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Protein

Peroxiredoxin-6

Gene

Prdx6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321For phospholipase activityBy similarity
Active sitei47 – 471Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  1. glutathione peroxidase activity Source: UniProtKB-EC
  2. peroxidase activity Source: MGI
  3. peroxiredoxin activity Source: UniProtKB-EC
  4. phospholipase A2 activity Source: MGI

GO - Biological processi

  1. bleb assembly Source: MGI
  2. phospholipid catabolic process Source: MGI
  3. response to oxidative stress Source: MGI
  4. response to reactive oxygen species Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Hydrolase, Oxidoreductase, Peroxidase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi1.11.1.15. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-6 (EC:1.11.1.15)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
Acidic calcium-independent phospholipase A2 (EC:3.1.1.-)
Short name:
aiPLA2
Antioxidant protein 2
Non-selenium glutathione peroxidase (EC:1.11.1.9)
Short name:
NSGPx
Gene namesi
Name:Prdx6
Synonyms:Aop2, Ltw4, Prdx5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:894320. Prdx6.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  3. cytosol Source: MGI
  4. extracellular space Source: MGI
  5. extracellular vesicular exosome Source: MGI
  6. lysosome Source: UniProtKB-SubCell
  7. membrane Source: MGI
  8. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 224223Peroxiredoxin-6PRO_0000135103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphothreonineBy similarity
Disulfide bondi47 – 47Interchain; in linked formBy similarity
Modified residuei63 – 631N6-acetyllysineBy similarity
Modified residuei89 – 891Phosphotyrosine1 Publication
Modified residuei209 – 2091N6-acetyllysine; alternateBy similarity
Modified residuei209 – 2091N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiO08709.
PaxDbiO08709.
PRIDEiO08709.

2D gel databases

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

PTM databases

PhosphoSiteiO08709.

Expressioni

Tissue specificityi

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

Gene expression databases

CleanExiMM_PRDX5.
MM_PRDX6.
GenevestigatoriO08709.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Gstp1P191572EBI-444895,EBI-2309446
Ncf2O701453EBI-444895,EBI-9550667

Protein-protein interaction databases

BioGridi198118. 1 interaction.
IntActiO08709. 9 interactions.
MINTiMINT-1869428.

Structurei

3D structure databases

ProteinModelPortaliO08709.
SMRiO08709. Positions 5-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 169165ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family. Rehydrin subfamily.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
HOVERGENiHBG105234.
InParanoidiO08709.
KOiK11188.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08709-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGGLLLGDE APNFEANTTI GRIRFHDFLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN GETPTEKLPF
110 120 130 140 150
PIIDDKGRDL AILLGMLDPV EKDDNNMPVT ARVVFIFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVVDSLQLT GTKPVATPVD WKKGESVMVV PTLSEEEAKQ
210 220
CFPKGVFTKE LPSGKKYLRY TPQP
Length:224
Mass (Da):24,871
Last modified:January 23, 2007 - v3
Checksum:iAECDEDD332858B8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541G → S in AAC67553 (PubMed:10395907).Curated
Sequence conflicti181 – 1811W → R in AAD03716 (PubMed:10395907).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241D → A in strain: C57BL/6, C57BL/6J and FVB/N.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004670 mRNA. Translation: AAC53277.1.
Y12883 mRNA. Translation: CAA73383.1.
AF093852 mRNA. Translation: AAC63376.1.
AF093853 Genomic DNA. Translation: AAC67553.1.
AF093857
, AF093854, AF093855, AF093856 Genomic DNA. Translation: AAD03716.1.
AK030413 mRNA. Translation: BAC26952.1.
BC013489 mRNA. Translation: AAH13489.1.
CCDSiCCDS15415.1.
RefSeqiNP_031479.1. NM_007453.4.
XP_006544594.1. XM_006544531.1.
UniGeneiMm.186185.

Genome annotation databases

GeneIDi102642619.
11758.
KEGGimmu:102642619.
mmu:11758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004670 mRNA. Translation: AAC53277.1.
Y12883 mRNA. Translation: CAA73383.1.
AF093852 mRNA. Translation: AAC63376.1.
AF093853 Genomic DNA. Translation: AAC67553.1.
AF093857
, AF093854, AF093855, AF093856 Genomic DNA. Translation: AAD03716.1.
AK030413 mRNA. Translation: BAC26952.1.
BC013489 mRNA. Translation: AAH13489.1.
CCDSiCCDS15415.1.
RefSeqiNP_031479.1. NM_007453.4.
XP_006544594.1. XM_006544531.1.
UniGeneiMm.186185.

3D structure databases

ProteinModelPortaliO08709.
SMRiO08709. Positions 5-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198118. 1 interaction.
IntActiO08709. 9 interactions.
MINTiMINT-1869428.

PTM databases

PhosphoSiteiO08709.

2D gel databases

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

Proteomic databases

MaxQBiO08709.
PaxDbiO08709.
PRIDEiO08709.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102642619.
11758.
KEGGimmu:102642619.
mmu:11758.

Organism-specific databases

CTDi9588.
MGIiMGI:894320. Prdx6.

Phylogenomic databases

eggNOGiCOG0450.
HOVERGENiHBG105234.
InParanoidiO08709.
KOiK11188.

Enzyme and pathway databases

BRENDAi1.11.1.15. 3474.

Miscellaneous databases

ChiTaRSiPrdx6. mouse.
NextBioi279511.
PROiO08709.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PRDX5.
MM_PRDX6.
GenevestigatoriO08709.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPRDX6_MOUSE
AccessioniPrimary (citable) accession number: O08709
Secondary accession number(s): Q91WT2, Q9QWP4, Q9QWW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.