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O77834 (PRDX6_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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-6

EC=1.11.1.15
Alternative name(s):
1-Cys peroxiredoxin
Short name=1-Cys PRX
Acidic calcium-independent phospholipase A2
Short name=aiPLA2
EC=3.1.1.-
Antioxidant protein 2
Ciliary body glutathione peroxidase
Non-selenium glutathione peroxidase
Short name=NSGPx
EC=1.11.1.9
PHGPx
Gene names
Name:PRDX6
Synonyms:AOP2, GPX, PHGPX
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in redox regulation of the cell. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.

Catalytic activity

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

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Subunit structure

Homotetramer. Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration. May interact with HTR2A. Interacts with APEX1 and STH By similarity. May interact with FAM168B By similarity. Ref.7

Subcellular location

Cytoplasm By similarity. Lysosome By similarity. Cytoplasmic vesicle By similarity. Note: Also found in lung secretory organelles By similarity.

Miscellaneous

The active site is the redox-active Cys-47 oxidized to Cys-SOH. Unlike 2-Cys peroxiredoxins, PRDX6 conserves only this peroxidatic cysteine. To regenerate and activate the enzyme, the oxidized form is directly reduced to cysteine by glutathione and not thioredoxin.

Irreversibly inactivated by overoxidation of Cys-47 (to Cys-SO3H) upon oxidative stress By similarity.

Sequence similarities

Belongs to the AhpC/TSA family. Rehydrin subfamily.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 224223Peroxiredoxin-6
PRO_0000135101

Regions

Domain5 – 169165Thioredoxin

Sites

Active site321For phospholipase activity By similarity
Active site471Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue441Phosphothreonine By similarity
Modified residue631N6-acetyllysine By similarity
Modified residue891Phosphotyrosine By similarity
Modified residue2091N6-acetyllysine; alternate By similarity
Modified residue2091N6-succinyllysine; alternate By similarity
Disulfide bond47Interchain; in linked form By similarity

Sequences

Sequence LengthMass (Da)Tools
O77834 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4013D59C4D9FC05E

FASTA22425,067
        10         20         30         40         50         60 
MPGGLLLGDE APNFEANTTI GRIRFHDYLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE 

        70         80         90        100        110        120 
FAKRNVKMIA LSIDSVEDHL AWSKDINAYN GEEPTEKLPF PIIDDKNRDL AIQLGMLDPA 

       130        140        150        160        170        180 
EKDEKGMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVIISLQLT AEKRVATPVD 

       190        200        210        220 
WKNGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP 

« Hide

References

« Hide 'large scale' references
[1]"A novel glutathione peroxidase in bovine eye. Sequence analysis, mRNA level, and translation."
Singh A.K., Shichi H.
J. Biol. Chem. 273:26171-26178(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ocular ciliary body.
[2]"Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase."
Fisher A.B., Dodia C., Manevich Y., Chen J.-W., Feinstein S.I.
J. Biol. Chem. 274:21326-21334(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[3]"Glutathione peroxidase in the bovine oviduct."
Rojas Garcia P.P., Einspanier R.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Oviduct.
[4]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[6]"Non-selenium glutathione peroxidase without glutathione S-transferase activity from bovine ciliary body."
Shichi H., Demar J.C.
Exp. Eye Res. 50:513-520(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30.
[7]"Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST."
Manevich Y., Feinstein S.I., Fisher A.B.
Proc. Natl. Acad. Sci. U.S.A. 101:3780-3785(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GSTP1, ACTIVATION BY GLUTATHIONE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF080228 mRNA. Translation: AAC63016.1.
AF090194 mRNA. Translation: AAC84043.1.
AJ243848 mRNA. Translation: CAB64802.1.
BT020967 mRNA. Translation: AAX08984.1.
BC102172 mRNA. Translation: AAI02173.1.
RefSeqNP_777068.1. NM_174643.1.
UniGeneBt.49705.

3D structure databases

ProteinModelPortalO77834.
SMRO77834. Positions 5-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000006383.

Protein family/group databases

PeroxiBase4423. Bt1CysPrx.

Proteomic databases

PaxDbO77834.
PRIDEO77834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000006383; ENSBTAP00000006383; ENSBTAG00000004855.
GeneID282438.
KEGGbta:282438.

Organism-specific databases

CTD9588.

Phylogenomic databases

eggNOGCOG0450.
GeneTreeENSGT00550000074794.
HOGENOMHOG000022346.
HOVERGENHBG105234.
InParanoidO77834.
KOK11188.
OMAHPNANDT.
OrthoDBEOG7CNZGP.
TreeFamTF105183.

Enzyme and pathway databases

BRENDA1.11.1.15. 908.

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

NextBio20806213.

Entry information

Entry namePRDX6_BOVIN
AccessionPrimary (citable) accession number: O77834
Secondary accession number(s): Q5E9F3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 99 of the entry and version 3 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