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P99029 (PRDX5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Prdx5
Synonyms:Prdx6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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' + H2O + 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
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNADPH oxidation

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide catabolic process

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of oxidoreductase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase III promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

reactive nitrogen species metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of apoptosis involved in tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

   Molecular_functionRNA polymerase III regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

antioxidant activity

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peroxynitrite reductase activity

Inferred from electronic annotation. Source: Ensembl

receptor binding

Inferred from sequence or structural similarity Ref.2. Source: UniProtKB

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

Modified residue701N6-acetyllysine; alternate Ref.10
Modified residue701N6-succinyllysine; alternate Ref.9
Modified residue711N6-acetyllysine Ref.10
Modified residue791N6-acetyllysine; alternate Ref.10
Modified residue791N6-succinyllysine; alternate Ref.9
Modified residue1121N6-succinyllysine Ref.9
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 »

FASTA16217,015

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] [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. 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] [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]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., 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS29507.1. [P99029-1]
PIRJC7239.
RefSeqNP_036151.1. NM_012021.2. [P99029-1]
UniGeneMm.279782.

3D structure databases

ProteinModelPortalP99029.
SMRP99029. Positions 50-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207718. 2 interactions.
IntActP99029. 4 interactions.
MINTMINT-1859227.

Protein family/group databases

PeroxiBase4453. MmPrxV.

PTM databases

PhosphoSiteP99029.

2D gel databases

REPRODUCTION-2DPAGEP99029.
SWISS-2DPAGEP99029.

Proteomic databases

MaxQBP99029.
PaxDbP99029.
PRIDEP99029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025904; ENSMUSP00000025904; ENSMUSG00000024953. [P99029-1]
GeneID54683.
KEGGmmu:54683.
UCSCuc008gjc.1. mouse. [P99029-1]

Organism-specific databases

CTD25824.
MGIMGI:1859821. Prdx5.

Phylogenomic databases

eggNOGCOG0678.
GeneTreeENSGT00390000018173.
HOGENOMHOG000255884.
HOVERGENHBG053675.
InParanoidP99029.
KOK11187.
OMAMSAWGKQ.
OrthoDBEOG77Q4XX.
PhylomeDBP99029.
TreeFamTF105182.

Gene expression databases

ArrayExpressP99029.
BgeeP99029.
CleanExMM_PRDX5.
MM_PRDX6.
GenevestigatorP99029.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio311536.
PROP99029.
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: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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