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Q949U7 (PRX2E_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxiredoxin-2E, chloroplastic

EC=1.11.1.15
Alternative name(s):
Peroxiredoxin IIE
Thioredoxin reductase 2E
Gene names
Name:PRXIIE
Ordered Locus Names:At3g52960
ORF Names:F8J2_130
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length234 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 or glutaredoxin system. May be involved in chloroplast redox homeostasis.

Catalytic activity

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

Subunit structure

Monomer. Ref.5

Subcellular location

Plastidchloroplast stroma Ref.5.

Tissue specificity

Expressed in all tissues but predominantly in buds, siliques and seeds. Ref.4 Ref.5

Induction

Down-regulated by salt stress. Ref.4

Post-translational modification

The Cys-121-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-121 (probably Cys-SOH) rapidly reacts with Cys-146-SH to form an intramolecular disulfide. This disulfide is subsequently reduced by thioredoxin to restore the reduced active form of the enzyme.

Sequence similarities

Belongs to the peroxiredoxin 2 family.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7070Chloroplast Potential
Chain71 – 234164Peroxiredoxin-2E, chloroplastic
PRO_0000282281

Regions

Domain73 – 234162Thioredoxin

Sites

Active site1211Cysteine sulfenic acid (-SOH) intermediate Potential

Amino acid modifications

Disulfide bond121 ↔ 146Redox-active

Experimental info

Sequence conflict1331A → V in AAK92817. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q949U7 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 4F66DA63CD15F003

FASTA23424,684
        10         20         30         40         50         60 
MATSLSVSRF MSSSATVISV AKPLLSPTVS FTAPLSFTRS LAPNLSLKFR NRRTNSASAT 

        70         80         90        100        110        120 
TRSFATTPVT ASISVGDKLP DSTLSYLDPS TGDVKTVTVS SLTAGKKTIL FAVPGAFTPT 

       130        140        150        160        170        180 
CSQKHVPGFV SKAGELRSKG IDVIACISVN DAFVMEAWRK DLGINDEVML LSDGNGEFTG 

       190        200        210        220        230 
KLGVELDLRD KPVGLGVRSR RYAILADDGV VKVLNLEEGG AFTNSSAEDM LKAL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Type II peroxiredoxin C, a member of the peroxiredoxin family of Arabidopsis thaliana: its expression and activity in comparison with other peroxiredoxins."
Horling F., Koenig J., Dietz K.-J.
Plant Physiol. Biochem. 40:491-499(2002)
Cited for: TISSUE SPECIFICITY, INDUCTION.
[5]"Resemblance and dissemblance of Arabidopsis type II peroxiredoxins: similar sequences for divergent gene expression, protein localization, and activity."
Brehelin C., Meyer E.H., de Souris J.-P., Bonnard G., Meyer Y.
Plant Physiol. 132:2045-2057(2003) [PubMed: 12913160] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"The plant multigenic family of thiol peroxidases."
Rouhier N., Jacquot J.-P.
Free Radic. Biol. Med. 38:1413-1421(2005) [PubMed: 15890615] [Abstract]
Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL132969 Genomic DNA. Translation: CAB86900.1.
CP002686 Genomic DNA. Translation: AEE79018.1.
AY050880 mRNA. Translation: AAK92817.1.
AY054638 mRNA. Translation: AAK96829.1.
AY072493 mRNA. Translation: AAL66908.1.
AY150397 mRNA. Translation: AAN12942.1.
IPIIPI00533612.
PIRPA0047.
T47553.
RefSeqNP_190864.1. NM_115156.2.
UniGeneAt.9858.

3D structure databases

HSSPHSSP built from PDB template 1OC3 based on UniProtKB P30044.
ProteinModelPortalQ949U7.
SMRQ949U7. Positions 71-234.
ModBaseSearch...

Protein-protein interaction databases

IntActQ949U7. 1 interaction.
STRINGQ949U7.

Protein family/group databases

PeroxiBase4353. AtPrxIIE.

Proteomic databases

PRIDEQ949U7.
ProMEXQ949U7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G52960.1; AT3G52960.1; AT3G52960.
GeneID824462.
GenomeReviewsGene locus AT3G52960 in contig BA000014_GR.
KEGGath:AT3G52960.
NMPDRfig|3702.1.peg.16571.

Organism-specific databases

TAIRAt3g52960.

Phylogenomic databases

eggNOGKOG0541.
GeneTreeEPGT00070000029465.
HOGENOMHBG493509.
InParanoidQ949U7.
OMAVIHLEES.
PhylomeDBQ949U7.
ProtClustDBCLSN2720528.

Gene expression databases

GenevestigatorQ949U7.

Family and domain databases

InterProIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRX2E_ARATH
AccessionPrimary (citable) accession number: Q949U7
Secondary accession number(s): Q9LF96
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families