Reviewed, UniProtKB/Swiss-Prot Q9Z0V6 (PRDX3_RAT)

Names and origin

Protein names

Recommended name:
    Thioredoxin-dependent peroxide reductase, mitochondrial
    EC=1.11.1.15
Alternative name(s):
    Peroxiredoxin-3
      Short name=PRX-3
    PRx III

Gene names

Name:

Prdx3

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	257 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. 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' + H(2)O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation By similarity. Binds MAP3K13 By similarity.
Subcellular location	MitochondrionBy 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. Irreversibly inactivated by overoxidation of Cys-109 (to Cys-SO(3)H) upon oxidative stress By similarity.
Sequence similarities	Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Redox-active center Transit peptide
Molecular function	Antioxidant Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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
	Transit peptide	1 – 62	62	Mitochondrion By similarity
	Chain	63 – 257	195	Thioredoxin-dependent peroxide reductase, mitochondrial By similarity		PRO_0000256859
Regions
	Domain	64 – 222	159	Thioredoxin
Sites
	Active site	109	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Disulfide bond	109		Interchain (with C-229); in linked form By similarity
	Disulfide bond	230		Interchain (with C-108); in linked form By similarity
Experimental info
	Sequence conflict	207 – 216	10	Missing in AAH60567. Ref.2
	Sequence conflict	232	1	A → P in AAD17992. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Z0V6-1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 752198F5918206AE	FASTA	257	28,295
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member." Matsumoto A., Okado A., Fujii T., Fujii J., Egashira M., Niikawa N., Taniguchi N. FEBS Lett. 443:246-250(1999) [PubMed: 10025941] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Kidney.
[2]	"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].
[3]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 171-208; 172-197 AND 209-239, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF106944 mRNA. Translation: AAD17992.1. BC060567 mRNA. Translation: AAH60567.1.
RefSeq	NP_071985.1.
UniGene	Rn.2011
3D structure databases
HSSP	HSSP built from PDB template 1QMV based on UniProtKB P32119.
SMR	Q9Z0V6. Positions 64-224.
ModBase	Search...
Protein family/group databases
PeroxiBase	4507. Rno2CysPrx03.
Genome annotation databases
Ensembl	ENSRNOG00000010958. Rattus norvegicus. [Contig view]
GeneID	64371.
KEGG	rno:64371.
Organism-specific databases
RGD	620040. Prdx3.
Phylogenomic databases
HOVERGEN	Q9Z0V6.
Gene expression databases
ArrayExpress	Q9Z0V6.
GermOnline	ENSRNOG00000010958. Rattus norvegicus.
Family and domain databases
InterPro	IPR000866. AhpC-TSA. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00578. AhpC-TSA. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	613116.

Entry information

Entry name

PRDX3_RAT

Accession

Primary (citable) accession number: Q9Z0V6
Secondary accession number(s): Q6P9W3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	November 25, 2008
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)