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O08807 (PRDX4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Peroxiredoxin IV
Short name=Prx-IV
Thioredoxin peroxidase AO372
Thioredoxin-dependent peroxide reductase A0372
Gene names
Name:Prdx4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length274 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.

Catalytic activity

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

Subunit structure

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

Subcellular location

Cytoplasm By similarity. Secreted By similarity.

Miscellaneous

The active site is the redox-active Cys-127 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-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.

Irreversibly inactivated by overoxidation of Cys-127 (to Cys-SO3H) upon oxidative stress By similarity.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Secreted
   DomainRedox-active center
Signal
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process4-hydroxyproline metabolic process

Inferred from genetic interaction PubMed 22981861. Source: MGI

cell redox homeostasis

Inferred from genetic interaction PubMed 23589496. Source: MGI

extracellular matrix organization

Inferred from genetic interaction PubMed 22981861. Source: MGI

male gonad development

Inferred from mutant phenotype PubMed 19105792. Source: MGI

negative regulation of male germ cell proliferation

Inferred from mutant phenotype PubMed 19105792. Source: MGI

oxidation-reduction process

Inferred from mutant phenotype PubMed 19105792. Source: MGI

protein maturation by protein folding

Inferred from genetic interaction PubMed 22981861. Source: MGI

reactive oxygen species metabolic process

Inferred from direct assay Ref.1. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 19105792. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: MGI

cytosol

Inferred from direct assay PubMed 21835919. Source: MGI

endoplasmic reticulum

Inferred from direct assay PubMed 21835919. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

   Molecular_functionperoxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peroxiredoxin activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein homodimerization activity

Inferred from direct assay PubMed 21835919. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 By similarity
Chain41 – 274234Peroxiredoxin-4
PRO_0000135099

Regions

Domain82 – 240159Thioredoxin

Sites

Active site1271Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond127Interchain (with C-248); in linked form By similarity
Disulfide bond248Interchain (with C-127); in linked form By similarity

Secondary structure

................................ 274
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O08807 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 73DB5374EC46241C

FASTA27431,053
        10         20         30         40         50         60 
MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR ENECHFYAGG 

        70         80         90        100        110        120 
QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP 

       130        140        150        160        170        180 
LDFTFVCPTE IIAFGDRIEE FKSINTEVVA CSVDSQFTHL AWINTPRRQG GLGPIRIPLL 

       190        200        210        220        230        240 
SDLNHQISKD YGVYLEDSGH TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY 

       250        260        270 
TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of human and mouse peroxiredoxin IV: evidence for inhibition by Prx-IV of epidermal growth factor- and p53-induced reactive oxygen species."
Wong C.M., Chun A.C., Kok K.H., Zhou Y., Fung P.C., Kung H.F., Jeang K.-T., Jin D.-Y.
Antioxid. Redox Signal. 2:507-518(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Bone marrow and Liver.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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].
Strain: C57BL/6J and NMRI.
Tissue: Mammary gland and Mammary tumor.
[5]Lubec G., Kang S.U., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 190-203 AND 216-226.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96746 mRNA. Translation: AAB57846.1.
AK005031 mRNA. Translation: BAB23758.1.
AK146402 mRNA. Translation: BAE27143.1.
AK152255 mRNA. Translation: BAE31074.1.
BX005263 Genomic DNA. Translation: CAM23139.1.
BC003349 mRNA. Translation: AAH03349.1.
BC019578 mRNA. Translation: AAH19578.1.
RefSeqNP_058044.1. NM_016764.4.
UniGeneMm.247542.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VWUX-ray3.30A/B/C/D/E/F/G/H/I/J41-274[»]
3VWVX-ray1.80A/B87-274[»]
3W8JX-ray2.10C/D244-263[»]
ProteinModelPortalO08807.
SMRO08807. Positions 78-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207303. 1 interaction.
IntActO08807. 5 interactions.
MINTMINT-1862981.
STRING10090.ENSMUSP00000026328.

Protein family/group databases

PeroxiBase4532. Mm2CysPrx04.

PTM databases

PhosphoSiteO08807.

2D gel databases

REPRODUCTION-2DPAGEO08807.

Proteomic databases

PaxDbO08807.
PRIDEO08807.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026328; ENSMUSP00000026328; ENSMUSG00000025289.
GeneID53381.
KEGGmmu:53381.
UCSCuc009uru.1. mouse.

Organism-specific databases

CTD10549.
MGIMGI:1859815. Prdx4.

Phylogenomic databases

eggNOGCOG0450.
GeneTreeENSGT00390000004653.
HOGENOMHOG000022343.
HOVERGENHBG000286.
InParanoidB1AZS7.
KOK03386.
OrthoDBEOG7T1RCD.
PhylomeDBO08807.
TreeFamTF105181.

Gene expression databases

ArrayExpressO08807.
BgeeO08807.
CleanExMM_PRDX4.
GenevestigatorO08807.

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

NextBio310209.
PROO08807.
SOURCESearch...

Entry information

Entry namePRDX4_MOUSE
AccessionPrimary (citable) accession number: O08807
Secondary accession number(s): B1AZS7, Q3U8E4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot