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O08807

- PRDX4_MOUSE

UniProt

O08807 - PRDX4_MOUSE

Protein

Peroxiredoxin-4

Gene

Prdx4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei127 – 1271Cysteine sulfenic acid (-SOH) intermediateBy similarity

    GO - Molecular functioni

    1. peroxidase activity Source: UniProtKB-KW
    2. peroxiredoxin activity Source: UniProtKB-EC
    3. protein homodimerization activity Source: MGI

    GO - Biological processi

    1. 4-hydroxyproline metabolic process Source: MGI
    2. cell redox homeostasis Source: MGI
    3. extracellular matrix organization Source: MGI
    4. male gonad development Source: MGI
    5. negative regulation of male germ cell proliferation Source: MGI
    6. oxidation-reduction process Source: MGI
    7. protein maturation by protein folding Source: MGI
    8. reactive oxygen species metabolic process Source: MGI
    9. spermatogenesis Source: MGI

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Protein family/group databases

    PeroxiBasei4532. Mm2CysPrx04.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin-4 (EC:1.11.1.15)
    Alternative name(s):
    Antioxidant enzyme AOE372
    Peroxiredoxin IV
    Short name:
    Prx-IV
    Thioredoxin peroxidase AO372
    Thioredoxin-dependent peroxide reductase A0372
    Gene namesi
    Name:Prdx4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1859815. Prdx4.

    Subcellular locationi

    Cytoplasm By similarity. Secreted By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: MGI
    3. endoplasmic reticulum Source: MGI
    4. extracellular space Source: Ensembl
    5. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4040By similarityAdd
    BLAST
    Chaini41 – 274234Peroxiredoxin-4PRO_0000135099Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi127 – 127Interchain (with C-248); in linked formBy similarity
    Disulfide bondi248 – 248Interchain (with C-127); in linked formBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO08807.
    PaxDbiO08807.
    PRIDEiO08807.

    2D gel databases

    REPRODUCTION-2DPAGEO08807.

    PTM databases

    PhosphoSiteiO08807.

    Expressioni

    Gene expression databases

    ArrayExpressiO08807.
    BgeeiO08807.
    CleanExiMM_PRDX4.
    GenevestigatoriO08807.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation.

    Protein-protein interaction databases

    BioGridi207303. 2 interactions.
    DIPiDIP-34137N.
    IntActiO08807. 5 interactions.
    MINTiMINT-1862981.
    STRINGi10090.ENSMUSP00000026328.

    Structurei

    Secondary structure

    1
    274
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi92 – 976
    Beta strandi100 – 1056
    Helixi106 – 1094
    Beta strandi112 – 1187
    Beta strandi122 – 1265
    Helixi129 – 1368
    Helixi138 – 1436
    Beta strandi146 – 1549
    Helixi156 – 1638
    Helixi167 – 1693
    Beta strandi179 – 1813
    Helixi186 – 1905
    Turni196 – 1994
    Beta strandi204 – 2085
    Beta strandi212 – 2198
    Helixi226 – 24419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VWUX-ray3.30A/B/C/D/E/F/G/H/I/J41-274[»]
    3VWVX-ray1.80A/B87-274[»]
    3W8JX-ray2.10C/D244-263[»]
    ProteinModelPortaliO08807.
    SMRiO08807. Positions 78-272.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini82 – 240159ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Redox-active center, Signal

    Phylogenomic databases

    eggNOGiCOG0450.
    GeneTreeiENSGT00390000004653.
    HOGENOMiHOG000022343.
    HOVERGENiHBG000286.
    InParanoidiB1AZS7.
    KOiK03386.
    OrthoDBiEOG7T1RCD.
    PhylomeDBiO08807.
    TreeFamiTF105181.

    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.

    O08807-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR    50
    ENECHFYAGG QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE 100
    FKELKLTDYR GKYLVFFFYP LDFTFVCPTE IIAFGDRIEE FKSINTEVVA 150
    CSVDSQFTHL AWINTPRRQG GLGPIRIPLL SDLNHQISKD YGVYLEDSGH 200
    TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY TDKHGEVCPA 250
    GWKPGSETII PDPAGKLKYF DKLN 274
    Length:274
    Mass (Da):31,053
    Last modified:July 1, 1997 - v1
    Checksum:i73DB5374EC46241C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96746 mRNA. Translation: AAB57846.1.
    AK005031 mRNA. Translation: BAB23758.1.
    AK146402 mRNA. Translation: BAE27143.1.
    AK152255 mRNA. Translation: BAE31074.1.
    BX005263 Genomic DNA. Translation: CAM23139.1.
    BC003349 mRNA. Translation: AAH03349.1.
    BC019578 mRNA. Translation: AAH19578.1.
    CCDSiCCDS30496.1.
    RefSeqiNP_058044.1. NM_016764.4.
    UniGeneiMm.247542.

    Genome annotation databases

    EnsembliENSMUST00000026328; ENSMUSP00000026328; ENSMUSG00000025289.
    GeneIDi53381.
    KEGGimmu:53381.
    UCSCiuc009uru.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96746 mRNA. Translation: AAB57846.1 .
    AK005031 mRNA. Translation: BAB23758.1 .
    AK146402 mRNA. Translation: BAE27143.1 .
    AK152255 mRNA. Translation: BAE31074.1 .
    BX005263 Genomic DNA. Translation: CAM23139.1 .
    BC003349 mRNA. Translation: AAH03349.1 .
    BC019578 mRNA. Translation: AAH19578.1 .
    CCDSi CCDS30496.1.
    RefSeqi NP_058044.1. NM_016764.4.
    UniGenei Mm.247542.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VWU X-ray 3.30 A/B/C/D/E/F/G/H/I/J 41-274 [» ]
    3VWV X-ray 1.80 A/B 87-274 [» ]
    3W8J X-ray 2.10 C/D 244-263 [» ]
    ProteinModelPortali O08807.
    SMRi O08807. Positions 78-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207303. 2 interactions.
    DIPi DIP-34137N.
    IntActi O08807. 5 interactions.
    MINTi MINT-1862981.
    STRINGi 10090.ENSMUSP00000026328.

    Protein family/group databases

    PeroxiBasei 4532. Mm2CysPrx04.

    PTM databases

    PhosphoSitei O08807.

    2D gel databases

    REPRODUCTION-2DPAGE O08807.

    Proteomic databases

    MaxQBi O08807.
    PaxDbi O08807.
    PRIDEi O08807.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026328 ; ENSMUSP00000026328 ; ENSMUSG00000025289 .
    GeneIDi 53381.
    KEGGi mmu:53381.
    UCSCi uc009uru.1. mouse.

    Organism-specific databases

    CTDi 10549.
    MGIi MGI:1859815. Prdx4.

    Phylogenomic databases

    eggNOGi COG0450.
    GeneTreei ENSGT00390000004653.
    HOGENOMi HOG000022343.
    HOVERGENi HBG000286.
    InParanoidi B1AZS7.
    KOi K03386.
    OrthoDBi EOG7T1RCD.
    PhylomeDBi O08807.
    TreeFami TF105181.

    Miscellaneous databases

    NextBioi 310209.
    PROi O08807.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08807.
    Bgeei O08807.
    CleanExi MM_PRDX4.
    Genevestigatori O08807.

    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. "Characterization of human and mouse peroxiredoxin IV: evidence for inhibition by Prx-IV of epidermal growth factor- and p53-induced reactive oxygen species."
      Wong C.M., Chun A.C., Kok K.H., Zhou Y., Fung P.C., Kung H.F., Jeang K.-T., Jin D.-Y.
      Antioxid. Redox Signal. 2:507-518(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and DBA/2.
      Tissue: Bone marrow and Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: C57BL/6J and NMRI.
      Tissue: Mammary gland and Mammary tumor.
    5. Lubec G., Kang S.U., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 190-203 AND 216-226.
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiPRDX4_MOUSE
    AccessioniPrimary (citable) accession number: O08807
    Secondary accession number(s): B1AZS7, Q3U8E4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 134 of the entry and version 1 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-127 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin By similarity.By similarity
    Irreversibly inactivated by overoxidation of Cys-127 (to Cys-SO3H) upon oxidative stress.By similarity

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3