antioxidant proteins.";
Genomics 42:474-478(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Skin;
PubMed=9291135 [NCBI, ExPASy, EBI, Israel, Japan]
Munz B., Frank S., Huebner G., Olsen E., Werner S.;
"A novel type of glutathione peroxidase: expression and regulation during wound repair.";
Biochem. J. 326:579-585(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/SvJ, and C57BL/6;
TISSUE=Brain;
DOI=10.1016/S0378-1119(99)00190-0; PubMed=10395907 [NCBI, ExPASy, EBI, Israel, Japan]
Lee T.-H., Yu S.-L., Kim S.-U., Kim Y.-M., Choi I., Kang S.W., Rhee S.G., Yu D.-Y.;
"Characterization of the murine gene encoding 1-Cys peroxiredoxin and identification of highly homologous genes.";
Gene 234:337-344(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Pituitary;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Colon;
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).
[6]
PROTEIN SEQUENCE OF 2-22; 25-53 AND 109-122, AND MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 2-22; 98-106; 109-122; 145-155 AND 163-182, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
INTERACTION WITH HTR2A.
DOI=10.1074/jbc.M312106200; PubMed=14988405 [NCBI, ExPASy, EBI, Israel, Japan]
Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., Bockaert J., Marin P.;
"The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins.";
J. Biol. Chem. 279:20257-20266(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).
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
AF004670; AAC53277.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y12883; CAA73383.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF093852; AAC63376.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF093853; AAC67553.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF093857; AAD03716.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF093854; AAD03716.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF093855; AAD03716.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF093856; AAD03716.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK030413; BAC26952.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013489; AAH13489.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_031479.1; -.
UniGene Mm.186185
3D structure databases
HSSP P30041; 1PRX. [HSSP ENTRY / PDB]
SMR O08709; 5-224.
ModBase O08709.
PTM databases
PhosphoSite O08709; -.
2D gel databases
SWISS-2DPAGE O08709; -.
REPRODUCTION-2DPAGE O08709; -.
Organism-specific databases
MGI MGI:894320; Prdx6.
Gene expression databases
ArrayExpress O08709; -.
CleanEx MM_PRDX5; -.
MM_PRDX6; -.
GermOnline ENSMUSG00000026701; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from MGI).
GO:0004601; Molecular function: peroxidase activity (inferred from mutant phenotype from MGI).
GO:0032060; Biological process: bleb formation (inferred from mutant phenotype from MGI).
GO:0000302; Biological process: response to reactive oxygen species (inferred from mutant phenotype from MGI).
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 O08709.
Genome annotation databases
Ensembl ENSMUSG00000026701; Mus musculus. [Contig view]
GeneID 11758; -.
KEGG mmu:11758; -.
Phylogenomic databases
HOVERGEN O08709; -.
Other
SOURCE Prdx6; Mus musculus.
ProtoNet O08709.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Cytoplasm; 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_0000135103
DOMAIN   5   169  165     Thioredoxin. 
ACT_SITE   32    32        For phospholipase activity (By similarity). 
ACT_SITE   47    47        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
MOD_RES   89    89        Phosphotyrosine. 
MOD_RES   93    93        Phosphothreonine. 
DISULFID   47    47        Interchain; in linked form (By similarity). 
VARIANT   124   124  1     D -> A (in strain: C57BL/6, C57BL/6J and FVB/N). 
CONFLICT   154   154        G -> S (in Ref. 3; AAC67553). 
CONFLICT   181   181        W -> R (in Ref. 3; AAD03716). 
Sequence information
Length: 224 AA [This is the length of the unprocessed precursor] Molecular weight: 24871 Da [This is the MW of the unprocessed precursor] CRC64: AECDEDD332858B8F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPGGLLLGDE APNFEANTTI GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE 

        70         80         90        100        110        120 
FAKRNVKLIA LSIDSVEDHL AWSKDINAYN GETPTEKLPF PIIDDKGRDL AILLGMLDPV 

       130        140        150        160        170        180 
EKDDNNMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVVDSLQLT GTKPVATPVD 

       190        200        210        220 
WKKGESVMVV PTLSEEEAKQ CFPKGVFTKE LPSGKKYLRY TPQP 

O08709 in FASTA format

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