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Q9V429

- THIO2_DROME

UniProt

Q9V429 - THIO2_DROME

Protein

Thioredoxin-2

Gene

Trx-2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. As a reducing substrate of peroxiredoxin 1, thioredoxin 2 is preferred over thioredoxin 1.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei34 – 341Deprotonates C-terminal active site CysBy similarity
    Active sitei40 – 401NucleophileBy similarity
    Sitei41 – 411Contributes to redox potential valueBy similarity
    Sitei42 – 421Contributes to redox potential valueBy similarity
    Active sitei43 – 431NucleophileBy similarity

    GO - Molecular functioni

    1. disulfide oxidoreductase activity Source: UniProtKB
    2. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: UniProtKB
    2. cellular response to DNA damage stimulus Source: FlyBase
    3. defense response to fungus Source: FlyBase
    4. determination of adult lifespan Source: FlyBase
    5. glycerol ether metabolic process Source: InterPro
    6. response to oxidative stress Source: FlyBase

    Keywords - Biological processi

    Electron transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin-2
    Short name:
    DmTrx-2
    Gene namesi
    Name:Trx-2
    ORF Names:CG31884
    OrganismiDrosophila melanogaster (Fruit fly)Imported
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0040070. Trx-2.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: FlyBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 114114Thioredoxin-2PRO_0000120034Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 43Redox-active1 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9V429.

    Expressioni

    Developmental stagei

    Larval stages.1 Publication

    Gene expression databases

    BgeeiQ9V429.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi60380. 53 interactions.
    IntActiQ9V429. 1 interaction.
    MINTiMINT-747162.

    Structurei

    Secondary structure

    1
    114
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 2610
    Beta strandi29 – 368
    Helixi41 – 5616
    Turni57 – 604
    Beta strandi61 – 677
    Turni68 – 703
    Helixi72 – 776
    Beta strandi82 – 909
    Beta strandi93 – 1008
    Helixi103 – 11210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XW9X-ray2.30A/B/C/D17-114[»]
    1XWAX-ray2.20A/B/C/D17-114[»]
    1XWBX-ray2.20A/B/C/D17-114[»]
    1XWCX-ray2.30A17-114[»]
    ProteinModelPortaliQ9V429.
    SMRiQ9V429. Positions 16-114.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9V429.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 114111ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0526.
    InParanoidiQ9V429.
    KOiK03671.
    OMAiFASFTHP.
    OrthoDBiEOG7H4DX9.
    PhylomeDBiQ9V429.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PANTHERiPTHR10438. PTHR10438. 1 hit.
    PfamiPF00085. Thioredoxin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000077. Thioredoxin. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
    PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q9V429-1) [UniParc]FASTAAdd to Basket

    Also known as: A, B

    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

    MMILLRDSTN LHFHLQADLD GQLTKASGKL VVLDFFATWC GPCKMISPKL    50
    VELSTQFADN VVVLKVDVDE CEDIAMEYNI SSMPTFVFLK NGVKVEEFAG 100
    ANAKRLEDVI KANI 114

    Note: No experimental confirmation available.

    Length:114
    Mass (Da):12,696
    Last modified:January 10, 2003 - v2
    Checksum:iD67E87151114C4CE
    GO
    Isoform Short (identifier: Q9V429-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: MMILLRDSTNLHFHLQ → MVYQVKDK

    Show »
    Length:106
    Mass (Da):11,737
    Checksum:i255341DD95839FB8
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1616MMILL…HFHLQ → MVYQVKDK in isoform Short. 1 PublicationVSP_006423Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220362 mRNA. Translation: AAF37263.1.
    AE014134 Genomic DNA. Translation: AAN10700.1.
    AE014134 Genomic DNA. Translation: AAN10701.1.
    AY060458 mRNA. Translation: AAL25497.1.
    RefSeqiNP_523526.1. NM_078802.4. [Q9V429-2]
    NP_723475.1. NM_164863.3. [Q9V429-2]
    UniGeneiDm.2664.

    Genome annotation databases

    GeneIDi34281.
    KEGGidme:Dmel_CG31884.
    UCSCiCG31884-RA. d. melanogaster. [Q9V429-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220362 mRNA. Translation: AAF37263.1 .
    AE014134 Genomic DNA. Translation: AAN10700.1 .
    AE014134 Genomic DNA. Translation: AAN10701.1 .
    AY060458 mRNA. Translation: AAL25497.1 .
    RefSeqi NP_523526.1. NM_078802.4. [Q9V429-2 ]
    NP_723475.1. NM_164863.3. [Q9V429-2 ]
    UniGenei Dm.2664.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XW9 X-ray 2.30 A/B/C/D 17-114 [» ]
    1XWA X-ray 2.20 A/B/C/D 17-114 [» ]
    1XWB X-ray 2.20 A/B/C/D 17-114 [» ]
    1XWC X-ray 2.30 A 17-114 [» ]
    ProteinModelPortali Q9V429.
    SMRi Q9V429. Positions 16-114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 60380. 53 interactions.
    IntActi Q9V429. 1 interaction.
    MINTi MINT-747162.

    Proteomic databases

    PaxDbi Q9V429.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 34281.
    KEGGi dme:Dmel_CG31884.
    UCSCi CG31884-RA. d. melanogaster. [Q9V429-1 ]

    Organism-specific databases

    CTDi 34281.
    FlyBasei FBgn0040070. Trx-2.

    Phylogenomic databases

    eggNOGi COG0526.
    InParanoidi Q9V429.
    KOi K03671.
    OMAi FASFTHP.
    OrthoDBi EOG7H4DX9.
    PhylomeDBi Q9V429.

    Miscellaneous databases

    EvolutionaryTracei Q9V429.
    GenomeRNAii 34281.
    NextBioi 787726.

    Gene expression databases

    Bgeei Q9V429.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    PANTHERi PTHR10438. PTHR10438. 1 hit.
    Pfami PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000077. Thioredoxin. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    TIGRFAMsi TIGR01068. thioredoxin. 1 hit.
    PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Charaterization of Drosophila thioredoxin."
      Seong K., Horiuchi N., Aigaki T.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Strain: Berkeley.
      Tissue: Embryo.
    5. "Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: isolation and characterization of a second thioredoxin in D.melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2."
      Bauer H., Kanzok S.M., Schirmer R.H.
      J. Biol. Chem. 277:17457-17463(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    6. "Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster."
      Wahl M.C., Irmler A., Hecker B., Schirmer R.H., Becker K.
      J. Mol. Biol. 345:1119-1130(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 17-114, SUBUNIT, DISULFIDE BOND.

    Entry informationi

    Entry nameiTHIO2_DROME
    AccessioniPrimary (citable) accession number: Q9V429
    Secondary accession number(s): A4V0H9, Q95SW4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2003
    Last sequence update: January 10, 2003
    Last modified: October 1, 2014
    This is version 114 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3