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Reviewed, UniProtKB/Swiss-Prot P99029 (PRDX5_MOUSE)

Last modified November 25, 2008. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxiredoxin-5, mitochondrial
    EC=1.11.1.15
Alternative name(s):
    Prx-V
    Peroxisomal antioxidant enzyme
    PLP
    Thioredoxin reductase
    Thioredoxin peroxidase PMP20
    Antioxidant enzyme B166
      Short name=AOEB166
    Liver tissue 2D-page spot 2D-0014IV
Gene names
Name: Prdx5
Synonyms: Prdx6
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.

Subunit structure

Monomer.

Subcellular location

Mitochondrion. Cytoplasm. Peroxisome.

Tissue specificity

Widely expressed.

Sequence similarities

Belongs to the peroxiredoxin 2 family.

Contains 1 thioredoxin domain.

Ontologies

Keywords

   Cellular componentCytoplasm
Mitochondrion
Peroxisome
   Coding sequence diversityAlternative initiation
   DomainRedox-active center
Transit peptide
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

peroxisome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: P99029-1)

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.
Isoform Cytoplasmic+peroxisomal (identifier: P99029-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4848Mitochondrion Potential
Chain49 – 210162Peroxiredoxin-5, mitochondrial
PRO_0000023795

Regions

Domain52 – 210159Thioredoxin
Motif208 – 2103Microbody targeting signal By similarity

Sites

Active site961Cysteine sulfenic acid (-SOH) intermediate Potential

Amino acid modifications

Disulfide bond96 ↔ 200Redox-active By similarity

Natural variations

Alternative sequence1 – 4848Missing in isoform Cytoplasmic+peroxisomal.
VSP_018830

Experimental info

Sequence conflict551G → D AA sequence Ref.7
Sequence conflict83 – 10220GVLFG…KTHLP → VFCLESLGHLHLAVLRPTA in AAF21016. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial [UniParc].

Last modified February 21, 2002. Version 2.
Checksum: E944104CC468BDD8

FASTA21021,897
        10         20         30         40         50         60 
MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA PIKVGDAIPS 

        70         80         90        100        110        120 
VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH LPGFVEQAGA LKAKGAQVVA 

       130        140        150        160        170        180 
CLSVNDVFVI EEWGRAHQAE GKVRLLADPT GAFGKATDLL LDDSLVSLFG NRRLKRFSMV 

       190        200        210 
IDNGIVKALN VEPDGTGLTC SLAPNILSQL 

« Hide

Isoform Cytoplasmic+peroxisomal [UniParc].

Checksum: EE32FFB439418B21
Show »

16217,015

References

« Hide 'large scale' references
[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: 10679306] [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: 10514471] [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: 10521424] [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: 10753630] [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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[7]Sanchez J.-C., Rouge V., Frutiger S., Hughes G.J., Yan J.X., Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.
Submitted (AUG-1998) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 50-61.
Tissue: Liver.
[8]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 72-79 AND 145-155, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[9]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 83-112 AND 156-172, MASS SPECTROMETRY.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
PIRJC7239.
RefSeqNP_036151.1.
UniGeneMm.279782

3D structure databases

HSSPHSSP built from PDB template 1HD2 based on UniProtKB P30044.
SMRP99029. Positions 50-210.
ModBaseSearch...

Protein family/group databases

PeroxiBase4453. MmPrxV.

PTM databases

PhosphoSiteP99029.

2-D gel databases

SWISS-2DPAGEP99029.
REPRODUCTION-2DPAGEP99029.

Genome annotation databases

EnsemblENSMUSG00000024953. Mus musculus. [Contig view]
GeneID54683.
KEGGmmu:54683.

Organism-specific databases

MGIMGI:1859821. Prdx5.

Phylogenomic databases

HOGENOMP99029.
HOVERGENP99029.

Gene expression databases

ArrayExpressP99029.
CleanExMM_PRDX5.
MM_PRDX6.
GermOnlineENSMUSG00000024953. Mus musculus.

Family and domain databases

InterProIPR013740. Redoxin.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio311536.
SOURCESearch...

Entry information

Entry namePRDX5_MOUSE
AccessionPrimary (citable) accession number: P99029
Secondary accession number(s): Q9QX45, Q9QZ75
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 21, 2002
Last modified: November 25, 2008
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents