Q2PFZ3 (PRDX2_MACFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-2
EC=1.11.1.15

Gene names

Name:	PRDX2
ORF Names:	QccE-19689

Organism

Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)

Taxonomic identifier

9541 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

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_0000256856
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)
	Q2PFZ3 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1AC781D908B32B46	FASTA	198	21,892
	10 20 30 40 50 60 MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN 70 80 90 100 110 120 RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT 130 140 150 160 170 180 DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS 190 DTIKPNVDDS KEYFSKHN

References

[1]	"Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA oligo-chips." Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S., Hashimoto K. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB220444 mRNA. Translation: BAE72977.1.
3D structure databases
HSSP	HSSP built from PDB template 1X0R based on UniProtKB Q9Y9L0.
ProteinModelPortal	Q2PFZ3.
SMR	Q2PFZ3. Positions 3-198.
ModBase	Search...
Protein family/group databases
PeroxiBase	4482. Mfa2CysPrx02.
Proteomic databases
PRIDE	Q2PFZ3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_MACFA

Accession

Primary (citable) accession number: Q2PFZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 23, 2007
Last modified:	October 19, 2011
This is version 41 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program