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Protein

Peroxiredoxin-5, mitochondrial

Gene

Prdx5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_308972. Detoxification of Reactive Oxygen Species.
REACT_360191. TP53 Regulates Metabolic Genes.

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 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1859821. Prdx5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • peroxisomal matrix Source: UniProtKB
  • peroxisome Source: MGI
Complete GO annotation...

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

BgeeiP99029.
CleanExiMM_PRDX5.
MM_PRDX6.
ExpressionAtlasiP99029. baseline and differential.
GenevisibleiP99029. MM.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi207718. 2 interactions.
IntActiP99029. 5 interactions.
MINTiMINT-1859227.
STRINGi10090.ENSMUSP00000025904.

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.
OMAiDLCAGKK.
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. AlignAdd to basket

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

        10         20         30         40         50
MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA
60 70 80 90 100
PIKVGDAIPS VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH
110 120 130 140 150
LPGFVEQAGA LKAKGAQVVA CLSVNDVFVI EEWGRAHQAE GKVRLLADPT
160 170 180 190 200
GAFGKATDLL LDDSLVSLFG NRRLKRFSMV IDNGIVKALN VEPDGTGLTC
210
SLAPNILSQL
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 (Ref. 7) Curated
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi207718. 2 interactions.
IntActiP99029. 5 interactions.
MINTiMINT-1859227.
STRINGi10090.ENSMUSP00000025904.

Protein family/group databases

PeroxiBasei4453. MmPrxV.

PTM databases

PhosphoSiteiP99029.

2D gel databases

REPRODUCTION-2DPAGEP99029.
SWISS-2DPAGEP99029.

Proteomic databases

MaxQBiP99029.
PaxDbiP99029.
PRIDEiP99029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi25824.
MGIiMGI:1859821. Prdx5.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_308972. Detoxification of Reactive Oxygen Species.
REACT_360191. TP53 Regulates Metabolic Genes.

Miscellaneous databases

NextBioi311536.
PROiP99029.
SOURCEiSearch...

Gene expression databases

BgeeiP99029.
CleanExiMM_PRDX5.
MM_PRDX6.
ExpressionAtlasiP99029. baseline and differential.
GenevisibleiP99029. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.