Q9Z0V6 (PRDX3_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin-dependent peroxide reductase, mitochondrial
EC=1.11.1.15

Alternative name(s):
PRx III
Peroxiredoxin-3
Short name=PRX-3

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' + H2O + ROH.
Subunit structure	Dodecameric ring assembled from homodimeric units; disulfide-linked, upon oxidation. The rings have an approximate diameter of 150 A and a central hole of 70 A. 3-5% of the rings are interlocked by pairs. Binds MAP3K13 By similarity. Interacts with NEK6 By similarity. Interacts with LRRK2 By similarity.
Subcellular location	Mitochondrion By similarity.
Tissue specificity	Ubiquitous. Ref.1
Post-translational modification	Phosphorylated by LRRK2; phosphorylation reduces perodixase activity By similarity.
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-SO3H) 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
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of neuron apoptosis Inferred from mutant phenotype. Source: RGD
Cellular component	mitochondrion Inferred from direct assay. Source: RGD
Molecular function	peroxidase 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
	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
	Modified residue	92	1	N6-acetyllysine By similarity
	Modified residue	147	1	Phosphothreonine By similarity
	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 [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF106944 mRNA. Translation: AAD17992.1. BC060567 mRNA. Translation: AAH60567.1.
IPI	IPI00208215.
RefSeq	NP_071985.1. NM_022540.1.
UniGene	Rn.2011.
3D structure databases
HSSP	HSSP built from PDB template 1ZYE based on UniProtKB P35705.
ProteinModelPortal	Q9Z0V6.
SMR	Q9Z0V6. Positions 64-254.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z0V6. 2 interactions.
MINT	MINT-4621394.
STRING	Q9Z0V6.
Protein family/group databases
PeroxiBase	4507. Rno2CysPrx03.
2D gel databases
World-2DPAGE	0004:Q9Z0V6.
Proteomic databases
PRIDE	Q9Z0V6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	64371.
KEGG	rno:64371.
UCSC	NM_022540. rat.
Organism-specific databases
CTD	10935.
RGD	620040. Prdx3.
Phylogenomic databases
eggNOG	roNOG07743.
GeneTree	ENSGT00390000004653.
HOVERGEN	HBG000286.
InParanoid	Q9Z0V6.
OrthoDB	EOG4S7JQS.
PhylomeDB	Q9Z0V6.
Gene expression databases
ArrayExpress	Q9Z0V6.
Genevestigator	Q9Z0V6.
GermOnline	ENSRNOG00000010958. 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	K03386.
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	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:	January 25, 2012
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program