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O75715

- GPX5_HUMAN

UniProt

O75715 - GPX5_HUMAN

Protein

Epididymal secretory glutathione peroxidase

Gene

GPX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.

    Catalytic activityi

    2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

    Sites

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

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipid metabolic process Source: ProtInc
    2. response to oxidative stress Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Protein family/group databases

    PeroxiBasei3604. HsGPx05-A.
    3629. HsGPx05-B.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epididymal secretory glutathione peroxidase (EC:1.11.1.9)
    Alternative name(s):
    Epididymis-specific glutathione peroxidase-like protein
    Short name:
    EGLP
    Glutathione peroxidase 5
    Short name:
    GPx-5
    Short name:
    GSHPx-5
    Gene namesi
    Name:GPX5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4557. GPX5.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28953.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 221200Epididymal secretory glutathione peroxidasePRO_0000013076Add
    BLAST

    Proteomic databases

    PaxDbiO75715.
    PRIDEiO75715.

    Expressioni

    Tissue specificityi

    Epididymis.

    Gene expression databases

    ArrayExpressiO75715.
    BgeeiO75715.
    CleanExiHS_GPX5.
    GenevestigatoriO75715.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000392398.

    Structurei

    Secondary structure

    1
    221
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 423
    Beta strandi44 – 518
    Beta strandi53 – 553
    Helixi56 – 594
    Beta strandi62 – 698
    Beta strandi71 – 733
    Helixi74 – 785
    Helixi79 – 8911
    Helixi90 – 923
    Beta strandi94 – 1007
    Helixi112 – 1143
    Helixi115 – 1217
    Beta strandi131 – 1355
    Beta strandi140 – 1423
    Helixi147 – 1559
    Turni166 – 1683
    Beta strandi171 – 1733
    Beta strandi185 – 1884
    Beta strandi194 – 1985
    Helixi204 – 21411
    Helixi215 – 2173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I3YX-ray2.00A28-220[»]
    ProteinModelPortaliO75715.
    SMRiO75715. Positions 31-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75715.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutathione peroxidase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0386.
    HOGENOMiHOG000115921.
    HOVERGENiHBG004333.
    InParanoidiO75715.
    KOiK00432.
    OMAiIAEFCTI.
    OrthoDBiEOG7KQ23C.
    PhylomeDBiO75715.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75715-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTTQLRVVHL LPLLLACFVQ TSPKQEKMKM DCHKDEKGTI YDYEAIALNK    50
    NEYVSFKQYV GKHILFVNVA TYCGLTAQYP ELNALQEELK PYGLVVLGFP 100
    CNQFGKQEPG DNKEILPGLK YVRPGGGFVP SFQLFEKGDV NGEKEQKVFS 150
    FLKHSCPHPS EILGTFKSIS WDPVKVHDIR WNFEKFLVGP DGIPVMRWSH 200
    RATVSSVKTD ILAYLKQFKT K 221
    Length:221
    Mass (Da):25,202
    Last modified:November 1, 1998 - v1
    Checksum:iCE3E7BFD53CE979F
    GO
    Isoform 2 (identifier: O75715-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         81-221: ELNALQEELK...LAYLKQFKTK → GMSVQGEDLYLVSSFLRKGM

    Note: No experimental confirmation available.

    Show »
    Length:100
    Mass (Da):11,429
    Checksum:i04BFE67B6E77684F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851L → P.
    Corresponds to variant rs58554303 [ dbSNP | Ensembl ].
    VAR_061206
    Natural varianti85 – 851L → V.1 Publication
    Corresponds to variant rs769188 [ dbSNP | Ensembl ].
    VAR_012040

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei81 – 221141ELNAL…QFKTK → GMSVQGEDLYLVSSFLRKGM in isoform 2. 1 PublicationVSP_043046Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005277 mRNA. Translation: CAA06463.1.
    AY882013 Genomic DNA. Translation: AAW56939.1.
    AL049543 Genomic DNA. Translation: CAB71121.1.
    CH471081 Genomic DNA. Translation: EAX03168.1.
    BC128159 mRNA. Translation: AAI28160.1.
    BC128160 mRNA. Translation: AAI28161.1.
    CCDSiCCDS4652.1. [O75715-1]
    CCDS4653.1. [O75715-2]
    RefSeqiNP_001500.1. NM_001509.2. [O75715-1]
    NP_003987.2. NM_003996.3. [O75715-2]
    UniGeneiHs.248129.

    Genome annotation databases

    EnsembliENST00000412168; ENSP00000392398; ENSG00000224586. [O75715-1]
    ENST00000469384; ENSP00000419935; ENSG00000224586. [O75715-2]
    GeneIDi2880.
    KEGGihsa:2880.
    UCSCiuc003nll.2. human. [O75715-1]
    uc003nlm.2. human. [O75715-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005277 mRNA. Translation: CAA06463.1 .
    AY882013 Genomic DNA. Translation: AAW56939.1 .
    AL049543 Genomic DNA. Translation: CAB71121.1 .
    CH471081 Genomic DNA. Translation: EAX03168.1 .
    BC128159 mRNA. Translation: AAI28160.1 .
    BC128160 mRNA. Translation: AAI28161.1 .
    CCDSi CCDS4652.1. [O75715-1 ]
    CCDS4653.1. [O75715-2 ]
    RefSeqi NP_001500.1. NM_001509.2. [O75715-1 ]
    NP_003987.2. NM_003996.3. [O75715-2 ]
    UniGenei Hs.248129.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I3Y X-ray 2.00 A 28-220 [» ]
    ProteinModelPortali O75715.
    SMRi O75715. Positions 31-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000392398.

    Chemistry

    DrugBanki DB00143. Glutathione.

    Protein family/group databases

    PeroxiBasei 3604. HsGPx05-A.
    3629. HsGPx05-B.

    Proteomic databases

    PaxDbi O75715.
    PRIDEi O75715.

    Protocols and materials databases

    DNASUi 2880.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000412168 ; ENSP00000392398 ; ENSG00000224586 . [O75715-1 ]
    ENST00000469384 ; ENSP00000419935 ; ENSG00000224586 . [O75715-2 ]
    GeneIDi 2880.
    KEGGi hsa:2880.
    UCSCi uc003nll.2. human. [O75715-1 ]
    uc003nlm.2. human. [O75715-2 ]

    Organism-specific databases

    CTDi 2880.
    GeneCardsi GC06P028493.
    HGNCi HGNC:4557. GPX5.
    MIMi 603435. gene.
    neXtProti NX_O75715.
    PharmGKBi PA28953.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0386.
    HOGENOMi HOG000115921.
    HOVERGENi HBG004333.
    InParanoidi O75715.
    KOi K00432.
    OMAi IAEFCTI.
    OrthoDBi EOG7KQ23C.
    PhylomeDBi O75715.
    TreeFami TF105318.

    Miscellaneous databases

    EvolutionaryTracei O75715.
    GeneWikii GPX5.
    GenomeRNAii 2880.
    NextBioi 11375.
    PROi O75715.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75715.
    Bgeei O75715.
    CleanExi HS_GPX5.
    Genevestigatori O75715.

    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. "The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract."
      Hall L., Williams K., Perry A.C.F., Frayne J., Jury J.A.
      Biochem. J. 333:5-9(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Epididymis.
    2. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-85.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2).
    6. "Crystal structure of human glutathione peroxidase 5."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-220.

    Entry informationi

    Entry nameiGPX5_HUMAN
    AccessioniPrimary (citable) accession number: O75715
    Secondary accession number(s): A1A4Y0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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