Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00435

- GPX1_BOVIN

UniProt

P00435 - GPX1_BOVIN

Protein

Glutathione peroxidase 1

Gene

GPX1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Protects the hemoglobin in erythrocytes from oxidative breakdown.

    Catalytic activityi

    2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei41 – 411Not glycated
    Active sitei52 – 521
    Sitei52 – 521Subject to oxidation and hydroselenide loss to dehydroalanineBy similarity
    Sitei91 – 911Not glycated
    Sitei100 – 1001Not glycated
    Sitei124 – 1241Not glycated
    Sitei151 – 1511Not glycated
    Sitei169 – 1691Not glycated

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. response to oxidative stress Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Protein family/group databases

    PeroxiBasei3635. BtGPx01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione peroxidase 1 (EC:1.11.1.9)
    Short name:
    GPx-1
    Short name:
    GSHPx-1
    Alternative name(s):
    Cellular glutathione peroxidase
    Gene namesi
    Name:GPX1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205Glutathione peroxidase 1PRO_0000066608Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei91 – 911N6-acetyllysineBy similarity
    Modified residuei117 – 1171N6-acetyllysine; alternateBy similarity
    Modified residuei117 – 1171N6-succinyllysine; alternateBy similarity
    Glycosylationi117 – 1171N-linked (Glc) (glycation); in vitro
    Modified residuei124 – 1241N6-acetyllysineBy similarity
    Modified residuei151 – 1511N6-acetyllysineBy similarity

    Post-translational modificationi

    During periods of oxidative stress, Sec-52 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.By similarity

    Keywords - PTMi

    Acetylation, Glycation, Glycoprotein

    Proteomic databases

    PaxDbiP00435.
    PRIDEiP00435.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with MIEN1.

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000005597.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 213
    Helixi35 – 384
    Beta strandi41 – 488
    Helixi55 – 6915
    Helixi70 – 723
    Beta strandi74 – 807
    Turni83 – 864
    Helixi92 – 943
    Helixi95 – 1017
    Beta strandi111 – 1155
    Beta strandi119 – 1224
    Helixi127 – 1359
    Helixi150 – 1523
    Beta strandi155 – 1573
    Beta strandi169 – 1724
    Beta strandi178 – 1825
    Helixi188 – 1914
    Helixi192 – 1998

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GP1X-ray2.00A/B8-205[»]
    ProteinModelPortaliP00435.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00435.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutathione peroxidase family.Curated

    Phylogenomic databases

    eggNOGiCOG0386.
    HOVERGENiHBG004333.
    InParanoidiP00435.
    KOiK00432.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR000889. Glutathione_peroxidase.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PANTHERiPTHR11592. PTHR11592. 1 hit.
    PfamiPF00255. GSHPx. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
    PRINTSiPR01011. GLUTPROXDASE.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
    PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
    PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00435-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCAAQRSAAA LAAAAPRTVY AFSARPLAGG EPFNLSSLRG KVLLIENVAS    50
    LUGTTVRDYT QMNDLQRRLG PRGLVVLGFP CNQFGHQENA KNEEILNCLK 100
    YVRPGGGFEP NFMLFEKCEV NGEKAHPLFA FLREVLPTPS DDATALMTDP 150
    KFITWSPVCR NDVSWNFEKF LVGPDGVPVR RYSRRFLTID IEPDIETLLS 200
    QGASA 205
    Length:205
    Mass (Da):22,659
    Last modified:February 26, 2008 - v3
    Checksum:i7CBDF736CAAA92F6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961L → P in AAI49309. 1 PublicationCurated

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei52 – 521Selenocysteine

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13684 mRNA. Translation: CAB40806.1.
    BC149308 mRNA. Translation: AAI49309.1.
    PIRiS04872. OPBOE.
    RefSeqiNP_776501.1. NM_174076.3.
    UniGeneiBt.4317.

    Genome annotation databases

    GeneIDi281209.
    KEGGibta:281209.

    Keywords - Coding sequence diversityi

    Selenocysteine

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13684 mRNA. Translation: CAB40806.1 .
    BC149308 mRNA. Translation: AAI49309.1 .
    PIRi S04872. OPBOE.
    RefSeqi NP_776501.1. NM_174076.3.
    UniGenei Bt.4317.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GP1 X-ray 2.00 A/B 8-205 [» ]
    ProteinModelPortali P00435.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000005597.

    Protein family/group databases

    PeroxiBasei 3635. BtGPx01.

    Proteomic databases

    PaxDbi P00435.
    PRIDEi P00435.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 281209.
    KEGGi bta:281209.

    Organism-specific databases

    CTDi 2876.

    Phylogenomic databases

    eggNOGi COG0386.
    HOVERGENi HBG004333.
    InParanoidi P00435.
    KOi K00432.

    Miscellaneous databases

    EvolutionaryTracei P00435.
    NextBioi 20805264.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR000889. Glutathione_peroxidase.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    PANTHERi PTHR11592. PTHR11592. 1 hit.
    Pfami PF00255. GSHPx. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000303. Glutathion_perox. 1 hit.
    PRINTSi PR01011. GLUTPROXDASE.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS00460. GLUTATHIONE_PEROXID_1. 1 hit.
    PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
    PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Selenocysteine's mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases."
      Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Tainer J.A., Hallewell R.A.
      Protein Eng. 2:239-246(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pituitary.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Liver.
    3. "The amino-acid sequence of bovine glutathione peroxidase."
      Gunzler W.A., Steffens G.J., Grossmann A., Kim S.-M.A., Otting F., Wendel A., Flohe L.
      Hoppe-Seyler's Z. Physiol. Chem. 365:195-212(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 8-205.
      Tissue: Erythrocyte.
    4. "Identification of the site of non-enzymatic glycation of glutathione peroxidase: rationalization of the glycation-related catalytic alterations on the basis of three-dimensional protein structure."
      Baldwin J.S., Lee L., Leung T.K., Muruganandam A., Mutus B.
      Biochim. Biophys. Acta 1247:60-64(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCATION AT LYS-117, ABSENCE OF GLYCATION AT LYS-41; LYS-91; LYS-100; LYS-124; LYS-151; LYS-169.
    5. "The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution."
      Epp O., Ladenstein R., Wendel A.
      Eur. J. Biochem. 133:51-69(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiGPX1_BOVIN
    AccessioniPrimary (citable) accession number: P00435
    Secondary accession number(s): A6QPG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 120 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3