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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  1. thioredoxin peroxidase activity Source: ProtInc

GO - Biological processi

  1. 4-hydroxyproline metabolic process Source: Ensembl
  2. cell redox homeostasis Source: Ensembl
  3. extracellular matrix organization Source: Ensembl
  4. I-kappaB phosphorylation Source: ProtInc
  5. male gonad development Source: Ensembl
  6. negative regulation of male germ cell proliferation Source: Ensembl
  7. protein maturation by protein folding Source: Ensembl
  8. reactive oxygen species metabolic process Source: Ensembl
  9. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 2681.

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
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:17169. PRDX4.

Subcellular locationi

Cytoplasm 1 Publication. Secreted 1 Publication

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: UniProtKB
  4. mitochondrion Source: Ensembl
  5. nucleus Source: UniProtKB
  6. smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33725.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 271234Peroxiredoxin-4PRO_0000135098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi124 – 124Interchain (with C-245); in linked formBy similarity
Disulfide bondi245 – 245Interchain (with C-124); in linked formBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ13162.
PaxDbiQ13162.
PeptideAtlasiQ13162.
PRIDEiQ13162.

2D gel databases

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

PTM databases

PhosphoSiteiQ13162.

Expressioni

Gene expression databases

BgeeiQ13162.
CleanExiHS_PRDX4.
ExpressionAtlasiQ13162. baseline and differential.
GenevestigatoriQ13162.

Organism-specific databases

HPAiCAB008659.
CAB027389.
CAB047362.

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. 52 interactions.
IntActiQ13162. 43 interactions.
MINTiMINT-3027265.
STRINGi9606.ENSP00000368646.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi75 – 784Combined sources
Beta strandi89 – 946Combined sources
Beta strandi97 – 1026Combined sources
Helixi103 – 1064Combined sources
Beta strandi109 – 1157Combined sources
Helixi123 – 13311Combined sources
Helixi135 – 1395Combined sources
Turni140 – 1423Combined sources
Beta strandi143 – 1519Combined sources
Helixi153 – 1608Combined sources
Helixi164 – 1663Combined sources
Beta strandi176 – 1783Combined sources
Helixi183 – 1875Combined sources
Turni193 – 1953Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi200 – 2056Combined sources
Beta strandi209 – 2179Combined sources
Helixi225 – 24117Combined sources
Turni260 – 2623Combined sources
Helixi263 – 2675Combined sources
Turni268 – 2703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ13162.
SMRiQ13162. Positions 74-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13162.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 237159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiCOG0450.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ13162.
KOiK03386.
OMAiFHKGEFV.
PhylomeDBiQ13162.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[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:October 31, 1996 - v1
Checksum:i7E56B580049FC60F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121P → S in CAG46469 (PubMed:15489334).Curated
Sequence conflicti51 – 511C → Y in CAG46469 (PubMed:15489334).Curated

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.
UCSCiuc004dam.3. human.

Polymorphism databases

DMDMi3024727.

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
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[»]
ProteinModelPortaliQ13162.
SMRiQ13162. Positions 74-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115800. 52 interactions.
IntActiQ13162. 43 interactions.
MINTiMINT-3027265.
STRINGi9606.ENSP00000368646.

Protein family/group databases

PeroxiBasei4530. Hs2CysPrx04.

PTM databases

PhosphoSiteiQ13162.

Polymorphism databases

DMDMi3024727.

2D gel databases

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

Proteomic databases

MaxQBiQ13162.
PaxDbiQ13162.
PeptideAtlasiQ13162.
PRIDEiQ13162.

Protocols and materials databases

DNASUi10549.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379341; ENSP00000368646; ENSG00000123131.
GeneIDi10549.
KEGGihsa:10549.
UCSCiuc004dam.3. human.

Organism-specific databases

CTDi10549.
GeneCardsiGC0XP023592.
HGNCiHGNC:17169. PRDX4.
HPAiCAB008659.
CAB027389.
CAB047362.
MIMi300927. gene.
neXtProtiNX_Q13162.
PharmGKBiPA33725.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0450.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ13162.
KOiK03386.
OMAiFHKGEFV.
PhylomeDBiQ13162.
TreeFamiTF105181.

Enzyme and pathway databases

BRENDAi1.11.1.15. 2681.

Miscellaneous databases

ChiTaRSiPRDX4. human.
EvolutionaryTraceiQ13162.
GeneWikiiPRDX4.
GenomeRNAii10549.
NextBioi40013.
PROiQ13162.
SOURCEiSearch...

Gene expression databases

BgeeiQ13162.
CleanExiHS_PRDX4.
ExpressionAtlasiQ13162. baseline and differential.
GenevestigatoriQ13162.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[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...

Publicationsi

« Hide 'large scale' publications
  1. "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation."
    Jin D.-Y., Chae H.Z., Rhee S.G., Jeang K.-T.
    J. Biol. Chem. 272:30952-30961(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
    Xu G., Shin S.B., Jaffrey S.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 38-46.
    Tissue: Leukemic T-cell.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (NOV-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 46-66; 81-99; 140-164; 174-208; 213-223 AND 231-263, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  6. "A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress."
    Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
    Biochem. J. 366:777-785(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: OVEROXIDATION AT CYS-124.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPRDX4_HUMAN
AccessioniPrimary (citable) accession number: Q13162
Secondary accession number(s): Q6FHT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 14, 1998
Last sequence update: October 31, 1996
Last modified: March 31, 2015
This is version 150 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

External Data

Dasty 3

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 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.