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Protein

Peroxiredoxin-2

Gene

PRDX2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei51Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Protein family/group databases

PeroxiBasei4552. Ppy2CysPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2 (EC:1.11.1.15)
Gene namesi
Name:PRDX2
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002568572 – 177Peroxiredoxin-2Add BLAST176

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Disulfide bondi51Interchain (with C-173); in linked formBy similarity
Modified residuei112PhosphoserineBy similarity1
Disulfide bondi173Interchain (with C-51); in linked formBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PRIDEiQ5RC63.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN (By similarity).By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000024125.

Structurei

3D structure databases

ProteinModelPortaliQ5RC63.
SMRiQ5RC63.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 164ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOVERGENiHBG000286.
InParanoidiQ5RC63.
KOiK03386.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR033046. PRDX2.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10681:SF124. PTHR10681:SF124. 1 hit.
PfamiPF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RC63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV
60 70 80 90 100
CPTEIIAFSN RAEDFHKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN
110 120 130 140 150
IPLLADVTRR LSEDYGVLKT DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR
160 170
SVDEALRLVQ AFQYTDEHGE GPCFASP
Length:177
Mass (Da):19,430
Last modified:January 23, 2007 - v3
Checksum:i6D95970252096370
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR858417 mRNA. Translation: CAH90647.1.
RefSeqiNP_001125349.1. NM_001131877.2.

Genome annotation databases

EnsembliENSPPYT00000011193; ENSPPYP00000010771; ENSPPYG00000009607.
GeneIDi100172251.
KEGGipon:100172251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR858417 mRNA. Translation: CAH90647.1.
RefSeqiNP_001125349.1. NM_001131877.2.

3D structure databases

ProteinModelPortaliQ5RC63.
SMRiQ5RC63.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000024125.

Protein family/group databases

PeroxiBasei4552. Ppy2CysPrx02.

Proteomic databases

PRIDEiQ5RC63.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSPPYT00000011193; ENSPPYP00000010771; ENSPPYG00000009607.
GeneIDi100172251.
KEGGipon:100172251.

Organism-specific databases

CTDi7001.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOVERGENiHBG000286.
InParanoidiQ5RC63.
KOiK03386.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR033046. PRDX2.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10681:SF124. PTHR10681:SF124. 1 hit.
PfamiPF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRDX2_PONAB
AccessioniPrimary (citable) accession number: Q5RC63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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).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).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.