Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O08709 (PRDX6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxiredoxin-6

EC=1.11.1.15
Alternative name(s):
1-Cys peroxiredoxin
Short name=1-Cys PRX
Acidic calcium-independent phospholipase A2
Short name=aiPLA2
EC=3.1.1.-
Antioxidant protein 2
Non-selenium glutathione peroxidase
Short name=NSGPx
EC=1.11.1.9
Gene names
Name:Prdx6
Synonyms:Aop2, Ltw4, Prdx5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Subunit structure

Homodimer. Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration. Interacts with APEX1 and STH By similarity. May interact with FAM168B By similarity. May interact with HTR2A. Ref.7

Subcellular location

Cytoplasm By similarity. Lysosome By similarity. Cytoplasmic vesicle 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. Unlike 2-Cys peroxiredoxins, PRDX6 conserves only this peroxidatic cysteine. To regenerate and activate the enzyme, the oxidized form is directly reduced to cysteine by glutathione and not 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 residue2091N6-acetyllysine; alternate By similarity
Modified residue2091N6-succinyllysine; alternate Ref.9
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_031479.1. NM_007453.3.
XP_006544594.1. XM_006544531.1.
UniGeneMm.186185.

3D structure databases

ProteinModelPortalO08709.
SMRO08709. Positions 5-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198118. 1 interaction.
IntActO08709. 7 interactions.
MINTMINT-1869428.

PTM databases

PhosphoSiteO08709.

2D gel databases

COMPLUYEAST-2DPAGEO08709.
REPRODUCTION-2DPAGEO08709.
SWISS-2DPAGEO08709.
UCD-2DPAGEO08709.

Proteomic databases

PaxDbO08709.
PRIDEO08709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102642619.
11758.
KEGGmmu:11758.

Organism-specific databases

CTD9588.
MGIMGI:894320. Prdx6.

Phylogenomic databases

eggNOGCOG0450.
HOVERGENHBG105234.
InParanoidO08709.
KOK11188.

Enzyme and pathway databases

BRENDA1.11.1.15. 3474.

Gene expression databases

CleanExMM_PRDX5.
MM_PRDX6.
GenevestigatorO08709.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRDX6. mouse.
NextBio279511.
PROO08709.
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: April 16, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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