Q5RC63 (PRDX2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-2
EC=1.11.1.15

Gene names

Name:

PRDX2

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	177 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-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-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)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 177	176	Peroxiredoxin-2		PRO_0000256857
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-173); in linked form By similarity
	Disulfide bond	173		Interchain (with C-51); in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RC63 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6D95970252096370	FASTA	177	19,430
	10 20 30 40 50 60 MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN 70 80 90 100 110 120 RAEDFHKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT 130 140 150 160 170 DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE GPCFASP

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR858417 mRNA. Translation: CAH90647.1.
RefSeq	NP_001125349.1. NM_001131877.1.
UniGene	Pab.19238.
3D structure databases
HSSP	HSSP built from PDB template 1QMV based on UniProtKB P32119.
ProteinModelPortal	Q5RC63.
SMR	Q5RC63. Positions 3-170.
ModBase	Search...
Protein family/group databases
PeroxiBase	4552. Ppy2CysPrx02.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSPPYT00000011193; ENSPPYP00000010771; ENSPPYG00000009607.
GeneID	100172251.
KEGG	pon:100172251.
Organism-specific databases
CTD	7001.
Phylogenomic databases
HOVERGEN	HBG000286.
InParanoid	Q5RC63.
OMA	HATAVEN.
OrthoDB	EOG4V6ZHJ.
Family and domain databases
InterPro	IPR000866. AhpC/TSA. IPR024706. Peroxiredoxin_AhpC-typ. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K03386.
Pfam	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_PONAB

Accession

Primary (citable) accession number: Q5RC63

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 56 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program