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Q9XEX2 (PRX2B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. 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-2B

EC=1.11.1.15
Alternative name(s):
Peroxiredoxin IIB
Peroxiredoxin TPx1
Thioredoxin reductase 2B
Thioredoxin-dependent peroxidase 1
Gene names
Name:PRXIIB
Synonyms:TPX1
Ordered Locus Names:At1g65980
ORF Names:F12P19.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
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 intracellular redox signaling. Ref.6

Catalytic activity

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

Subunit structure

Monomer. Ref.5 Ref.6

Subcellular location

Cytoplasm Ref.6.

Tissue specificity

Expressed in all tissues but mostly in reproductive tissues such as buds, flowers, siliques and seeds. Ref.5 Ref.6

Induction

Slightly induced by salt stress. Ref.5

Post-translational modification

The Cys-51-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-51 (probably Cys-SOH) rapidly reacts with Cys-76-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.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9XEX2-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 162162Peroxiredoxin-2B
PRO_0000282279

Regions

Domain4 – 162159Thioredoxin

Sites

Active site511Cysteine sulfenic acid (-SOH) intermediate Potential

Amino acid modifications

Disulfide bond51 ↔ 76Redox-active

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 6EB4690D17598814

FASTA16217,428
        10         20         30         40         50         60 
MAPIAVGDVV PDGTISFFDE NDQLQTASVH SLAAGKKVIL FGVPGAFTPT CSMKHVPGFI 

        70         80         90        100        110        120 
EKAEELKSKG VDEIICFSVN DPFVMKAWGK TYPENKHVKF VADGSGEYTH LLGLELDLKD 

       130        140        150        160 
KGLGVRSRRF ALLLDDLKVT VANVESGGEF TVSSADDILK AL 

« Hide

References

« Hide 'large scale' references
[1]"In vivo characterization of a thioredoxin H target protein defines a new peroxiredoxin family."
Verdoucq L., Vignols F., Jacquot J.-P., Chartier Y., Meyer Y.
J. Biol. Chem. 274:19714-19722(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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: SUBUNIT, TISSUE SPECIFICITY, INDUCTION.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]"The plant multigenic family of thiol peroxidases."
Rouhier N., Jacquot J.-P.
Free Radic. Biol. Med. 38:1413-1421(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF121355 mRNA. Translation: AAD28242.1.
AC009513 Genomic DNA. Translation: AAF06058.1.
CP002684 Genomic DNA. Translation: AEE34447.1.
AF332464 mRNA. Translation: AAG48827.1.
AY065056 mRNA. Translation: AAL57690.1.
PIRB96684.
PA0022.
RefSeqNP_176773.1. NM_105270.2. [Q9XEX2-1]
UniGeneAt.20543.

3D structure databases

ProteinModelPortalQ9XEX2.
SMRQ9XEX2. Positions 1-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9XEX2. 2 interactions.

Protein family/group databases

PeroxiBase4344. AtPrxII02.

Proteomic databases

PaxDbQ9XEX2.
PRIDEQ9XEX2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G65980.1; AT1G65980.1; AT1G65980. [Q9XEX2-1]
GeneID842910.
KEGGath:AT1G65980.

Organism-specific databases

GeneFarm755.
TAIRAT1G65980.

Phylogenomic databases

eggNOGCOG0678.
HOGENOMHOG000255884.
InParanoidQ9XEX2.
OMAEDITACP.
PhylomeDBQ9XEX2.

Enzyme and pathway databases

BioCycARA:AT1G65980-MONOMER.
ARA:GQT-2601-MONOMER.

Gene expression databases

ArrayExpressQ9XEX2.
GenevestigatorQ9XEX2.

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...

Entry information

Entry namePRX2B_ARATH
AccessionPrimary (citable) accession number: Q9XEX2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: November 1, 1999
Last modified: May 14, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names