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Protein

Peroxiredoxin-5, mitochondrial

Gene

Prdx5

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei99 – 991Cysteine sulfenic acid (-SOH) intermediateSequence analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.

Protein family/group databases

PeroxiBasei4452. RnoPrxV.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-5, mitochondrial (EC:1.11.1.15)
Alternative name(s):
Antioxidant enzyme B166
Short name:
AOEB166
PLP
Peroxiredoxin V
Short name:
Prx-V
Peroxisomal antioxidant enzyme
Thioredoxin peroxidase PMP20
Thioredoxin reductase
Gene namesi
Name:Prdx5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71007. Prdx5.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: HGNC
  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5151MitochondrionSequence analysisAdd
BLAST
Chaini52 – 213162Peroxiredoxin-5, mitochondrialPRO_0000023799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysineBy similarity
Modified residuei82 – 821N6-acetyllysine; alternateBy similarity
Modified residuei82 – 821N6-succinyllysine; alternateBy similarity
Disulfide bondi99 ↔ 203Redox-activePROSITE-ProRule annotation
Modified residuei115 – 1151N6-succinyllysineBy similarity
Modified residuei170 – 1701PhosphoserineCombined sources
Modified residuei181 – 1811PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ9R063.
PRIDEiQ9R063.

PTM databases

iPTMnetiQ9R063.
PhosphoSiteiQ9R063.
SwissPalmiQ9R063.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi250207. 1 interaction.
IntActiQ9R063. 1 interaction.
STRINGi10116.ENSRNOP00000028687.

Structurei

3D structure databases

ProteinModelPortaliQ9R063.
SMRiQ9R063. Positions 53-213.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 213159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi211 – 2133Microbody 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

eggNOGiKOG0541. Eukaryota.
COG0678. LUCA.
HOGENOMiHOG000255884.
HOVERGENiHBG053675.
InParanoidiQ9R063.
KOiK11187.
OrthoDBiEOG77Q4XX.
PhylomeDBiQ9R063.
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: Q9R063-1) [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
MVQLRFCVLG SIAGSVLRAS ATWTCVAGRA GRKGAGWECG GARSFSSAAV
60 70 80 90 100
TMAPIKVGDT IPSVEVFEGE PGKKVNLAEL FKDKKGVLFG VPGAFTPGCS
110 120 130 140 150
KTHLPGFVEQ AGALKAKGAQ VVACLSVNDA FVTAEWGRAH QAEGKVQLLA
160 170 180 190 200
DPTGAFGKET DLLLDDSLVS LFGNRRLKRF SMVIDKGVVK ALNVEPDGTG
210
LTCSLAPNIL SQL
Length:213
Mass (Da):22,179
Last modified:May 1, 2000 - v1
Checksum:i9F0D03A4CC87708A
GO
Isoform Cytoplasmic+peroxisomal (identifier: Q9R063-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.

Show »
Length:162
Mass (Da):17,035
Checksum:i4230B34E574E2654
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681E → G.
Natural varianti114 – 1141L → P.
Natural varianti130 – 1301A → V.1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151Missing in isoform Cytoplasmic+peroxisomal. CuratedVSP_018832Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF110732 mRNA. Translation: AAF03751.1.
BC078771 mRNA. Translation: AAH78771.1.
RefSeqiNP_446062.1. NM_053610.1. [Q9R063-1]
UniGeneiRn.2944.

Genome annotation databases

GeneIDi113898.
KEGGirno:113898.
UCSCiRGD:71007. rat. [Q9R063-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF110732 mRNA. Translation: AAF03751.1.
BC078771 mRNA. Translation: AAH78771.1.
RefSeqiNP_446062.1. NM_053610.1. [Q9R063-1]
UniGeneiRn.2944.

3D structure databases

ProteinModelPortaliQ9R063.
SMRiQ9R063. Positions 53-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250207. 1 interaction.
IntActiQ9R063. 1 interaction.
STRINGi10116.ENSRNOP00000028687.

Protein family/group databases

PeroxiBasei4452. RnoPrxV.

PTM databases

iPTMnetiQ9R063.
PhosphoSiteiQ9R063.
SwissPalmiQ9R063.

Proteomic databases

PaxDbiQ9R063.
PRIDEiQ9R063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi113898.
KEGGirno:113898.
UCSCiRGD:71007. rat. [Q9R063-1]

Organism-specific databases

CTDi25824.
RGDi71007. Prdx5.

Phylogenomic databases

eggNOGiKOG0541. Eukaryota.
COG0678. LUCA.
HOGENOMiHOG000255884.
HOVERGENiHBG053675.
InParanoidiQ9R063.
KOiK11187.
OrthoDBiEOG77Q4XX.
PhylomeDBiQ9R063.
TreeFamiTF105182.

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.

Miscellaneous databases

NextBioi617974.
PROiQ9R063.

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. "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 [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "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], VARIANT VAL-130.
    Tissue: Heart.
  3. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 75-82; 86-115 AND 159-176, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPRDX5_RAT
AccessioniPrimary (citable) accession number: Q9R063
Secondary accession number(s): Q68G22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 114 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.