O35244 (PRDX6_RAT) 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
Thiol-specific antioxidant protein

Gene names

Name:	Prdx6
Synonyms:	Aipla2, Aop2, Tsa

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. 2 glutathione + H2O2 = glutathione disulfide + 2 H2O.
Subunit structure	Homotetramer. Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration. May interact with HTR2A. Interacts with APEX1 and STH By similarity.
Subcellular location	Cytoplasm. Lysosome. Cytoplasmic vesicle By similarity. Note: Also found in lung secretory organelles.
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. 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 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	hydrogen peroxide catabolic process Inferred from direct assay. Source: RGD
Cellular component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glutathione peroxidase activity Inferred from direct assay. Source: RGD peroxiredoxin activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 224	223	Peroxiredoxin-6		PRO_0000135104
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 By similarity
	Modified residue	209	1	N6-acetyllysine By similarity
	Disulfide bond	47		Interchain; in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	O35244 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EE41D9079A708FD9	FASTA	224	24,819
	10 20 30 40 50 60 MPGGLLLGDE APNFEANTTI GHIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE 70 80 90 100 110 120 FAKRNVKLIA LSIDSVEDHF AWSKDINAYN GAAPTEKLPF PIIDDKDRDL AILLGMLDPA 130 140 150 160 170 180 EKDEKGMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVVDSLQLT ASNPVATPVD 190 200 210 220 WKKGESVMVL PTLPEEEAKQ LFPKGVFTKE LPSGKKYLRY TPQP

References

[1]	Kim T.-S., Feinstein S.I., Dodia C., Hennigan B.B., Fisher A.B. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Lung.
[2]	Andreeva S. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Olfactory epithelium.
[3]	Lubec G., Afjehi-Sadat L., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-41; 57-84; 98-118; 133-142; 156-162 AND 183-199, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.
[4]	"Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein." Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B. J. Biol. Chem. 272:2542-2550(1997) [PubMed: 8999971] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-42 AND 146-163.
[5]	Erratum Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B. J. Biol. Chem. 272:10981-10981(1997)
[6]	"Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST." Manevich Y., Feinstein S.I., Fisher A.B. Proc. Natl. Acad. Sci. U.S.A. 101:3780-3785(2004) [PubMed: 15004285] [Abstract] Cited for: ACTIVATION BY GLUTATHIONE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF014009 mRNA. Translation: AAB66341.1. Y17295 mRNA. Translation: CAA76732.1.
IPI	IPI00231260.
RefSeq	NP_446028.1. NM_053576.2.
UniGene	Rn.42.
3D structure databases
ProteinModelPortal	O35244.
SMR	O35244. Positions 5-224.
ModBase	Search...
Protein-protein interaction databases
IntAct	O35244. 1 interaction.
STRING	O35244.
Protein family/group databases
PeroxiBase	4427. Rno1CysPrx.
PTM databases
PhosphoSite	O35244.
2D gel databases
World-2DPAGE	0004:O35244.
Proteomic databases
PRIDE	O35244.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000034583; ENSRNOP00000030323; ENSRNOG00000002896.
GeneID	94167.
KEGG	rno:94167.
UCSC	NM_053576. rat.
Organism-specific databases
CTD	9588.
RGD	71005. Prdx6.
Phylogenomic databases
eggNOG	roNOG13330.
GeneTree	ENSGT00550000074794.
HOVERGEN	HBG105234.
InParanoid	O35244.
OMA	NYPILAD.
OrthoDB	EOG4M399H.
PhylomeDB	O35244.
Enzyme and pathway databases
BRENDA	1.11.1.15. 5301.
Gene expression databases
ArrayExpress	O35244.
Genevestigator	O35244.
GermOnline	ENSRNOG00000002896. Rattus norvegicus.
Family and domain databases
InterPro	IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR019479. Peroxiredoxin_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K11188.
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
NextBio	617808.

Entry information

Entry name

PRDX6_RAT

Accession

Primary (citable) accession number: O35244

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program