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Q9V429

- THIO2_DROME

UniProt

Q9V429 - THIO2_DROME

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Protein

Thioredoxin-2

Gene
Trx-2, CG31884
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Cys By similarity
Active sitei40 – 401Nucleophile By similarity
Sitei41 – 411Contributes to redox potential value By similarity
Sitei42 – 421Contributes to redox potential value By similarity
Active sitei43 – 431Nucleophile By 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
Complete GO annotation...

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)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0040070. Trx-2.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: FlyBase
Complete GO annotation...

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-activeBy similarity1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiQ9V429.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 114111ThioredoxinAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.By similarity
Contains 1 thioredoxin domain.

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. VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 113 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

Similar proteinsi