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Q13162 (PRDX4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PRDX4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Subunit structure

Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation By similarity. Ref.1

Subcellular location

Cytoplasm. Secreted Ref.1.

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.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Ref.4
Chain38 – 271234Peroxiredoxin-4
PRO_0000135098

Regions

Domain79 – 237159Thioredoxin

Sites

Active site1241Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond124Interchain (with C-245); in linked form By similarity
Disulfide bond245Interchain (with C-124); in linked form By similarity

Experimental info

Sequence conflict121P → S in CAG46469. Ref.3
Sequence conflict511C → Y in CAG46469. Ref.3

Secondary structure

..................................... 271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13162 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7E56B580049FC60F

FASTA27130,540
        10         20         30         40         50         60 
MEALPLLAAT TPDHGRHRRL LLLPLLLFLL PAGAVQGWET EERPRTREEE CHFYAGGQVY 

        70         80         90        100        110        120 
PGEASRVSVA DHSLHLSKAK ISKPAPYWEG TAVIDGEFKE LKLTDYRGKY LVFFFYPLDF 

       130        140        150        160        170        180 
TFVCPTEIIA FGDRLEEFRS INTEVVACSV DSQFTHLAWI NTPRRQGGLG PIRIPLLSDL 

       190        200        210        220        230        240 
THQISKDYGV YLEDSGHTLR GLFIIDDKGI LRQITLNDLP VGRSVDETLR LVQAFQYTDK 

       250        260        270 
HGEVCPAGWK PGSETIIPDP AGKLKYFDKL N 

« Hide

References

« Hide 'large scale' references
[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(1997) [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 (JUN-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(2004) [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(2009) [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 (DEC-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(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: OVEROXIDATION AT CYS-124.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14206.1.
PIRG01790.
RefSeqNP_006397.1. NM_006406.1.
UniGeneHs.83383.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ13162.
SMRQ13162. Positions 74-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115800. 46 interactions.
IntActQ13162. 43 interactions.
MINTMINT-3027265.
STRING9606.ENSP00000368646.

Protein family/group databases

PeroxiBase4530. Hs2CysPrx04.

PTM databases

PhosphoSiteQ13162.

Polymorphism databases

DMDM3024727.

2D gel databases

OGPQ13162.
REPRODUCTION-2DPAGEIPI00011937.
UCD-2DPAGEQ13162.

Proteomic databases

MaxQBQ13162.
PaxDbQ13162.
PeptideAtlasQ13162.
PRIDEQ13162.

Protocols and materials databases

DNASU10549.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379341; ENSP00000368646; ENSG00000123131.
GeneID10549.
KEGGhsa:10549.
UCSCuc004dam.3. human.

Organism-specific databases

CTD10549.
GeneCardsGC0XP023592.
HGNCHGNC:17169. PRDX4.
HPACAB008659.
CAB027389.
CAB047362.
MIM606506. gene.
neXtProtNX_Q13162.
PharmGKBPA33725.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0450.
HOGENOMHOG000022343.
HOVERGENHBG000286.
InParanoidQ13162.
KOK03386.
OMAHWEGTAV.
PhylomeDBQ13162.
TreeFamTF105181.

Gene expression databases

ArrayExpressQ13162.
BgeeQ13162.
CleanExHS_PRDX4.
GenevestigatorQ13162.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13162.
GeneWikiPRDX4.
GenomeRNAi10549.
NextBio40013.
PROQ13162.
SOURCESearch...

Entry information

Entry namePRDX4_HUMAN
AccessionPrimary (citable) accession number: Q13162
Secondary accession number(s): Q6FHT3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM