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Reviewed, UniProtKB/Swiss-Prot Q9BGI2 (PRDX4_BOVIN)

Last modified June 16, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxiredoxin-4
    EC=1.11.1.15
Alternative name(s):
    Prx-IV
Gene names
Name: PRDX4
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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 By similarity.

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.

Subcellular location

Cytoplasm 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
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 274274Peroxiredoxin-4
PRO_0000135097

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

Sequences

Sequence LengthMass (Da)Tools
Q9BGI2-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: AE14176CF1C70E37

FASTA27430,741
        10         20         30         40         50         60 
MEAPPPPPPL PATTLAPGRS RKLLLLPLLL FLLRAEAVRG FEAEERPRTR EEECHFYAGG 

        70         80         90        100        110        120 
QVYPGEVSRV SVAEHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP 

       130        140        150        160        170        180 
LDFTFVCPTE IIAFGDRIDE FRSINTEVVA CSVDSQFTHL AWINTPRRQG GLGSINIPLL 

       190        200        210        220        230        240 
ADLNHQISKD YGVYLEDSGH TLRGLFIIDD KGILRQITLN DLPVGRSVDE TLRLVQAFQY 

       250        260        270 
TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of 4 new bovine peroxiredoxins, and screening of the complete peroxiredoxin family in different bovine tissues."
Leyens G., Donnay I., Knoops B.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.

Cross-references

Sequence databases

AF305563 mRNA. Translation: AAG53660.1.
BC109824 mRNA. Translation: AAI09825.1.
IPIIPI00691994.
RefSeqNP_776858.1.
UniGeneBt.5203

3D structure databases

HSSPHSSP built from PDB template 1QQ2 based on UniProtKB Q63716.
ModBaseSearch...

Protein family/group databases

PeroxiBase4531. Bt2CysPrx04.

Genome annotation databases

EnsemblENSBTAG00000006165. Bos taurus. [Contig view]
GeneID281999.
KEGGbta:281999.

Phylogenomic databases

HOVERGENQ9BGI2.
OMAQ9BGI2. AINTEVV.

Enzyme and pathway databases

BRENDA1.11.1.15. 251.

Family and domain databases

InterProIPR000866. Alkyl_hydroperoxide_Rdtase.
IPR019479. Peroxiredoxin_C.
IPR017936. Thioredoxin-like.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRDX4_BOVIN
AccessionPrimary (citable) accession number: Q9BGI2
Secondary accession number(s): Q32L06
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents