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Protein

Peroxiredoxin-1

Gene

PRDX1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in redox regulation of the cell (By similarity). Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin (By similarity). May play an important role in eliminating peroxides generated during metabolism (By similarity). 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 similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei52 – 521Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiR-GGA-3299685. Detoxification of Reactive Oxygen Species.
R-GGA-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-1 (EC:1.11.1.15)
Gene namesi
Name:PRDX1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 8

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521C → S: Abolishes the ability to form a mixed-disulfide with GDPD5; when associated with S-173. 1 Publication
Mutagenesisi173 – 1731C → S: Abolishes the ability to form a mixed-disulfide with GDPD5; when associated with S-52. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Peroxiredoxin-1PRO_0000387961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 – 52Interchain (with C-173); in linked formBy similarity
Disulfide bondi173 – 173Interchain (with C-52); in linked formBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0CB50.
PRIDEiP0CB50.

Expressioni

Gene expression databases

BgeeiENSGALG00000010243.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation (By similarity). Forms a mixed-disulfide with GDPD5.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
GDPD5Q3KTM25EBI-2464239,EBI-2464223

Protein-protein interaction databases

IntActiP0CB50. 1 interaction.
STRINGi9031.ENSGALP00000016629.

Structurei

3D structure databases

ProteinModelPortaliP0CB50.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 165160ThioredoxinPROSITE-ProRule annotationAdd
BLAST

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.
HOGENOMiHOG000022343.
InParanoidiP0CB50.
KOiK13279.
OMAiTAEVHFA.
OrthoDBiEOG091G0IE5.
PhylomeDBiP0CB50.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. 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.

P0CB50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGKAFIGK PAPDFTATAV MPDGQFKDIK LSDYRGKYVV FFFYPLDFTF
60 70 80 90 100
VCPTEIIAYS DRADEFKKIN CEIIGASVDS HFCHLAWINT PKKQGGLGTM
110 120 130 140 150
KIPLVSDTKR VIAKDYGVLK EDEGIAYRGL FIIDEKGILR QITINDLPVG
160 170 180 190
RSVDETLRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVQK SKEYFSKQK
Length:199
Mass (Da):22,315
Last modified:November 3, 2009 - v1
Checksum:i6377365A582E9171
GO

Sequence databases

RefSeqiNP_001258861.1. NM_001271932.1.
UniGeneiGga.5204.

Genome annotation databases

EnsembliENSGALT00000016648; ENSGALP00000016629; ENSGALG00000010243.
GeneIDi424598.
KEGGigga:424598.

Cross-referencesi

Sequence databases

RefSeqiNP_001258861.1. NM_001271932.1.
UniGeneiGga.5204.

3D structure databases

ProteinModelPortaliP0CB50.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0CB50. 1 interaction.
STRINGi9031.ENSGALP00000016629.

Proteomic databases

PaxDbiP0CB50.
PRIDEiP0CB50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000016648; ENSGALP00000016629; ENSGALG00000010243.
GeneIDi424598.
KEGGigga:424598.

Organism-specific databases

CTDi5052.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
InParanoidiP0CB50.
KOiK13279.
OMAiTAEVHFA.
OrthoDBiEOG091G0IE5.
PhylomeDBiP0CB50.

Enzyme and pathway databases

ReactomeiR-GGA-3299685. Detoxification of Reactive Oxygen Species.
R-GGA-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

PROiP0CB50.

Gene expression databases

BgeeiENSGALG00000010243.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. 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 nameiPRDX1_CHICK
AccessioniPrimary (citable) accession number: P0CB50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: November 3, 2009
Last modified: September 7, 2016
This is version 49 of the entry and version 1 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-52 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-52 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
Reduced levels of PRDX1 by RNAi cause the loss of motor neurons but did not alter the number of motor neuron progenitors or the dorsal-ventral pattering of spinal progenitors, and did not compromise motor neuron survival.

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.