P35704 (PRDX2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-2
EC=1.11.1.15

Alternative name(s):
Thiol-specific antioxidant protein
Short name=TSA
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1

Gene names

Name:	Prdx2
Synonyms:	Tdpx1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

Protein attributes

Sequence length	198 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. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN By similarity.
Subcellular location	Cytoplasm.
Miscellaneous	The active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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. Inactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized By similarity.
Sequence similarities	Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell proliferation Inferred from electronic annotation. Source: Compara activation of MAPK activity Inferred from electronic annotation. Source: Compara homeostasis of number of cells Inferred from electronic annotation. Source: Compara hydrogen peroxide catabolic process Inferred from electronic annotation. Source: Compara negative regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara negative regulation of T cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of lipopolysaccharide-mediated signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 17663478. Source: RGD negative regulation of reactive oxygen species metabolic process Inferred from electronic annotation. Source: Compara positive regulation of blood coagulation Inferred from electronic annotation. Source: Compara regulation of hydrogen peroxide metabolic process Inferred from electronic annotation. Source: Compara removal of superoxide radicals Inferred from electronic annotation. Source: Compara respiratory burst involved in inflammatory response Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from mutant phenotype PubMed 17663478. Source: RGD thymus development Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay PubMed 11350800. Source: RGD mitochondrion Inferred from electronic annotation. Source: Compara
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 198	197	Peroxiredoxin-2		PRO_0000135083
Regions
	Domain	6 – 164	159	Thioredoxin
Sites
	Active site	51	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Disulfide bond	51		Interchain (with C-172); in linked form By similarity
	Disulfide bond	172		Interchain (with C-51); in linked form By similarity
Experimental info
	Sequence conflict	17	1	G → A in AAH58481. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P35704 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FC6AD9B0E9C4447B	FASTA	198	21,784
	10 20 30 40 50 60 MASGNAHIGK PAPDFTGTAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD 70 80 90 100 110 120 HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN 130 140 150 160 170 180 DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS 190 DTIKPNVDDS KEYFSKHN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes." Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G. Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary.
[3]	Lubec G., Afjehi-Sadat L., Diao W., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 93-135 AND 140-157, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U06099 mRNA. Translation: AAA19959.1. BC058481 mRNA. Translation: AAH58481.1.
IPI	IPI00201561.
PIR	A57716.
RefSeq	NP_058865.1. NM_017169.1.
UniGene	Rn.2511.
3D structure databases
ProteinModelPortal	P35704.
SMR	P35704. Positions 3-198.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35704. 1 interaction.
STRING	10116.ENSRNOP00000004799.
Protein family/group databases
PeroxiBase	4477. Rno2CysPrx02.
PTM databases
PhosphoSite	P35704.
2D gel databases
World-2DPAGE	0004:P35704.
Proteomic databases
PaxDb	P35704.
PRIDE	P35704.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000004799; ENSRNOP00000004799; ENSRNOG00000003520.
GeneID	29338.
KEGG	rno:29338.
Organism-specific databases
CTD	7001.
RGD	3838. Prdx2.
Phylogenomic databases
eggNOG	COG0450.
GeneTree	ENSGT00390000004653.
HOGENOM	HOG000022343.
HOVERGEN	HBG000286.
InParanoid	P35704.
KO	K03386.
OrthoDB	EOG4V6ZHJ.
Gene expression databases
Genevestigator	P35704.
GermOnline	ENSRNOG00000003520. Rattus norvegicus.
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
NextBio	608824.

Entry information

Entry name

PRDX2_RAT

Accession

Primary (citable) accession number: P35704
Secondary accession number(s): Q6PDV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program