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Q13162

- PRDX4_HUMAN

UniProt

Q13162 - PRDX4_HUMAN

Protein

Peroxiredoxin-4

Gene

PRDX4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei124 – 1241Cysteine sulfenic acid (-SOH) intermediateBy similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. thioredoxin peroxidase activity Source: ProtInc

    GO - Biological processi

    1. I-kappaB phosphorylation Source: ProtInc
    2. male gonad development Source: Ensembl
    3. negative regulation of male germ cell proliferation Source: Ensembl
    4. reactive oxygen species metabolic process Source: Ensembl
    5. spermatogenesis Source: Ensembl

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Protein family/group databases

    PeroxiBasei4530. Hs2CysPrx04.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin-4 (EC:1.11.1.15)
    Alternative name(s):
    Antioxidant enzyme AOE372
    Short name:
    AOE37-2
    Peroxiredoxin IV
    Short name:
    Prx-IV
    Thioredoxin peroxidase AO372
    Thioredoxin-dependent peroxide reductase A0372
    Gene namesi
    Name:PRDX4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:17169. PRDX4.

    Subcellular locationi

    Cytoplasm 1 Publication. Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrion Source: Ensembl
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33725.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 37371 PublicationAdd
    BLAST
    Chaini38 – 271234Peroxiredoxin-4PRO_0000135098Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi124 – 124Interchain (with C-245); in linked formBy similarity
    Disulfide bondi245 – 245Interchain (with C-124); in linked formBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ13162.
    PaxDbiQ13162.
    PeptideAtlasiQ13162.
    PRIDEiQ13162.

    2D gel databases

    OGPiQ13162.
    REPRODUCTION-2DPAGEIPI00011937.
    UCD-2DPAGEQ13162.

    PTM databases

    PhosphoSiteiQ13162.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13162.
    BgeeiQ13162.
    CleanExiHS_PRDX4.
    GenevestigatoriQ13162.

    Organism-specific databases

    HPAiCAB008659.
    CAB027389.
    CAB047362.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LBPP184284EBI-2211957,EBI-3927059
    P4HBP072372EBI-2211957,EBI-395883
    PDIA3P301012EBI-2211957,EBI-979862
    PDIA6Q150842EBI-2211957,EBI-1043087
    TBXA2RP217313EBI-2211957,EBI-2625082
    TXNDC5Q8NBS92EBI-2211957,EBI-2510815

    Protein-protein interaction databases

    BioGridi115800. 48 interactions.
    IntActiQ13162. 43 interactions.
    MINTiMINT-3027265.
    STRINGi9606.ENSP00000368646.

    Structurei

    Secondary structure

    1
    271
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi75 – 784
    Beta strandi89 – 946
    Beta strandi97 – 1026
    Helixi103 – 1064
    Beta strandi109 – 1157
    Helixi123 – 13311
    Helixi135 – 1395
    Turni140 – 1423
    Beta strandi143 – 1519
    Helixi153 – 1608
    Helixi164 – 1663
    Beta strandi176 – 1783
    Helixi183 – 1875
    Turni193 – 1953
    Beta strandi196 – 1983
    Beta strandi200 – 2056
    Beta strandi209 – 2179
    Helixi225 – 24117
    Turni260 – 2623
    Helixi263 – 2675
    Turni268 – 2703

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PN8X-ray1.80A/B/C/D/E/F/G/H/I/J84-271[»]
    3TJBX-ray2.38A/B/C/D/E38-271[»]
    3TJFX-ray2.04A/B/C/D/E38-271[»]
    3TJGX-ray2.24A/B/C/D/E38-271[»]
    3TJJX-ray1.91A/B/C/D/E38-271[»]
    3TJKX-ray2.09A/B/C/D/E38-271[»]
    3TKPX-ray2.49A/B/C/D/E38-271[»]
    3TKQX-ray2.22A/B/C/D/E38-271[»]
    3TKRX-ray2.10A/B/C/D/E/F/G/H/I/J38-271[»]
    3TKSX-ray2.40A/B/C/D/E38-271[»]
    ProteinModelPortaliQ13162.
    SMRiQ13162. Positions 74-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13162.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini79 – 237159ThioredoxinPROSITE-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.
    HOGENOMiHOG000022343.
    HOVERGENiHBG000286.
    InParanoidiQ13162.
    KOiK03386.
    OMAiHWEGTAV.
    PhylomeDBiQ13162.
    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.

    Q13162-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEALPLLAAT TPDHGRHRRL LLLPLLLFLL PAGAVQGWET EERPRTREEE    50
    CHFYAGGQVY PGEASRVSVA DHSLHLSKAK ISKPAPYWEG TAVIDGEFKE 100
    LKLTDYRGKY LVFFFYPLDF TFVCPTEIIA FGDRLEEFRS INTEVVACSV 150
    DSQFTHLAWI NTPRRQGGLG PIRIPLLSDL THQISKDYGV YLEDSGHTLR 200
    GLFIIDDKGI LRQITLNDLP VGRSVDETLR LVQAFQYTDK HGEVCPAGWK 250
    PGSETIIPDP AGKLKYFDKL N 271
    Length:271
    Mass (Da):30,540
    Last modified:November 1, 1996 - v1
    Checksum:i7E56B580049FC60F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121P → S in CAG46469. (PubMed:15489334)Curated
    Sequence conflicti51 – 511C → Y in CAG46469. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25182 mRNA. Translation: AAB95175.1.
    CR541668 mRNA. Translation: CAG46469.1.
    CR541705 mRNA. Translation: CAG46506.1.
    BC003609 mRNA. Translation: AAH03609.1.
    BC007107 mRNA. Translation: AAH07107.1.
    BC016770 mRNA. Translation: AAH16770.1.
    CCDSiCCDS14206.1.
    PIRiG01790.
    RefSeqiNP_006397.1. NM_006406.1.
    UniGeneiHs.83383.

    Genome annotation databases

    EnsembliENST00000379341; ENSP00000368646; ENSG00000123131.
    GeneIDi10549.
    KEGGihsa:10549.
    UCSCiuc004dam.3. human.

    Polymorphism databases

    DMDMi3024727.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25182 mRNA. Translation: AAB95175.1 .
    CR541668 mRNA. Translation: CAG46469.1 .
    CR541705 mRNA. Translation: CAG46506.1 .
    BC003609 mRNA. Translation: AAH03609.1 .
    BC007107 mRNA. Translation: AAH07107.1 .
    BC016770 mRNA. Translation: AAH16770.1 .
    CCDSi CCDS14206.1.
    PIRi G01790.
    RefSeqi NP_006397.1. NM_006406.1.
    UniGenei Hs.83383.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PN8 X-ray 1.80 A/B/C/D/E/F/G/H/I/J 84-271 [» ]
    3TJB X-ray 2.38 A/B/C/D/E 38-271 [» ]
    3TJF X-ray 2.04 A/B/C/D/E 38-271 [» ]
    3TJG X-ray 2.24 A/B/C/D/E 38-271 [» ]
    3TJJ X-ray 1.91 A/B/C/D/E 38-271 [» ]
    3TJK X-ray 2.09 A/B/C/D/E 38-271 [» ]
    3TKP X-ray 2.49 A/B/C/D/E 38-271 [» ]
    3TKQ X-ray 2.22 A/B/C/D/E 38-271 [» ]
    3TKR X-ray 2.10 A/B/C/D/E/F/G/H/I/J 38-271 [» ]
    3TKS X-ray 2.40 A/B/C/D/E 38-271 [» ]
    ProteinModelPortali Q13162.
    SMRi Q13162. Positions 74-269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115800. 48 interactions.
    IntActi Q13162. 43 interactions.
    MINTi MINT-3027265.
    STRINGi 9606.ENSP00000368646.

    Protein family/group databases

    PeroxiBasei 4530. Hs2CysPrx04.

    PTM databases

    PhosphoSitei Q13162.

    Polymorphism databases

    DMDMi 3024727.

    2D gel databases

    OGPi Q13162.
    REPRODUCTION-2DPAGE IPI00011937.
    UCD-2DPAGE Q13162.

    Proteomic databases

    MaxQBi Q13162.
    PaxDbi Q13162.
    PeptideAtlasi Q13162.
    PRIDEi Q13162.

    Protocols and materials databases

    DNASUi 10549.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379341 ; ENSP00000368646 ; ENSG00000123131 .
    GeneIDi 10549.
    KEGGi hsa:10549.
    UCSCi uc004dam.3. human.

    Organism-specific databases

    CTDi 10549.
    GeneCardsi GC0XP023592.
    HGNCi HGNC:17169. PRDX4.
    HPAi CAB008659.
    CAB027389.
    CAB047362.
    MIMi 606506. gene.
    neXtProti NX_Q13162.
    PharmGKBi PA33725.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0450.
    HOGENOMi HOG000022343.
    HOVERGENi HBG000286.
    InParanoidi Q13162.
    KOi K03386.
    OMAi HWEGTAV.
    PhylomeDBi Q13162.
    TreeFami TF105181.

    Miscellaneous databases

    EvolutionaryTracei Q13162.
    GeneWikii PRDX4.
    GenomeRNAii 10549.
    NextBioi 40013.
    PROi Q13162.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13162.
    Bgeei Q13162.
    CleanExi HS_PRDX4.
    Genevestigatori Q13162.

    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. "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation."
      Jin D.-Y., Chae H.Z., Rhee S.G., Jeang K.-T.
      J. Biol. Chem. 272:30952-30961(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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: Brain.
    4. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
      Xu G., Shin S.B., Jaffrey S.R.
      Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 38-46.
      Tissue: Leukemic T-cell.
    5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 46-66; 81-99; 140-164; 174-208; 213-223 AND 231-263, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    6. "A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress."
      Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
      Biochem. J. 366:777-785(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: OVEROXIDATION AT CYS-124.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPRDX4_HUMAN
    AccessioniPrimary (citable) accession number: Q13162
    Secondary accession number(s): Q6FHT3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 145 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

    Miscellaneous

    The active site is the redox-active Cys-124 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-245-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.
    Irreversibly inactivated by overoxidation of Cys-124 (to Cys-SO3H) upon oxidative stress.

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3