Q8K3U7 (PRDX2_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-2
EC=1.11.1.15

Gene names

Name:

PRDX2

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

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 transcript 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 By similarity.
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 By similarity.
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
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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_0000256855
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

Sequences

	Sequence		Length	Mass (Da)
	Q8K3U7 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5A11BF0B70F27B4C	FASTA	198	21,813
	10 20 30 40 50 60 MASGNAHIGK PAPDFTATAV VDGAFKEVKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSN 70 80 90 100 110 120 HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRS LSENYGVLKT 130 140 150 160 170 180 DEGIAYRGLF IIDAKGILRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS 190 DTIKPNVDDS KEYFSKHN

References

[1]	"2D Gel analysis of the proteomic adaptation of a mammalian cell line to oxidative stress reveals changes in the expression of metabolically relevant enzymes." Keightley J.A., Shang L., Kinter M. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF532110 mRNA. Translation: AAM95673.1.
RefSeq	NP_001233709.1. NM_001246780.1.
3D structure databases
HSSP	HSSP built from PDB template 1QMV based on UniProtKB P32119.
ProteinModelPortal	Q8K3U7.
SMR	Q8K3U7. Positions 3-198.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100689349.
Phylogenomic databases
HOVERGEN	HBG000286.
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.
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...

Entry information

Entry name

PRDX2_CRIGR

Accession

Primary (citable) accession number: Q8K3U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 52 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program