Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peroxiredoxin 1

Gene

Jafrac1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2 (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).By similarity

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin (By similarity). As a reducing substrate, thioredoxin 2 is preferred over thioredoxin 1 (PubMed:11877442).By similarity1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei47Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

  • thioredoxin peroxidase activity Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: FlyBase
  • cell redox homeostasis Source: UniProtKB
  • cellular response to DNA damage stimulus Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • germ cell development Source: FlyBase
  • germ cell migration Source: FlyBase
  • hydrogen peroxide catabolic process Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • response to oxidative stress Source: FlyBase
  • response to starvation Source: FlyBase

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiR-DME-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin 1 (EC:1.11.1.151 Publication)
Alternative name(s):
Cytosolic thioredoxin peroxidase
Short name:
DPx-4783
Short name:
DmTPx-1
Thioredoxin peroxidase
Gene namesi
Name:Jafrac1
Synonyms:TPX-1
ORF Names:CG1633
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0040309. Jafrac1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001350851 – 194Peroxiredoxin 1Add BLAST194

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47Interchain (with C-168); in linked formBy similarity
Disulfide bondi168Interchain (with C-47); in linked formBy similarity
Modified residuei193Phosphothreonine1 Publication1
Modified residuei194Phosphoserine1 Publication1

Post-translational modificationi

The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ9V3P0.
PRIDEiQ9V3P0.

PTM databases

iPTMnetiQ9V3P0.

Expressioni

Developmental stagei

Highly expressed during embryogenesis, weakly expressed during larval stages.2 Publications

Gene expression databases

BgeeiFBgn0040309.
ExpressionAtlasiQ9V3P0. differential.
GenevisibleiQ9V3P0. DM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (By similarity). Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity). Interacts with SESN1 and SESN2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
MtnBP119562EBI-82319,EBI-88468

Protein-protein interaction databases

BioGridi72802. 21 interactors.
DIPiDIP-17916N.
IntActiQ9V3P0. 18 interactors.
MINTiMINT-763596.
STRINGi7227.FBpp0073594.

Structurei

3D structure databases

ProteinModelPortaliQ9V3P0.
SMRiQ9V3P0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 160ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
InParanoidiQ9V3P0.
KOiK13279.
OMAiCPANWEE.
OrthoDBiEOG091G0IE5.
PhylomeDBiQ9V3P0.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9V3P0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQLQKPAPA FAGTAVVNGV FKDIKLSDYK GKYLVLFFYP LDFTFVCPTE
60 70 80 90 100
IIAFSESAAE FRKINCEVIG CSTDSQFTHL AWINTPRKQG GLGSMDIPLL
110 120 130 140 150
ADKSMKVARD YGVLDEETGI PFRGLFIIDD KQNLRQITVN DLPVGRSVEE
160 170 180 190
TLRLVQAFQY TDKYGEVCPA NWKPGQKTMV ADPTKSKEYF ETTS
Length:194
Mass (Da):21,738
Last modified:May 1, 2000 - v1
Checksum:i93ED319BE144E8D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF167098 mRNA. Translation: AAF42985.1.
AF321615 mRNA. Translation: AAK06770.1.
AF321616 mRNA. Translation: AAK06771.1.
AE014298 Genomic DNA. Translation: AAF48253.1.
AY070534 mRNA. Translation: AAL48005.1.
BT014630 mRNA. Translation: AAT27254.1.
RefSeqiNP_001285202.1. NM_001298273.1.
NP_001285203.1. NM_001298274.1.
NP_001285204.1. NM_001298275.1.
NP_477510.1. NM_058162.3.
NP_727689.1. NM_167359.2.
UniGeneiDm.3464.

Genome annotation databases

EnsemblMetazoaiFBtr0073763; FBpp0073594; FBgn0040309.
FBtr0073764; FBpp0073595; FBgn0040309.
FBtr0339699; FBpp0308756; FBgn0040309.
FBtr0339700; FBpp0308757; FBgn0040309.
FBtr0345161; FBpp0311371; FBgn0040309.
GeneIDi53578.
KEGGidme:Dmel_CG1633.

Similar proteinsi

Entry informationi

Entry nameiPRDX1_DROME
AccessioniPrimary (citable) accession number: Q9V3P0
Secondary accession number(s): Q0KHT0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: May 1, 2000
Last modified: September 27, 2017
This is version 148 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families