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Protein

Peroxiredoxin-5, mitochondrial

Gene

PRDX5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.3 Publications

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys Prx, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin.2 Publications

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei100Cysteine sulfenic acid (-SOH) intermediate2 Publications1

GO - Molecular functioni

  • antioxidant activity Source: UniProtKB
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  • peroxidase activity Source: UniProtKB
  • peroxiredoxin activity Source: UniProtKB
  • peroxynitrite reductase activity Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • RNA polymerase III regulatory region DNA binding Source: UniProtKB
  • thioredoxin peroxidase activity Source: Reactome

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular response to oxidative stress Source: Reactome
  • cellular response to reactive oxygen species Source: UniProtKB
  • hydrogen peroxide catabolic process Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • NADPH oxidation Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of oxidoreductase activity Source: UniProtKB
  • negative regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  • positive regulation of collagen biosynthetic process Source: UniProtKB
  • reactive nitrogen species metabolic process Source: UniProtKB
  • regulation of apoptosis involved in tissue homeostasis Source: UniProtKB
  • response to oxidative stress Source: UniProtKB

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
SIGNORiP30044.

Protein family/group databases

PeroxiBasei4448. HsPrxV.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-5, mitochondrial (EC:1.11.1.151 Publication)
Alternative name(s):
Alu corepressor 1
Antioxidant enzyme B166
Short name:
AOEB166
Liver tissue 2D-page spot 71B
PLP
Peroxiredoxin V
Short name:
Prx-V
Peroxisomal antioxidant enzyme
TPx type VI
Thioredoxin peroxidase PMP20
Gene namesi
Name:PRDX5
Synonyms:ACR1
ORF Names:SBBI10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000126432.13.
HGNCiHGNC:9355. PRDX5.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi100C → S: Complete loss of activity. 1 Publication1
Mutagenesisi125C → S: No change in activity. 1 Publication1
Mutagenesisi204C → S: Complete loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi25824.
OpenTargetsiENSG00000126432.
PharmGKBiPA33726.

Chemistry databases

ChEMBLiCHEMBL3627586.
DrugBankiDB00995. Auranofin.
DB03793. Benzoic Acid.
DB03608. Diminazene.

Polymorphism and mutation databases

BioMutaiPRDX5.
DMDMi317373539.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 52MitochondrionSequence analysisAdd BLAST52
ChainiPRO_000002379353 – 214Peroxiredoxin-5, mitochondrialAdd BLAST162

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei75N6-acetyllysineBy similarity1
Modified residuei83N6-acetyllysine; alternateCombined sources1
Modified residuei83N6-succinyllysine; alternateBy similarity1
Disulfide bondi100 ↔ 204Redox-activePROSITE-ProRule annotation2 Publications
Modified residuei116N6-succinyllysineBy similarity1
Modified residuei171PhosphoserineBy similarity1
Modified residuei182PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP30044.
MaxQBiP30044.
PaxDbiP30044.
PeptideAtlasiP30044.
PRIDEiP30044.
TopDownProteomicsiP30044-1. [P30044-1]
P30044-2. [P30044-2]

2D gel databases

OGPiP30044.
REPRODUCTION-2DPAGEiIPI00759663.
SWISS-2DPAGEiP30044.
UCD-2DPAGEiP30044.

PTM databases

iPTMnetiP30044.
PhosphoSitePlusiP30044.
SwissPalmiP30044.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000126432.
CleanExiHS_PRDX5.
GenevisibleiP30044. HS.

Organism-specific databases

HPAiCAB008661.
HPA037915.
HPA037916.

Interactioni

Subunit structurei

Monomer.1 Publication

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117352. 80 interactors.
IntActiP30044. 29 interactors.
MINTiMINT-5002532.
STRINGi9606.ENSP00000265462.

Structurei

Secondary structure

1214
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi66 – 68Combined sources3
Helixi72 – 74Combined sources3
Beta strandi75 – 77Combined sources3
Helixi78 – 81Combined sources4
Turni82 – 84Combined sources3
Beta strandi85 – 91Combined sources7
Helixi98 – 102Combined sources5
Helixi104 – 110Combined sources7
Helixi112 – 116Combined sources5
Turni117 – 119Combined sources3
Beta strandi122 – 129Combined sources8
Helixi131 – 140Combined sources10
Turni144 – 146Combined sources3
Beta strandi148 – 151Combined sources4
Helixi156 – 161Combined sources6
Helixi167 – 169Combined sources3
Helixi170 – 173Combined sources4
Beta strandi181 – 186Combined sources6
Beta strandi189 – 195Combined sources7
Beta strandi199 – 203Combined sources5
Helixi207 – 213Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H4OX-ray1.95A/B/C/D/E/F/G/H54-214[»]
1HD2X-ray1.50A54-214[»]
1OC3X-ray2.00A/B/C54-214[»]
1URMX-ray1.70A54-214[»]
2VL2X-ray1.92A/B/C54-214[»]
2VL3X-ray1.83A/B/C54-214[»]
2VL9X-ray2.70A/B/C/D54-214[»]
3MNGX-ray1.45A54-214[»]
4K7IX-ray2.25A/B/C54-214[»]
4K7NX-ray2.30A/B/C54-214[»]
4K7OX-ray1.98A/B/C54-214[»]
4MMMX-ray1.47A/C/E/G54-214[»]
ProteinModelPortaliP30044.
SMRiP30044.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30044.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini56 – 214ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi212 – 214Microbody targeting signal1 Publication3

Sequence similaritiesi

Belongs to the peroxiredoxin family. Prx5 subfamily.Curated

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0541. Eukaryota.
COG0678. LUCA.
GeneTreeiENSGT00390000018173.
HOGENOMiHOG000255884.
HOVERGENiHBG053675.
InParanoidiP30044.
KOiK11187.
OMAiQRYAMVV.
OrthoDBiEOG091G0OSA.
PhylomeDBiP30044.
TreeFamiTF105182.

Family and domain databases

InterProiView protein in InterPro
IPR013740. Redoxin.
IPR036249. Thioredoxin-like_sf.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF08534. Redoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform Mitochondrial (identifier: P30044-1) [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
MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS GGVRSFSRAA
60 70 80 90 100
AAMAPIKVGD AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC
110 120 130 140 150
SKTHLPGFVE QAEALKAKGV QVVACLSVND AFVTGEWGRA HKAEGKVRLL
160 170 180 190 200
ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR FSMVVQDGIV KALNVEPDGT
210
GLTCSLAPNI ISQL
Length:214
Mass (Da):22,086
Last modified:January 11, 2011 - v4
Checksum:iDA1DEB21120254EE
GO
Isoform Cytoplasmic+peroxisomal (identifier: P30044-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Show »
Length:162
Mass (Da):17,031
Checksum:i370DF621012F880D
GO
Isoform 3 (identifier: P30044-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     102-145: Missing.

Note: No experimental confirmation available.
Show »
Length:170
Mass (Da):17,454
Checksum:i29984B81B33F82C1
GO
Isoform 4 (identifier: P30044-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-145: Missing.

Note: Produced by alternative splicing.
Show »
Length:125
Mass (Da):12,897
Checksum:iF3A1C1531E4E4A73
GO

Sequence cautioni

The sequence AAF17200 differs from that shown. Reason: Frameshift at positions 14 and 30.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti141H → T in AAF04856 (PubMed:10679306).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02504933Y → C7 PublicationsCorresponds to variant dbSNP:rs7938623Ensembl.1
Natural variantiVAR_036406157F → L in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0188291 – 52Missing in isoform Cytoplasmic+peroxisomal. 4 PublicationsAdd BLAST52
Alternative sequenceiVSP_04668257 – 145Missing in isoform 4. 1 PublicationAdd BLAST89
Alternative sequenceiVSP_045783102 – 145Missing in isoform 3. 1 PublicationAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231705 mRNA. Translation: AAF78899.1.
AF124993 mRNA. Translation: AAF27531.1.
AF110731 mRNA. Translation: AAF03750.1.
AF197952 mRNA. Translation: AAF04856.1.
AJ249483 mRNA. Translation: CAB62210.1.
AF242525 mRNA. Translation: AAF99605.1.
AF112212 mRNA. Translation: AAF17200.1. Frameshift.
CR457203 mRNA. Translation: CAG33484.1.
DQ247769 Genomic DNA. Translation: ABB05181.1.
AP001453 Genomic DNA. No translation available.
AP003774 Genomic DNA. No translation available.
BC110983 mRNA. Translation: AAI10984.1.
BC113723 mRNA. Translation: AAI13724.1.
BC113725 mRNA. Translation: AAI13726.1.
BC143849 mRNA. Translation: AAI43850.1.
BC171733 mRNA. Translation: AAI71733.1.
CCDSiCCDS8069.1. [P30044-1]
CCDS8070.1. [P30044-3]
CCDS8071.1. [P30044-4]
RefSeqiNP_036226.1. NM_012094.4.
NP_857634.1. NM_181651.2.
NP_857635.1. NM_181652.2.
UniGeneiHs.502823.

Genome annotation databases

EnsembliENST00000265462; ENSP00000265462; ENSG00000126432. [P30044-1]
ENST00000347941; ENSP00000335363; ENSG00000126432. [P30044-4]
ENST00000352435; ENSP00000335334; ENSG00000126432. [P30044-3]
GeneIDi25824.
KEGGihsa:25824.
UCSCiuc001nzu.4. human. [P30044-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPRDX5_HUMAN
AccessioniPrimary (citable) accession number: P30044
Secondary accession number(s): A6NC19
, A6NG06, B7ZLJ4, B7ZVW3, Q14CK0, Q6IAF2, Q9UBU5, Q9UJU4, Q9UKX4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 11, 2011
Last modified: October 25, 2017
This is version 190 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families