Reviewed, UniProtKB/Swiss-Prot Q9BGI3 (PRDX2_BOVIN)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin-2
    EC=1.11.1.15

Gene names

Name:

PRDX2

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-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-52 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	Disulfide bond
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-SubCell
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
	Chain	1 – 199	199	Peroxiredoxin-2		PRO_0000135079
Regions
	Domain	7 – 165	159	Thioredoxin
Sites
	Active site	52	1	Cysteine sulfenic acid (-SOH) intermediate By similarity
Amino acid modifications
	Disulfide bond	52		Interchain (with C-173); in linked form By similarity
	Disulfide bond	173		Interchain (with C-52); in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9BGI3-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 5F256CE54090E2DE	FASTA	199	21,946
	10 20 30 40 50 60 MACVCKAHVG KPAPEFQATA VVDGAFKEVK LSDYKGKYVV LFFYPLDFTF VCPTEIVAFS 70 80 90 100 110 120 DRAAEFHKLN CEVLGVSVDS QFTHLAWINT PRKEGGLGPL NIPLLADVTR KLSSDYGVLK 130 140 150 160 170 180 EDEGIAYRGL FVIDGKGVLR QVTINDLPVG RSVDEALRLV QAFQYTDEHG EVCPAGWTPG 190 SDTIKPNVDD SKEYFSKHN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of 4 new bovine peroxiredoxins, and screening of the complete peroxiredoxin family in different bovine tissues." Leyens G., Donnay I., Knoops B. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF305562 mRNA. Translation: AAG53659.1. BC102351 mRNA. Translation: AAI02352.1.
IPI	IPI00713112.
RefSeq	NP_777188.1.
UniGene	Bt.2689
3D structure databases
HSSP	HSSP built from PDB template 1QMV based on UniProtKB P32119.
SMR	Q9BGI3. Positions 7-199.
ModBase	Search...
Protein family/group databases
PeroxiBase	4473. Bt2CysPrx02.
Proteomic databases
PRIDE	Q9BGI3.
Genome annotation databases
Ensembl	ENSBTAG00000012062. Bos taurus. [Contig view]
GeneID	286793.
KEGG	bta:286793.
Phylogenomic databases
HOVERGEN	Q9BGI3.
OMA	Q9BGI3. EISAAYN.
Enzyme and pathway databases
BRENDA	1.11.1.15. 251.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_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]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRDX2_BOVIN

Accession

Primary (citable) accession number: Q9BGI3
Secondary accession number(s): Q3T0L0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)