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O77834

- PRDX6_BOVIN

UniProt

O77834 - PRDX6_BOVIN

Protein

Peroxiredoxin-6

Gene

PRDX6

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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 activityBy similarity
    Active sitei47 – 471Cysteine sulfenic acid (-SOH) intermediateBy 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

    GO - Biological processi

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

    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

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Lysosome

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441PhosphothreonineBy similarity
    Disulfide bondi47 – 47Interchain; in linked formBy similarity
    Modified residuei63 – 631N6-acetyllysineBy similarity
    Modified residuei89 – 891PhosphotyrosineBy similarity
    Modified residuei209 – 2091N6-acetyllysine; alternateBy similarity
    Modified residuei209 – 2091N6-succinyllysine; alternateBy 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.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000006383.

    Structurei

    3D structure databases

    ProteinModelPortaliO77834.
    SMRiO77834. Positions 5-224.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 169165ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AhpC/TSA family. Rehydrin subfamily.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 102 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