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Protein

Peroxiredoxin 1

Gene

Jafrac1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -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
  • determination of adult lifespan Source: FlyBase
  • germ cell development Source: FlyBase
  • germ cell migration Source: FlyBase
  • hydrogen peroxide catabolic 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 baseline and 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
MINTiQ9V3P0
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
IPR036249 Thioredoxin-like_sf
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: July 18, 2018
This is version 153 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

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