Reviewed, UniProtKB/Swiss-Prot P35704 (PRDX2_RAT)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-2
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin peroxidase 1
    Thioredoxin-dependent peroxide reductase 1
    Thiol-specific antioxidant protein
      Short name=TSA

Gene names

Name:	Prdx2
Synonyms:	Tdpx1

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	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 H(2)O(2).
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H(2)O + 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-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H 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
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	cytoplasm 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
	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)
	P35704-1 [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: 8041738] [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: 15489334] [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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U06099 mRNA. Translation: AAA19959.1. BC058481 mRNA. Translation: AAH58481.1.
PIR	A57716.
RefSeq	NP_058865.1.
UniGene	Rn.2511
3D structure databases
HSSP	HSSP built from PDB template 1QMV based on UniProtKB P32119.
SMR	P35704. Positions 2-197, 3-198.
ModBase	Search...
Protein family/group databases
PeroxiBase	4477. Rno2CysPrx02.
PTM databases
PhosphoSite	P35704.
Genome annotation databases
Ensembl	ENSRNOG00000003520. Rattus norvegicus. [Contig view]
GeneID	29338.
KEGG	rno:29338.
Organism-specific databases
RGD	3838. Prdx2.
Phylogenomic databases
HOVERGEN	P35704.
Gene expression databases
ArrayExpress	P35704.
GermOnline	ENSRNOG00000003520. 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	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:	November 25, 2008
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)