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P22352

- GPX3_HUMAN

UniProt

P22352 - GPX3_HUMAN

Protein

Glutathione peroxidase 3

Gene

GPX3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.

    Catalytic activityi

    2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei73 – 731

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: UniProtKB
    2. selenium binding Source: UniProtKB
    3. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB
    2. protein homotetramerization Source: UniProtKB
    3. response to lipid hydroperoxide Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08224-MONOMER.
    ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

    Protein family/group databases

    PeroxiBasei3602. HsGPx03.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione peroxidase 3 (EC:1.11.1.9)
    Short name:
    GPx-3
    Short name:
    GSHPx-3
    Alternative name(s):
    Extracellular glutathione peroxidase
    Plasma glutathione peroxidase
    Short name:
    GPx-P
    Short name:
    GSHPx-P
    Gene namesi
    Name:GPX3
    Synonyms:GPXP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4555. GPX3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28951.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 226206Glutathione peroxidase 3PRO_0000013062Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    MaxQBiP22352.
    PaxDbiP22352.
    PRIDEiP22352.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00026199.
    SWISS-2DPAGEP22352.

    Expressioni

    Tissue specificityi

    Secreted in plasma.

    Gene expression databases

    ArrayExpressiP22352.
    BgeeiP22352.
    CleanExiHS_GPX3.
    GenevestigatoriP22352.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi109136. 1 interaction.
    IntActiP22352. 6 interactions.
    STRINGi9606.ENSP00000373477.

    Structurei

    Secondary structure

    1
    226
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 423
    Beta strandi44 – 474
    Beta strandi53 – 553
    Helixi56 – 594
    Beta strandi62 – 698
    Beta strandi71 – 733
    Turni74 – 774
    Helixi78 – 8912
    Helixi90 – 923
    Beta strandi94 – 1007
    Helixi112 – 1143
    Helixi115 – 1217
    Beta strandi131 – 1355
    Beta strandi140 – 1423
    Helixi147 – 1559
    Helixi166 – 1683
    Beta strandi185 – 1884
    Beta strandi194 – 1985
    Helixi204 – 22320

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R37X-ray1.85A/B25-223[»]
    ProteinModelPortaliP22352.
    SMRiP22352. Positions 36-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22352.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutathione peroxidase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0386.
    HOGENOMiHOG000277055.
    HOVERGENiHBG004333.
    InParanoidiP22352.
    KOiK00432.
    OMAiWYHRTTV.
    OrthoDBiEOG7KQ23C.
    PhylomeDBiP22352.
    TreeFamiTF105318.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22352-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARLLQASCL LSLLLAGFVS QSRGQEKSKM DCHGGISGTI YEYGALTIDG    50
    EEYIPFKQYA GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVILGFP 100
    CNQFGKQEPG ENSEILPTLK YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT 150
    FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR WNFEKFLVGP DGIPIMRWHH 200
    RTTVSNVKMD ILSYMRRQAA LGVKRK 226
    Length:226
    Mass (Da):25,552
    Last modified:February 26, 2008 - v2
    Checksum:iA839E87A5CDB51A9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281F → L.1 Publication
    Corresponds to variant rs8177445 [ dbSNP | Ensembl ].
    VAR_020943

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei73 – 731Selenocysteine1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00632 mRNA. Translation: BAA00525.1.
    X58295 mRNA. Translation: CAA41228.2.
    D16360 Genomic DNA. Translation: BAA03862.1.
    D16361 Genomic DNA. Translation: BAA03863.2.
    D16362 Genomic DNA. Translation: BAA03864.1.
    AF217787 mRNA. Translation: AAF43005.1.
    AY310878 Genomic DNA. Translation: AAP50261.1.
    AC008641 Genomic DNA. No translation available.
    BC013601 mRNA. Translation: AAH13601.1.
    BC035841 mRNA. Translation: AAH35841.1.
    BC050378 mRNA. Translation: AAH50378.2.
    CCDSiCCDS43389.1.
    PIRiI53822. JQ0476.
    RefSeqiNP_002075.2. NM_002084.3.
    UniGeneiHs.386793.

    Genome annotation databases

    EnsembliENST00000388825; ENSP00000373477; ENSG00000211445.
    GeneIDi2878.
    KEGGihsa:2878.
    UCSCiuc021yga.1. human.

    Polymorphism databases

    DMDMi172046796.

    Keywords - Coding sequence diversityi

    Polymorphism, Selenocysteine

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Glutathione peroxidase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00632 mRNA. Translation: BAA00525.1 .
    X58295 mRNA. Translation: CAA41228.2 .
    D16360 Genomic DNA. Translation: BAA03862.1 .
    D16361 Genomic DNA. Translation: BAA03863.2 .
    D16362 Genomic DNA. Translation: BAA03864.1 .
    AF217787 mRNA. Translation: AAF43005.1 .
    AY310878 Genomic DNA. Translation: AAP50261.1 .
    AC008641 Genomic DNA. No translation available.
    BC013601 mRNA. Translation: AAH13601.1 .
    BC035841 mRNA. Translation: AAH35841.1 .
    BC050378 mRNA. Translation: AAH50378.2 .
    CCDSi CCDS43389.1.
    PIRi I53822. JQ0476.
    RefSeqi NP_002075.2. NM_002084.3.
    UniGenei Hs.386793.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2R37 X-ray 1.85 A/B 25-223 [» ]
    ProteinModelPortali P22352.
    SMRi P22352. Positions 36-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109136. 1 interaction.
    IntActi P22352. 6 interactions.
    STRINGi 9606.ENSP00000373477.

    Chemistry

    DrugBanki DB00143. Glutathione.

    Protein family/group databases

    PeroxiBasei 3602. HsGPx03.

    Polymorphism databases

    DMDMi 172046796.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00026199.
    SWISS-2DPAGE P22352.

    Proteomic databases

    MaxQBi P22352.
    PaxDbi P22352.
    PRIDEi P22352.

    Protocols and materials databases

    DNASUi 2878.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000388825 ; ENSP00000373477 ; ENSG00000211445 .
    GeneIDi 2878.
    KEGGi hsa:2878.
    UCSCi uc021yga.1. human.

    Organism-specific databases

    CTDi 2878.
    GeneCardsi GC05P150381.
    H-InvDB HIX0024803.
    HGNCi HGNC:4555. GPX3.
    MIMi 138321. gene.
    neXtProti NX_P22352.
    PharmGKBi PA28951.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0386.
    HOGENOMi HOG000277055.
    HOVERGENi HBG004333.
    InParanoidi P22352.
    KOi K00432.
    OMAi WYHRTTV.
    OrthoDBi EOG7KQ23C.
    PhylomeDBi P22352.
    TreeFami TF105318.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08224-MONOMER.
    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi GPX3. human.
    EvolutionaryTracei P22352.
    GeneWikii GPX3.
    GenomeRNAii 2878.
    NextBioi 11363.
    PROi P22352.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22352.
    Bgeei P22352.
    CleanExi HS_GPX3.
    Genevestigatori P22352.

    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. "Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences."
      Takahashi K., Akasaka M., Yamamoto Y., Kobayashi C., Mizoguchi J., Koyama J.
      J. Biochem. 108:145-148(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Fetal liver and Placenta.
    2. "Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung, and breast in humans and rodents."
      Chu F.-F., Esworthy R.S., Doroshow J.H., Doan K., Liu X.F.
      Blood 79:3233-3238(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    3. Chu F.-F.
      Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 73.
    4. "The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32."
      Yoshimura S., Suemizu H., Taniguchi Y., Arimori K., Kawabe N., Moriuchi T.
      Gene 145:293-297(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Lymphocyte.
    5. "Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke."
      Comhair S.A.A., Thomassen M.J., Erzurum S.C.
      Am. J. Respir. Cell Mol. Biol. 23:350-354(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. NIEHS SNPs program
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-128.
    7. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Duodenum, Lung and Pancreas.
    9. "Characterization and partial amino acid sequence of human plasma glutathione peroxidase."
      Esworthy R.S., Chu F.-F., Paxton R.J., Akman S., Doroshow J.H.
      Arch. Biochem. Biophys. 286:330-336(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 107-138 AND 148-175, CHARACTERIZATION.
    10. "Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)."
      Structural genomics consortium (SGC)
      Submitted (SEP-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 25-223.

    Entry informationi

    Entry nameiGPX3_HUMAN
    AccessioniPrimary (citable) accession number: P22352
    Secondary accession number(s): O43787
    , Q86W78, Q9NZ74, Q9UEL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3