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Q13162

- PRDX4_HUMAN

UniProt

Q13162 - PRDX4_HUMAN

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Protein

Peroxiredoxin-4

Gene

PRDX4

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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: Chromosome X

Organism-specific databases

HGNCiHGNC:17169. PRDX4.

Subcellular locationi

Cytoplasm 1 Publication. Secreted 1 Publication

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum Source: Ensembl
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: UniProt
  5. mitochondrion Source: Ensembl
  6. nucleus Source: UniProt
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. 48 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 – 784
Beta strandi89 – 946
Beta strandi97 – 1026
Helixi103 – 1064
Beta strandi109 – 1157
Helixi123 – 13311
Helixi135 – 1395
Turni140 – 1423
Beta strandi143 – 1519
Helixi153 – 1608
Helixi164 – 1663
Beta strandi176 – 1783
Helixi183 – 1875
Turni193 – 1953
Beta strandi196 – 1983
Beta strandi200 – 2056
Beta strandi209 – 2179
Helixi225 – 24117
Turni260 – 2623
Helixi263 – 2675
Turni268 – 2703

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiHWEGTAV.
PhylomeDBiQ13162.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[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.

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)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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14206.1.
PIRi G01790.
RefSeqi NP_006397.1. NM_006406.1.
UniGenei Hs.83383.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PN8 X-ray 1.80 A/B/C/D/E/F/G/H/I/J 84-271 [» ]
3TJB X-ray 2.38 A/B/C/D/E 38-271 [» ]
3TJF X-ray 2.04 A/B/C/D/E 38-271 [» ]
3TJG X-ray 2.24 A/B/C/D/E 38-271 [» ]
3TJJ X-ray 1.91 A/B/C/D/E 38-271 [» ]
3TJK X-ray 2.09 A/B/C/D/E 38-271 [» ]
3TKP X-ray 2.49 A/B/C/D/E 38-271 [» ]
3TKQ X-ray 2.22 A/B/C/D/E 38-271 [» ]
3TKR X-ray 2.10 A/B/C/D/E/F/G/H/I/J 38-271 [» ]
3TKS X-ray 2.40 A/B/C/D/E 38-271 [» ]
ProteinModelPortali Q13162.
SMRi Q13162. Positions 74-269.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115800. 48 interactions.
IntActi Q13162. 43 interactions.
MINTi MINT-3027265.
STRINGi 9606.ENSP00000368646.

Protein family/group databases

PeroxiBasei 4530. Hs2CysPrx04.

PTM databases

PhosphoSitei Q13162.

Polymorphism databases

DMDMi 3024727.

2D gel databases

OGPi Q13162.
REPRODUCTION-2DPAGE IPI00011937.
UCD-2DPAGE Q13162.

Proteomic databases

MaxQBi Q13162.
PaxDbi Q13162.
PeptideAtlasi Q13162.
PRIDEi Q13162.

Protocols and materials databases

DNASUi 10549.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379341 ; ENSP00000368646 ; ENSG00000123131 .
GeneIDi 10549.
KEGGi hsa:10549.
UCSCi uc004dam.3. human.

Organism-specific databases

CTDi 10549.
GeneCardsi GC0XP023592.
HGNCi HGNC:17169. PRDX4.
HPAi CAB008659.
CAB027389.
CAB047362.
MIMi 300927. gene.
neXtProti NX_Q13162.
PharmGKBi PA33725.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0450.
HOGENOMi HOG000022343.
HOVERGENi HBG000286.
InParanoidi Q13162.
KOi K03386.
OMAi HWEGTAV.
PhylomeDBi Q13162.
TreeFami TF105181.

Miscellaneous databases

EvolutionaryTracei Q13162.
GeneWikii PRDX4.
GenomeRNAii 10549.
NextBioi 40013.
PROi Q13162.
SOURCEi Search...

Gene expression databases

Bgeei Q13162.
CleanExi HS_PRDX4.
ExpressionAtlasi Q13162. baseline and differential.
Genevestigatori Q13162.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000239. AHPC. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: October 29, 2014
This is version 146 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