Reviewed, UniProtKB/Swiss-Prot O08709 (PRDX6_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cytoplasm Lysosome
Domain	Redox-active center
Molecular function	Antioxidant Hydrolase Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	bleb formation Inferred from mutant phenotype. Source: MGI cell redox homeostasis Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to reactive oxygen species Inferred from mutant phenotype. Source: MGI
Cellular component	cytosol Inferred from direct assay. Source: MGI lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: MGI
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW peroxiredoxin activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1 Ref.6
	Chain	2 – 224	223	Peroxiredoxin-6		PRO_0000135103
Regions
	Domain	5 – 169	165	Thioredoxin
Sites
	Active site	32	1	For phospholipase activity By similarity
	Active site	47	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Modified residue	44	1	Phosphothreonine By similarity
	Modified residue	63	1	N6-acetyllysine By similarity
	Modified residue	89	1	Phosphotyrosine Ref.8
	Modified residue	93	1	Phosphothreonine Ref.9
	Modified residue	209	1	N6-acetyllysine By similarity
	Disulfide bond	47		Interchain; in linked form By similarity
Natural variations
	Natural variant	124	1	D → A in strain: C57BL/6, C57BL/6J and FVB/N.
Experimental info
	Sequence conflict	154	1	G → S in AAC67553. Ref.3
	Sequence conflict	181	1	W → R in AAD03716. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O08709-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AECDEDD332858B8F	FASTA	224	24,871
	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

References

	« Hide 'large scale' referencesShow '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. , 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
EMBLGenBankDDBJ	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.
IPI	IPI00555059.
RefSeq	NP_031479.1.
UniGene	Mm.186185
3D structure databases
HSSP	HSSP built from PDB template 1PRX based on UniProtKB P30041.
SMR	O08709. Positions 5-224.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08709. 2 interactions.
STRING	O08709.
PTM databases
PhosphoSite	O08709.
2-D gel databases
SWISS-2DPAGE	O08709.
REPRODUCTION-2DPAGE	O08709.
Proteomic databases
PRIDE	O08709.
Genome annotation databases
Ensembl	ENSMUST00000071718; ENSMUSP00000071636; ENSMUSG00000026701; Mus musculus. [Genome view]
GeneID	11758.
KEGG	mmu:11758.
Organism-specific databases
CTD	11758.
MGI	MGI:894320. Prdx6.
Phylogenomic databases
HOVERGEN	O08709.
Enzyme and pathway databases
BRENDA	1.11.1.15. 244. 1.11.1.7. 244.
Gene expression databases
ArrayExpress	O08709.
Bgee	O08709.
CleanEx	MM_PRDX5. MM_PRDX6.
Genevestigator	O08709.
GermOnline	ENSMUSG00000026701. Mus musculus.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	279511.
SOURCE	Search...

Entry information

Entry name

PRDX6_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)