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Q9XEX2

- PRX2B_ARATH

UniProt

Q9XEX2 - PRX2B_ARATH

Protein

Peroxiredoxin-2B

Gene

PRXIIB

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

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

    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

    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

    ArrayExpressiQ9XEX2.
    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.
    OMAiEDITACP.
    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

    MAPIAVGDVV PDGTISFFDE NDQLQTASVH SLAAGKKVIL FGVPGAFTPT    50
    CSMKHVPGFI EKAEELKSKG VDEIICFSVN DPFVMKAWGK TYPENKHVKF 100
    VADGSGEYTH LLGLELDLKD KGLGVRSRRF ALLLDDLKVT VANVESGGEF 150
    TVSSADDILK AL 162
    Length:162
    Mass (Da):17,428
    Last modified:November 1, 1999 - v1
    Checksum:i6EB4690D17598814
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi B96684.
    PA0022.
    RefSeqi NP_176773.1. NM_105270.2. [Q9XEX2-1 ]
    UniGenei At.20543.

    3D structure databases

    ProteinModelPortali Q9XEX2.
    SMRi Q9XEX2. Positions 1-162.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9XEX2. 2 interactions.

    Protein family/group databases

    PeroxiBasei 4344. AtPrxII02.

    Proteomic databases

    PaxDbi Q9XEX2.
    PRIDEi Q9XEX2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G65980.1 ; AT1G65980.1 ; AT1G65980 . [Q9XEX2-1 ]
    GeneIDi 842910.
    KEGGi ath:AT1G65980.

    Organism-specific databases

    GeneFarmi 755.
    TAIRi AT1G65980.

    Phylogenomic databases

    eggNOGi COG0678.
    HOGENOMi HOG000255884.
    InParanoidi Q9XEX2.
    OMAi EDITACP.
    PhylomeDBi Q9XEX2.

    Enzyme and pathway databases

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

    Gene expression databases

    ArrayExpressi Q9XEX2.
    Genevestigatori Q9XEX2.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR013740. Redoxin.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF08534. Redoxin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 105 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