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Protein

Peroxiredoxin-4

Gene

Prdx4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei126 – 1261Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.

Protein family/group databases

PeroxiBasei4533. Rno2CysPrx04.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-4 (EC:1.11.1.15)
Alternative name(s):
Antioxidant enzyme AOE372
Peroxiredoxin IV
Short name:
Prx-IV
Thioredoxin peroxidase AO372
Thioredoxin-dependent peroxide reductase A0372
Gene namesi
Name:Prdx4
Synonyms:Rno2CysPrx04
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi620043. Prdx4.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • mitochondrion Source: Ensembl
  • nucleus Source: Ensembl
  • smooth endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4040By similarityAdd
BLAST
Chaini41 – 273233Peroxiredoxin-4PRO_0000390877Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-succinyllysineBy similarity
Disulfide bondi126 – 126Interchain (with C-248); in linked formBy similarity
Disulfide bondi247 – 247Interchain (with C-127); in linked formBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9Z0V5.
PRIDEiQ9Z0V5.

PTM databases

iPTMnetiQ9Z0V5.

Expressioni

Gene expression databases

GenevisibleiQ9Z0V5. RN.

Interactioni

Subunit structurei

Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation.By similarity

Protein-protein interaction databases

IntActiQ9Z0V5. 2 interactions.
STRINGi10116.ENSRNOP00000005014.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0V5.
SMRiQ9Z0V5. Positions 84-271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 239159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ9Z0V5.
KOiK03386.
OMAiYAGGHVY.
OrthoDBiEOG7T1RCD.
PhylomeDBiQ9Z0V5.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Z0V5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METWSKLLDG TTPSRRWRKL VLLLPPLLLF LLQTEALQGL ESDDRFRTRE
60 70 80 90 100
NECHFYAGGQ VYPGEVSRVS VADHSLHLSK AKISKPAPYW EGTAVINGEF
110 120 130 140 150
KELKLTDYRG KYLVFFFYPL DFTFVCPTEI IAFGDRIEEF KSINTEVVAC
160 170 180 190 200
SVDSQFTHLA WINTPRRQGG LGPIRIPLLS DLNHQISKDY GVYLEDSGHT
210 220 230 240 250
LRGLFIIDDK GVLRQITLND LPVGRSVDET LRLVQAFQYT DKHGEVCPAG
260 270
WKPGSETIIP DPAGKLKYFD KLN
Length:273
Mass (Da):31,007
Last modified:May 1, 1999 - v1
Checksum:i09E614794F1DC6C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106945 mRNA. Translation: AAD17993.1.
BC059122 mRNA. Translation: AAH59122.1.
RefSeqiNP_445964.1. NM_053512.2.
UniGeneiRn.17958.

Genome annotation databases

EnsembliENSRNOT00000005014; ENSRNOP00000005014; ENSRNOG00000003763.
GeneIDi85274.
KEGGirno:85274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106945 mRNA. Translation: AAD17993.1.
BC059122 mRNA. Translation: AAH59122.1.
RefSeqiNP_445964.1. NM_053512.2.
UniGeneiRn.17958.

3D structure databases

ProteinModelPortaliQ9Z0V5.
SMRiQ9Z0V5. Positions 84-271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z0V5. 2 interactions.
STRINGi10116.ENSRNOP00000005014.

Protein family/group databases

PeroxiBasei4533. Rno2CysPrx04.

PTM databases

iPTMnetiQ9Z0V5.

Proteomic databases

PaxDbiQ9Z0V5.
PRIDEiQ9Z0V5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005014; ENSRNOP00000005014; ENSRNOG00000003763.
GeneIDi85274.
KEGGirno:85274.

Organism-specific databases

CTDi10549.
RGDi620043. Prdx4.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ9Z0V5.
KOiK03386.
OMAiYAGGHVY.
OrthoDBiEOG7T1RCD.
PhylomeDBiQ9Z0V5.
TreeFamiTF105181.

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.

Miscellaneous databases

PROiQ9Z0V5.

Gene expression databases

GenevisibleiQ9Z0V5. RN.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member."
    Matsumoto A., Okado A., Fujii T., Fujii J., Egashira M., Niikawa N., Taniguchi N.
    FEBS Lett. 443:246-250(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Pituitary.
  3. "Peroxiredoxin IV is a secretable protein with heparin-binding properties under reduced conditions."
    Okado-Matsumoto A., Matsumoto A., Fujii J., Taniguchi N.
    J. Biochem. 127:493-501(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPRDX4_RAT
AccessioniPrimary (citable) accession number: Q9Z0V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is the redox-active Cys-126 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-247-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin (By similarity).By similarity
Irreversibly inactivated by overoxidation of Cys-126 (to Cys-SO3H) upon oxidative stress.By similarity

Keywords - Technical termi

Complete proteome, 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.