O08709 (PRDX6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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
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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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. 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.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Cytoplasm Cytoplasmic vesicle Lysosome
Domain	Redox-active center
Molecular function	Antioxidant Hydrolase Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	bleb assembly Inferred from mutant phenotype PubMed 17135244. Source: MGI lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to reactive oxygen species Inferred from mutant phenotype PubMed 12732627. Source: MGI
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 12732627. Source: MGI lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI
Molecular_function	glutathione peroxidase activity Inferred from electronic annotation. Source: EC hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from mutant phenotype PubMed 12732627. Source: MGI 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 [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] [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, 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, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, MASS SPECTROMETRY. 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 , AF093854, AF093855, AF093856 Genomic DNA. Translation: AAD03716.1. AK030413 mRNA. Translation: BAC26952.1. BC013489 mRNA. Translation: AAH13489.1.
IPI	IPI00555059.
RefSeq	NP_031479.1. NM_007453.3.
UniGene	Mm.186185.
3D structure databases
ProteinModelPortal	O08709.
SMR	O08709. Positions 5-224.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08709. 4 interactions.
PTM databases
PhosphoSite	O08709.
2D gel databases
COMPLUYEAST-2DPAGE	O08709.
REPRODUCTION-2DPAGE	O08709.
SWISS-2DPAGE	O08709.
UCD-2DPAGE	O08709.
Proteomic databases
PaxDb	O08709.
PRIDE	O08709.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	11758.
KEGG	mmu:11758. mmu:677654.
Organism-specific databases
CTD	9588.
MGI	MGI:894320. Prdx6.
Phylogenomic databases
eggNOG	COG0450.
HOVERGEN	HBG105234.
InParanoid	O08709.
KO	K11188.
OrthoDB	EOG4M399H.
Enzyme and pathway databases
BRENDA	1.11.1.15. 3474.
Gene expression databases
CleanEx	MM_PRDX5. MM_PRDX6.
Genevestigator	O08709.
GermOnline	ENSMUSG00000026701. Mus musculus.
Family and domain databases
Gene3D	3.40.30.10. 1 hit.
InterPro	IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PIRSF	PIRSF000239. AHPC. 1 hit.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PRDX6. mouse.
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:	May 1, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program