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Protein

Peroxiredoxin-2B

Gene

PRXIIB

Organism
Arabidopsis thaliana (Mouse-ear cress)
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 or glutaredoxin system. May be involved in intracellular redox signaling.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511Cysteine sulfenic acid (-SOH) intermediateSequence Analysis

GO - Molecular functioni

  1. peroxidase activity Source: UniProtKB-KW
  2. peroxiredoxin activity Source: UniProtKB-EC

GO - Biological processi

  1. response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciARA:AT1G65980-MONOMER.
ARA:GQT-2601-MONOMER.
ReactomeiREACT_180046. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei4344. AtPrxII02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2B (EC:1.11.1.15)
Alternative name(s):
Peroxiredoxin IIB
Peroxiredoxin TPx1
Thioredoxin reductase 2B
Thioredoxin-dependent peroxidase 1
Gene namesi
Name:PRXIIB
Synonyms:TPX1
Ordered Locus Names:At1g65980
ORF Names:F12P19.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G65980.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. cytosol Source: TAIR
  3. membrane Source: TAIR
  4. plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Peroxiredoxin-2BPRO_0000282279Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 76Redox-active

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9XEX2.
PRIDEiQ9XEX2.

Expressioni

Tissue specificityi

Expressed in all tissues but mostly in reproductive tissues such as buds, flowers, siliques and seeds.2 Publications

Inductioni

Slightly induced by salt stress.1 Publication

Gene expression databases

ExpressionAtlasiQ9XEX2. baseline and differential.
GenevestigatoriQ9XEX2.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

IntActiQ9XEX2. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9XEX2.
SMRiQ9XEX2. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 162159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peroxiredoxin 2 family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0678.
HOGENOMiHOG000255884.
InParanoidiQ9XEX2.
OMAiYYASKEW.
PhylomeDBiQ9XEX2.

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]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9XEX2-1) [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
MAPIAVGDVV PDGTISFFDE NDQLQTASVH SLAAGKKVIL FGVPGAFTPT
60 70 80 90 100
CSMKHVPGFI EKAEELKSKG VDEIICFSVN DPFVMKAWGK TYPENKHVKF
110 120 130 140 150
VADGSGEYTH LLGLELDLKD KGLGVRSRRF ALLLDDLKVT VANVESGGEF
160
TVSSADDILK AL
Length:162
Mass (Da):17,428
Last modified:November 1, 1999 - v1
Checksum:i6EB4690D17598814
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB96684.
PA0022.
RefSeqiNP_176773.1. NM_105270.2. [Q9XEX2-1]
UniGeneiAt.20543.

Genome annotation databases

EnsemblPlantsiAT1G65980.1; AT1G65980.1; AT1G65980. [Q9XEX2-1]
GeneIDi842910.
KEGGiath:AT1G65980.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB96684.
PA0022.
RefSeqiNP_176773.1. NM_105270.2. [Q9XEX2-1]
UniGeneiAt.20543.

3D structure databases

ProteinModelPortaliQ9XEX2.
SMRiQ9XEX2. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9XEX2. 2 interactions.

Protein family/group databases

PeroxiBasei4344. AtPrxII02.

Proteomic databases

PaxDbiQ9XEX2.
PRIDEiQ9XEX2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G65980.1; AT1G65980.1; AT1G65980. [Q9XEX2-1]
GeneIDi842910.
KEGGiath:AT1G65980.

Organism-specific databases

GeneFarmi755.
TAIRiAT1G65980.

Phylogenomic databases

eggNOGiCOG0678.
HOGENOMiHOG000255884.
InParanoidiQ9XEX2.
OMAiYYASKEW.
PhylomeDBiQ9XEX2.

Enzyme and pathway databases

BioCyciARA:AT1G65980-MONOMER.
ARA:GQT-2601-MONOMER.
ReactomeiREACT_180046. Detoxification of Reactive Oxygen Species.

Gene expression databases

ExpressionAtlasiQ9XEX2. baseline and differential.
GenevestigatoriQ9XEX2.

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. "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.
    , 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.
    , 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.

Entry informationi

Entry nameiPRX2B_ARATH
AccessioniPrimary (citable) accession number: Q9XEX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: November 1, 1999
Last modified: January 7, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.