[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. TISSUE=Kidney; DOI=10.1016/S0014-5793(98)01736-0; PubMed=10025941 [NCBI, ExPASy, EBI, Israel, Japan] Matsumoto A., Okado A., Fujii T., Fujii J., Egashira M., Niikawa N., Taniguchi N.; "Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member."; FEBS Lett. 443:246-250(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 171-208; 172-197 AND 209-239, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.

Comments

FUNCTION: Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (By similarity).
CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H₂O + ROH.
SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity). Binds MAP3K13 (By similarity).
SUBCELLULAR LOCATION: Mitochondrion (By similarity).
TISSUE SPECIFICITY: Ubiquitous.
MISCELLANEOUS: The active site is the redox-active Cys-109 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-230-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).
MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-109 (to Cys-SO(3)H) upon oxidative stress (By similarity).
SIMILARITY: Belongs to the ahpC/TSA family.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF106944; AAD17992.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC060567; AAH60567.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_071985.1; -.

UniGene

Rn.2011

3D structure databases

HSSP

P32119; 1QMV. [HSSP ENTRY / PDB]

SMR

Q9Z0V6; 64-224.

ModBase

Q9Z0V6.

Protein family/group databases

PeroxiBase

4507; Rno2CysPrx03.

Organism-specific databases

RGD

620040; Prdx3.

Gene expression databases

ArrayExpress

Q9Z0V6; -.

GermOnline

ENSRNOG00000010958; Rattus norvegicus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0051920;	Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.

PROSITE

PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000010958; Rattus norvegicus. [Contig view]

GeneID

64371; -.

KEGG

rno:64371; -.

Phylogenomic databases

HOVERGEN

Q9Z0V6; -.

Other

NextBio

613116; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antioxidant; Direct protein sequencing; Mitochondrion; Oxidoreductase; Peroxidase; Redox-active center; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 62`	`62`	`Mitochondrion (By similarity).`
`CHAIN`	`63 257`	`195`	`Thioredoxin-dependent peroxide reductase, mitochondrial (By similarity).`	`PRO_0000256859`
`DOMAIN`	`64 222`	`159`	`Thioredoxin.`
`ACT_SITE`	`109 109`		`Cysteine sulfenic acid (-SOH) intermediate (By similarity).`
`DISULFID`	`109 109`		`Interchain (with C-229); in linked form (By similarity).`
`DISULFID`	`230 230`		`Interchain (with C-108); in linked form (By similarity).`
`CONFLICT`	`207 216`		`Missing (in Ref. 2; AAH60567).`
`CONFLICT`	`232 232`		`A -> P (in Ref. 1; AAD17992).`

Sequence information

Length: 257 AA [This is the length of the unprocessed precursor]

Molecular weight: 28295 Da [This is the MW of the unprocessed precursor]

CRC64: 752198F5918206AE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAAGRLLW SSVARPASTI FRSISASTVL RPVASRRTCL TDMLWSACPQ AKFAFSTSSS 

        70         80         90        100        110        120 
FHTPAVTQHA PHFKGTAVVN GEFKELSLDD FKGKYLVLFF YPLDFTFVCP TEIVAFSDKA 

       130        140        150        160        170        180 
NEFHDVNCEV VAVSVDSHFS HLAWINTPRK NGGLGHMNIT LLSDLTKQIS RDYGVLLESA 

       190        200        210        220        230        240 
GIALRGLFII DPNGVIKHLS VNDLPVGRSV EEPLRLVKAF QFVETHGEVC PANWTPESPT 

       250 
IKPSPTASKE YFEKVHQ

Q9Z0V6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools