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O77834

- PRDX6_BOVIN

UniProt

O77834 - PRDX6_BOVIN

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Protein
Peroxiredoxin-6
Gene
PRDX6, AOP2, GPX, PHGPX
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321For phospholipase activity By similarity
Active sitei47 – 471Cysteine sulfenic acid (-SOH) intermediate By similarity

GO - Molecular functioni

  1. glutathione peroxidase activity Source: UniProtKB-EC
  2. peroxidase activity Source: AgBase
  3. peroxiredoxin activity Source: UniProtKB-EC
  4. phospholipase A2 activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. phospholipid catabolic process Source: Ensembl
  2. response to reactive oxygen species Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Hydrolase, Oxidoreductase, Peroxidase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi1.11.1.15. 908.
ReactomeiREACT_204534. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei4423. Bt1CysPrx.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-6 (EC:1.11.1.15)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
Acidic calcium-independent phospholipase A2 (EC:3.1.1.-)
Short name:
aiPLA2
Antioxidant protein 2
Ciliary body glutathione peroxidase
Non-selenium glutathione peroxidase (EC:1.11.1.9)
Short name:
NSGPx
PHGPx
Gene namesi
Name:PRDX6
Synonyms:AOP2, GPX, PHGPX
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 16

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  3. cytosol Source: AgBase
  4. lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 224223Peroxiredoxin-6
PRO_0000135101Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Phosphothreonine By similarity
Disulfide bondi47 – 47Interchain; in linked form By similarity
Modified residuei63 – 631N6-acetyllysine By similarity
Modified residuei89 – 891Phosphotyrosine By similarity
Modified residuei209 – 2091N6-acetyllysine; alternate By similarity
Modified residuei209 – 2091N6-succinyllysine; alternate By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiO77834.
PRIDEiO77834.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006383.

Structurei

3D structure databases

ProteinModelPortaliO77834.
SMRiO77834. Positions 5-224.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 169165Thioredoxin
Add
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
GeneTreeiENSGT00550000074794.
HOGENOMiHOG000022346.
HOVERGENiHBG105234.
InParanoidiO77834.
KOiK11188.
OMAiSTGRNFH.
OrthoDBiEOG7CNZGP.
TreeFamiTF105183.

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.

O77834-1 [UniParc]FASTAAdd to Basket

« Hide

MPGGLLLGDE APNFEANTTI GRIRFHDYLG DSWGILFSHP RDFTPVCTTE    50
LGRAAKLAPE FAKRNVKMIA LSIDSVEDHL AWSKDINAYN GEEPTEKLPF 100
PIIDDKNRDL AIQLGMLDPA EKDEKGMPVT ARVVFIFGPD KKLKLSILYP 150
ATTGRNFDEI LRVIISLQLT AEKRVATPVD WKNGDSVMVL PTIPEEEAKK 200
LFPKGVFTKE LPSGKKYLRY TPQP 224
Length:224
Mass (Da):25,067
Last modified:January 23, 2007 - v3
Checksum:i4013D59C4D9FC05E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_777068.1. NM_174643.1.
UniGeneiBt.49705.

Genome annotation databases

EnsembliENSBTAT00000006383; ENSBTAP00000006383; ENSBTAG00000004855.
GeneIDi282438.
KEGGibta:282438.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_777068.1. NM_174643.1.
UniGenei Bt.49705.

3D structure databases

ProteinModelPortali O77834.
SMRi O77834. Positions 5-224.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000006383.

Protein family/group databases

PeroxiBasei 4423. Bt1CysPrx.

Proteomic databases

PaxDbi O77834.
PRIDEi O77834.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000006383 ; ENSBTAP00000006383 ; ENSBTAG00000004855 .
GeneIDi 282438.
KEGGi bta:282438.

Organism-specific databases

CTDi 9588.

Phylogenomic databases

eggNOGi COG0450.
GeneTreei ENSGT00550000074794.
HOGENOMi HOG000022346.
HOVERGENi HBG105234.
InParanoidi O77834.
KOi K11188.
OMAi STGRNFH.
OrthoDBi EOG7CNZGP.
TreeFami TF105183.

Enzyme and pathway databases

BRENDAi 1.11.1.15. 908.
Reactomei REACT_204534. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi 20806213.

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. "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. 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.

Entry informationi

Entry nameiPRDX6_BOVIN
AccessioniPrimary (citable) accession number: O77834
Secondary accession number(s): Q5E9F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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