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Protein

Peroxiredoxin-4

Gene

PRDX4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei124Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

  • thioredoxin peroxidase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciZFISH:HS04632-MONOMER.
BRENDAi1.11.1.15. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Protein family/group databases

PeroxiBasei4530. Hs2CysPrx04.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-4 (EC:1.11.1.15)
Alternative name(s):
Antioxidant enzyme AOE372
Short name:
AOE37-2
Peroxiredoxin IV
Short name:
Prx-IV
Thioredoxin peroxidase AO372
Thioredoxin-dependent peroxide reductase A0372
Gene namesi
Name:PRDX4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:17169. PRDX4.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: Ensembl
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB
  • smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi10549.
OpenTargetsiENSG00000123131.
PharmGKBiPA33725.

Polymorphism and mutation databases

BioMutaiPRDX4.
DMDMi3024727.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 37Combined sources1 PublicationAdd BLAST37
ChainiPRO_000013509838 – 271Peroxiredoxin-4Add BLAST234

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi124Interchain (with C-245); in linked formBy similarity
Disulfide bondi245Interchain (with C-124); in linked formBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ13162.
PaxDbiQ13162.
PeptideAtlasiQ13162.
PRIDEiQ13162.
TopDownProteomicsiQ13162.

2D gel databases

OGPiQ13162.
REPRODUCTION-2DPAGEIPI00011937.
UCD-2DPAGEQ13162.

PTM databases

iPTMnetiQ13162.
PhosphoSitePlusiQ13162.
SwissPalmiQ13162.

Expressioni

Gene expression databases

BgeeiENSG00000123131.
CleanExiHS_PRDX4.
ExpressionAtlasiQ13162. baseline and differential.
GenevisibleiQ13162. HS.

Organism-specific databases

HPAiCAB008659.
CAB027389.

Interactioni

Subunit structurei

Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LBPP184284EBI-2211957,EBI-3927059
P4HBP072372EBI-2211957,EBI-395883
PDIA3P301012EBI-2211957,EBI-979862
PDIA6Q150842EBI-2211957,EBI-1043087
TBXA2RP217313EBI-2211957,EBI-2625082
TXNDC5Q8NBS92EBI-2211957,EBI-2510815

Protein-protein interaction databases

BioGridi115800. 54 interactors.
IntActiQ13162. 49 interactors.
MINTiMINT-3027265.
STRINGi9606.ENSP00000368646.

Structurei

Secondary structure

1271
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi75 – 78Combined sources4
Beta strandi89 – 94Combined sources6
Beta strandi97 – 102Combined sources6
Helixi103 – 106Combined sources4
Beta strandi109 – 115Combined sources7
Helixi123 – 133Combined sources11
Helixi135 – 139Combined sources5
Turni140 – 142Combined sources3
Beta strandi143 – 151Combined sources9
Helixi153 – 160Combined sources8
Helixi164 – 166Combined sources3
Beta strandi176 – 178Combined sources3
Helixi183 – 187Combined sources5
Turni193 – 195Combined sources3
Beta strandi196 – 198Combined sources3
Beta strandi200 – 205Combined sources6
Beta strandi209 – 217Combined sources9
Helixi225 – 241Combined sources17
Turni260 – 262Combined sources3
Helixi263 – 267Combined sources5
Turni268 – 270Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PN8X-ray1.80A/B/C/D/E/F/G/H/I/J84-271[»]
3TJBX-ray2.38A/B/C/D/E38-271[»]
3TJFX-ray2.04A/B/C/D/E38-271[»]
3TJGX-ray2.24A/B/C/D/E38-271[»]
3TJJX-ray1.91A/B/C/D/E38-271[»]
3TJKX-ray2.09A/B/C/D/E38-271[»]
3TKPX-ray2.49A/B/C/D/E38-271[»]
3TKQX-ray2.22A/B/C/D/E38-271[»]
3TKRX-ray2.10A/B/C/D/E/F/G/H/I/J38-271[»]
3TKSX-ray2.40A/B/C/D/E38-271[»]
4RQXX-ray2.26A/B/C/D/E79-271[»]
5HQPX-ray2.60A/B38-271[»]
ProteinModelPortaliQ13162.
SMRiQ13162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13162.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini79 – 237ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ13162.
KOiK03386.
OMAiYAGGHVY.
OrthoDBiEOG091G0IE5.
PhylomeDBiQ13162.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
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]
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.

Q13162-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEALPLLAAT TPDHGRHRRL LLLPLLLFLL PAGAVQGWET EERPRTREEE
60 70 80 90 100
CHFYAGGQVY PGEASRVSVA DHSLHLSKAK ISKPAPYWEG TAVIDGEFKE
110 120 130 140 150
LKLTDYRGKY LVFFFYPLDF TFVCPTEIIA FGDRLEEFRS INTEVVACSV
160 170 180 190 200
DSQFTHLAWI NTPRRQGGLG PIRIPLLSDL THQISKDYGV YLEDSGHTLR
210 220 230 240 250
GLFIIDDKGI LRQITLNDLP VGRSVDETLR LVQAFQYTDK HGEVCPAGWK
260 270
PGSETIIPDP AGKLKYFDKL N
Length:271
Mass (Da):30,540
Last modified:November 1, 1996 - v1
Checksum:i7E56B580049FC60F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12P → S in CAG46469 (PubMed:15489334).Curated1
Sequence conflicti51C → Y in CAG46469 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25182 mRNA. Translation: AAB95175.1.
CR541668 mRNA. Translation: CAG46469.1.
CR541705 mRNA. Translation: CAG46506.1.
BC003609 mRNA. Translation: AAH03609.1.
BC007107 mRNA. Translation: AAH07107.1.
BC016770 mRNA. Translation: AAH16770.1.
CCDSiCCDS14206.1.
PIRiG01790.
RefSeqiNP_006397.1. NM_006406.1.
UniGeneiHs.83383.

Genome annotation databases

EnsembliENST00000379341; ENSP00000368646; ENSG00000123131.
GeneIDi10549.
KEGGihsa:10549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25182 mRNA. Translation: AAB95175.1.
CR541668 mRNA. Translation: CAG46469.1.
CR541705 mRNA. Translation: CAG46506.1.
BC003609 mRNA. Translation: AAH03609.1.
BC007107 mRNA. Translation: AAH07107.1.
BC016770 mRNA. Translation: AAH16770.1.
CCDSiCCDS14206.1.
PIRiG01790.
RefSeqiNP_006397.1. NM_006406.1.
UniGeneiHs.83383.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PN8X-ray1.80A/B/C/D/E/F/G/H/I/J84-271[»]
3TJBX-ray2.38A/B/C/D/E38-271[»]
3TJFX-ray2.04A/B/C/D/E38-271[»]
3TJGX-ray2.24A/B/C/D/E38-271[»]
3TJJX-ray1.91A/B/C/D/E38-271[»]
3TJKX-ray2.09A/B/C/D/E38-271[»]
3TKPX-ray2.49A/B/C/D/E38-271[»]
3TKQX-ray2.22A/B/C/D/E38-271[»]
3TKRX-ray2.10A/B/C/D/E/F/G/H/I/J38-271[»]
3TKSX-ray2.40A/B/C/D/E38-271[»]
4RQXX-ray2.26A/B/C/D/E79-271[»]
5HQPX-ray2.60A/B38-271[»]
ProteinModelPortaliQ13162.
SMRiQ13162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115800. 54 interactors.
IntActiQ13162. 49 interactors.
MINTiMINT-3027265.
STRINGi9606.ENSP00000368646.

Protein family/group databases

PeroxiBasei4530. Hs2CysPrx04.

PTM databases

iPTMnetiQ13162.
PhosphoSitePlusiQ13162.
SwissPalmiQ13162.

Polymorphism and mutation databases

BioMutaiPRDX4.
DMDMi3024727.

2D gel databases

OGPiQ13162.
REPRODUCTION-2DPAGEIPI00011937.
UCD-2DPAGEQ13162.

Proteomic databases

EPDiQ13162.
PaxDbiQ13162.
PeptideAtlasiQ13162.
PRIDEiQ13162.
TopDownProteomicsiQ13162.

Protocols and materials databases

DNASUi10549.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379341; ENSP00000368646; ENSG00000123131.
GeneIDi10549.
KEGGihsa:10549.

Organism-specific databases

CTDi10549.
DisGeNETi10549.
GeneCardsiPRDX4.
HGNCiHGNC:17169. PRDX4.
HPAiCAB008659.
CAB027389.
MIMi300927. gene.
neXtProtiNX_Q13162.
OpenTargetsiENSG00000123131.
PharmGKBiPA33725.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ13162.
KOiK03386.
OMAiYAGGHVY.
OrthoDBiEOG091G0IE5.
PhylomeDBiQ13162.
TreeFamiTF105181.

Enzyme and pathway databases

BioCyciZFISH:HS04632-MONOMER.
BRENDAi1.11.1.15. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiPRDX4. human.
EvolutionaryTraceiQ13162.
GeneWikiiPRDX4.
GenomeRNAii10549.
PROiQ13162.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000123131.
CleanExiHS_PRDX4.
ExpressionAtlasiQ13162. baseline and differential.
GenevisibleiQ13162. HS.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
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]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRDX4_HUMAN
AccessioniPrimary (citable) accession number: Q13162
Secondary accession number(s): Q6FHT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The active site is the redox-active Cys-124 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-245-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.
Irreversibly inactivated by overoxidation of Cys-124 (to Cys-SO3H) upon oxidative stress.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.