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)

P99029

- PRDX5_MOUSE

UniProt

P99029 - PRDX5_MOUSE

Protein

Peroxiredoxin-5, mitochondrial

Gene

Prdx5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (21 Feb 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei96 – 961Cysteine sulfenic acid (-SOH) intermediateSequence Analysis

    GO - Molecular functioni

    1. antioxidant activity Source: UniProtKB
    2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: Ensembl
    3. peroxidase activity Source: UniProtKB-KW
    4. peroxynitrite reductase activity Source: Ensembl
    5. receptor binding Source: UniProtKB
    6. RNA polymerase III regulatory region DNA binding Source: Ensembl

    GO - Biological processi

    1. hydrogen peroxide catabolic process Source: UniProtKB
    2. NADPH oxidation Source: Ensembl
    3. negative regulation of apoptotic process Source: Ensembl
    4. negative regulation of oxidoreductase activity Source: Ensembl
    5. negative regulation of transcription from RNA polymerase III promoter Source: Ensembl
    6. positive regulation of collagen biosynthetic process Source: Ensembl
    7. reactive nitrogen species metabolic process Source: Ensembl
    8. regulation of apoptosis involved in tissue homeostasis Source: Ensembl
    9. response to oxidative stress Source: UniProtKB

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

    Protein family/group databases

    PeroxiBasei4453. MmPrxV.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin-5, mitochondrial (EC:1.11.1.15)
    Alternative name(s):
    Antioxidant enzyme B166
    Short name:
    AOEB166
    Liver tissue 2D-page spot 2D-0014IV
    PLP
    Peroxiredoxin V
    Short name:
    Prx-V
    Peroxisomal antioxidant enzyme
    Thioredoxin peroxidase PMP20
    Thioredoxin reductase
    Gene namesi
    Name:Prdx5
    Synonyms:Prdx6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1859821. Prdx5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle Source: Ensembl
    3. cytosol Source: Ensembl
    4. mitochondrion Source: MGI
    5. nucleus Source: Ensembl
    6. perinuclear region of cytoplasm Source: Ensembl
    7. peroxisomal matrix Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4848MitochondrionSequence AnalysisAdd
    BLAST
    Chaini49 – 210162Peroxiredoxin-5, mitochondrialPRO_0000023795Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701N6-acetyllysine; alternate1 Publication
    Modified residuei70 – 701N6-succinyllysine; alternate1 Publication
    Modified residuei71 – 711N6-acetyllysine1 Publication
    Modified residuei79 – 791N6-acetyllysine; alternate1 Publication
    Modified residuei79 – 791N6-succinyllysine; alternate1 Publication
    Disulfide bondi96 ↔ 200Redox-activePROSITE-ProRule annotation
    Modified residuei112 – 1121N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP99029.
    PaxDbiP99029.
    PRIDEiP99029.

    2D gel databases

    REPRODUCTION-2DPAGEP99029.
    SWISS-2DPAGEP99029.

    PTM databases

    PhosphoSiteiP99029.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiP99029.
    BgeeiP99029.
    CleanExiMM_PRDX5.
    MM_PRDX6.
    GenevestigatoriP99029.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi207718. 2 interactions.
    IntActiP99029. 4 interactions.
    MINTiMINT-1859227.

    Structurei

    3D structure databases

    ProteinModelPortaliP99029.
    SMRiP99029. Positions 50-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini52 – 210159ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi208 – 2103Microbody targeting signalBy similarity

    Sequence similaritiesi

    Belongs to the peroxiredoxin 2 family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0678.
    GeneTreeiENSGT00390000018173.
    HOGENOMiHOG000255884.
    HOVERGENiHBG053675.
    InParanoidiP99029.
    KOiK11187.
    OMAiMSAWGKQ.
    OrthoDBiEOG77Q4XX.
    PhylomeDBiP99029.
    TreeFamiTF105182.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR013740. Redoxin.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF08534. Redoxin. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS51352. THIOREDOXIN_2. 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 initiation. Align

    Isoform Mitochondrial (identifier: P99029-1) [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

    MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA    50
    PIKVGDAIPS VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH 100
    LPGFVEQAGA LKAKGAQVVA CLSVNDVFVI EEWGRAHQAE GKVRLLADPT 150
    GAFGKATDLL LDDSLVSLFG NRRLKRFSMV IDNGIVKALN VEPDGTGLTC 200
    SLAPNILSQL 210
    Length:210
    Mass (Da):21,897
    Last modified:February 21, 2002 - v2
    Checksum:iE944104CC468BDD8
    GO
    Isoform Cytoplasmic+peroxisomal (identifier: P99029-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: Missing.

    Show »
    Length:162
    Mass (Da):17,015
    Checksum:iEE32FFB439418B21
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551G → D AA sequence 1 PublicationCurated
    Sequence conflicti83 – 10220GVLFG…KTHLP → VFCLESLGHLHLAVLRPTA in AAF21016. (PubMed:10753630)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4848Missing in isoform Cytoplasmic+peroxisomal. CuratedVSP_018830Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197951 mRNA. Translation: AAF04855.1.
    AF124994 mRNA. Translation: AAF27532.1.
    AF110733 mRNA. Translation: AAG13450.1.
    AF208730, AF208729 Genomic DNA. Translation: AAF21016.1.
    AK002383 mRNA. Translation: BAB22058.1.
    AK003332 mRNA. Translation: BAB22720.1.
    BC008174 mRNA. Translation: AAH08174.1.
    CCDSiCCDS29507.1. [P99029-1]
    PIRiJC7239.
    RefSeqiNP_036151.1. NM_012021.2. [P99029-1]
    UniGeneiMm.279782.

    Genome annotation databases

    EnsembliENSMUST00000025904; ENSMUSP00000025904; ENSMUSG00000024953. [P99029-1]
    GeneIDi54683.
    KEGGimmu:54683.
    UCSCiuc008gjc.1. mouse. [P99029-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197951 mRNA. Translation: AAF04855.1 .
    AF124994 mRNA. Translation: AAF27532.1 .
    AF110733 mRNA. Translation: AAG13450.1 .
    AF208730 , AF208729 Genomic DNA. Translation: AAF21016.1 .
    AK002383 mRNA. Translation: BAB22058.1 .
    AK003332 mRNA. Translation: BAB22720.1 .
    BC008174 mRNA. Translation: AAH08174.1 .
    CCDSi CCDS29507.1. [P99029-1 ]
    PIRi JC7239.
    RefSeqi NP_036151.1. NM_012021.2. [P99029-1 ]
    UniGenei Mm.279782.

    3D structure databases

    ProteinModelPortali P99029.
    SMRi P99029. Positions 50-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207718. 2 interactions.
    IntActi P99029. 4 interactions.
    MINTi MINT-1859227.

    Protein family/group databases

    PeroxiBasei 4453. MmPrxV.

    PTM databases

    PhosphoSitei P99029.

    2D gel databases

    REPRODUCTION-2DPAGE P99029.
    SWISS-2DPAGE P99029.

    Proteomic databases

    MaxQBi P99029.
    PaxDbi P99029.
    PRIDEi P99029.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025904 ; ENSMUSP00000025904 ; ENSMUSG00000024953 . [P99029-1 ]
    GeneIDi 54683.
    KEGGi mmu:54683.
    UCSCi uc008gjc.1. mouse. [P99029-1 ]

    Organism-specific databases

    CTDi 25824.
    MGIi MGI:1859821. Prdx5.

    Phylogenomic databases

    eggNOGi COG0678.
    GeneTreei ENSGT00390000018173.
    HOGENOMi HOG000255884.
    HOVERGENi HBG053675.
    InParanoidi P99029.
    KOi K11187.
    OMAi MSAWGKQ.
    OrthoDBi EOG77Q4XX.
    PhylomeDBi P99029.
    TreeFami TF105182.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    NextBioi 311536.
    PROi P99029.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P99029.
    Bgeei P99029.
    CleanExi MM_PRDX5.
    MM_PRDX6.
    Genevestigatori P99029.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR013740. Redoxin.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF08534. Redoxin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis."
      Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., Fung P.C.W., Kung H.-F., Jin D.-Y.
      Biochem. Biophys. Res. Commun. 268:921-927(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    2. "Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro."
      Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., Subramani S., Rogers R.A., Avraham H.
      J. Biol. Chem. 274:29897-29904(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    3. "Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family."
      Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., Duconseille E., Falmagne P., Bernard A.
      J. Biol. Chem. 274:30451-30458(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, CHARACTERIZATION.
      Strain: C3H/HeJ.
      Tissue: Lung.
    4. "Molecular cloning and characterization of the mouse Peroxiredoxin V gene."
      Lee T.H., Kim S.J., Kang S.W., Lee K.K., Rhee S.G., Yu D.Y.
      Biochem. Biophys. Res. Commun. 270:356-362(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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.
      Tissue: Kidney.
    6. "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: Mammary tumor.
    7. Cited for: PROTEIN SEQUENCE OF 50-61.
      Tissue: Liver.
    8. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 72-79; 83-112 AND 145-172, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-79 AND LYS-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-71 AND LYS-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiPRDX5_MOUSE
    AccessioniPrimary (citable) accession number: P99029
    Secondary accession number(s): Q9QX45, Q9QZ75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: February 21, 2002
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3