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Reviewed, UniProtKB/Swiss-Prot O08709 (PRDX6_MOUSE)

Last modified November 3, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxiredoxin-6
    EC=1.11.1.15
Alternative name(s):
    Antioxidant protein 2
    1-Cys peroxiredoxin
      Short name=1-Cys PRX
    Acidic calcium-independent phospholipase A2
      Short name=aiPLA2
    EC=3.1.1.-
    Non-selenium glutathione peroxidase
      Short name=NSGPx
    EC=1.11.1.7
Gene names
Name: Prdx6
Synonyms: Aop2, Ltw4, Prdx5
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury By similarity.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Donor + H2O2 = oxidized donor + 2 H2O.

Subunit structure

Homodimer. Interacts with STH By similarity. May interact with HTR2A.

Subcellular location

Cytoplasm By similarity. Lysosome By similarity. Note: Also found in lung secretory organelles By similarity.

Tissue specificity

Highly expressed in heart, kidney and liver. Moderate expression in brain and stomach. Very low levels in intestine.

Miscellaneous

The active site is the redox-active Cys-47 oxidized to Cys-SOH. Cys-SOH may rapidly react with a Cys-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin By similarity.

Irreversibly inactivated by overoxidation of Cys-47 (to Cys-SO3H) upon oxidative stress By similarity.

Sequence similarities

Belongs to the ahpC/TSA family. Rehydrin subfamily.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.6
Chain2 – 224223Peroxiredoxin-6
PRO_0000135103

Regions

Domain5 – 169165Thioredoxin

Sites

Active site321For phospholipase activity By similarity
Active site471Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue441Phosphothreonine By similarity
Modified residue631N6-acetyllysine By similarity
Modified residue891Phosphotyrosine Ref.8
Modified residue931Phosphothreonine Ref.9
Modified residue2091N6-acetyllysine By similarity
Disulfide bond47Interchain; in linked form By similarity

Natural variations

Natural variant1241D → A in strain: C57BL/6, C57BL/6J and FVB/N.

Experimental info

Sequence conflict1541G → S in AAC67553. Ref.3
Sequence conflict1811W → R in AAD03716. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O08709-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AECDEDD332858B8F

FASTA22424,871
        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 

« Hide

References

« Hide 'large scale' references
[1]"LTW4 protein on mouse chromosome 1 is a member of a family of antioxidant proteins."
Iakoubova O.A., Pacella L.A., Her H., Beier D.R.
Genomics 42:474-478(1997) [PubMed: 9205120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-26.
Strain: C3H/FEJ, C57BL/6J and DBA/2J.
Tissue: Kidney and Liver.
[2]"A novel type of glutathione peroxidase: expression and regulation during wound repair."
Munz B., Frank S., Huebner G., Olsen E., Werner S.
Biochem. J. 326:579-585(1997) [PubMed: 9291135] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Skin.
[3]"Characterization of the murine gene encoding 1-Cys peroxiredoxin and identification of highly homologous genes."
Lee T.-H., Yu S.-L., Kim S.-U., Kim Y.-M., Choi I., Kang S.W., Rhee S.G., Yu D.-Y.
Gene 234:337-344(1999) [PubMed: 10395907] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/SvJ and C57BL/6.
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pituitary.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
[6]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-22; 25-53; 98-106; 109-122; 145-155 AND 163-182, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[7]"The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins."
Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., Bockaert J., Marin P.
J. Biol. Chem. 279:20257-20266(2004) [PubMed: 14988405] [Abstract]
Cited for: INTERACTION WITH HTR2A.
[8]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, MASS SPECTROMETRY.
Tissue: Brain.
[9]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF004670 mRNA. Translation: AAC53277.1.
Y12883 mRNA. Translation: CAA73383.1.
AF093852 mRNA. Translation: AAC63376.1.
AF093853 Genomic DNA. Translation: AAC67553.1.
AF093857 expand/collapse EMBL AC list , AF093854, AF093855, AF093856 Genomic DNA. Translation: AAD03716.1.
AK030413 mRNA. Translation: BAC26952.1.
BC013489 mRNA. Translation: AAH13489.1.
IPIIPI00555059.
RefSeqNP_031479.1.
UniGeneMm.186185

3D structure databases

HSSPHSSP built from PDB template 1PRX based on UniProtKB P30041.
SMRO08709. Positions 5-224.
ModBaseSearch...

Protein-protein interaction databases

IntActO08709. 2 interactions.
STRINGO08709.

PTM databases

PhosphoSiteO08709.

2-D gel databases

SWISS-2DPAGEO08709.
REPRODUCTION-2DPAGEO08709.

Proteomic databases

PRIDEO08709.

Genome annotation databases

EnsemblENSMUST00000071718; ENSMUSP00000071636; ENSMUSG00000026701; Mus musculus. [Genome view]
GeneID11758.
KEGGmmu:11758.

Organism-specific databases

CTD11758.
MGIMGI:894320. Prdx6.

Phylogenomic databases

HOVERGENO08709.

Enzyme and pathway databases

BRENDA1.11.1.15. 244.
1.11.1.7. 244.

Gene expression databases

ArrayExpressO08709.
BgeeO08709.
CleanExMM_PRDX5.
MM_PRDX6.
GenevestigatorO08709.
GermOnlineENSMUSG00000026701. Mus musculus.

Family and domain databases

InterProIPR000866. Alkyl_hydroperoxide_Rdtase.
IPR019479. Peroxiredoxin_C.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio279511.
SOURCESearch...

Entry information

Entry namePRDX6_MOUSE
AccessionPrimary (citable) accession number: O08709
Secondary accession number(s): Q91WT2, Q9QWP4, Q9QWW0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents