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Q9V429 (THIO2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Thioredoxin-2

Short name=DmTrx-2
Gene names
Name:Trx-2
ORF Names:CG31884
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Subunit structure

Monomer. Ref.6

Developmental stage

Larval stages. Ref.5

Sequence similarities

Belongs to the thioredoxin family. UniProtKB P47938

Contains 1 thioredoxin domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q9V429-1)

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.
Note: No experimental confirmation available.
Isoform Short (identifier: Q9V429-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 114114Thioredoxin-2
PRO_0000120034

Regions

Domain4 – 114111Thioredoxin

Sites

Active site401Nucleophile By similarity
Active site431Nucleophile By similarity
Site341Deprotonates C-terminal active site Cys By similarity
Site411Contributes to redox potential value By similarity
Site421Contributes to redox potential value By similarity

Amino acid modifications

Disulfide bond40 ↔ 43Redox-active Ref.6 UniProtKB P47938

Natural variations

Alternative sequence1 – 1616MMILL…HFHLQ → MVYQVKDK in isoform Short.
VSP_006423

Secondary structure

.................. 114
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (A) (B) [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: D67E87151114C4CE

FASTA11412,696
        10         20         30         40         50         60 
MMILLRDSTN LHFHLQADLD GQLTKASGKL VVLDFFATWC GPCKMISPKL VELSTQFADN 

        70         80         90        100        110 
VVVLKVDVDE CEDIAMEYNI SSMPTFVFLK NGVKVEEFAG ANAKRLEDVI KANI 

« Hide

Isoform Short [UniParc].

Checksum: 255341DD95839FB8
Show »

FASTA10611,737

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF220362 mRNA. Translation: AAF37263.1.
AE014134 Genomic DNA. Translation: AAN10700.1.
AE014134 Genomic DNA. Translation: AAN10701.1.
AY060458 mRNA. Translation: AAL25497.1.
RefSeqNP_523526.1. NM_078802.4. [Q9V429-2]
NP_723475.1. NM_164863.3. [Q9V429-2]
UniGeneDm.2664.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9V429.
SMRQ9V429. Positions 16-114.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60380. 53 interactions.
IntActQ9V429. 1 interaction.
MINTMINT-747162.

Proteomic databases

PaxDbQ9V429.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID34281.
KEGGdme:Dmel_CG31884.
UCSCCG31884-RA. d. melanogaster. [Q9V429-1]

Organism-specific databases

CTD34281.
FlyBaseFBgn0040070. Trx-2.

Phylogenomic databases

eggNOGCOG0526.
InParanoidQ9V429.
KOK03671.
OMAFASFTHP.
OrthoDBEOG7H4DX9.
PhylomeDBQ9V429.

Gene expression databases

BgeeQ9V429.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERPTHR10438. PTHR10438. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFPIRSF000077. Thioredoxin. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR01068. thioredoxin. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9V429.
GenomeRNAi34281.
NextBio787726.

Entry information

Entry nameTHIO2_DROME
AccessionPrimary (citable) accession number: Q9V429
Secondary accession number(s): A4V0H9, Q95SW4
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase