Q9V429 (THIO2_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thioredoxin-2
Short name=DmTrx-2

Gene names

Name:	Trx-2
ORF Names:	CG31884

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	114 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Electron transport Transport
Coding sequence diversity	Alternative splicing
Domain	Redox-active center
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from direct assay Ref.5. Source: UniProtKB determination of adult lifespan Inferred from mutant phenotype PubMed 17567437. Source: FlyBase electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro response to DNA damage stimulus Inferred from mutant phenotype PubMed 19543366. Source: FlyBase response to oxidative stress Inferred from mutant phenotype PubMed 17567437. Source: FlyBase
Cellular_component	nucleus Inferred from direct assay PubMed 14579129. Source: FlyBase
Molecular_function	disulfide oxidoreductase activity Inferred from direct assay Ref.5. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 114

114

Thioredoxin-2

PRO_0000120034

Regions

Domain

4 – 114

111

Thioredoxin

Sites

Active site

40

1

Nucleophile By similarity

Active site

43

1

Nucleophile By similarity

Site

34

1

Deprotonates C-terminal active site Cys By similarity

Site

41

1

Contributes to redox potential value By similarity

Site

42

1

Contributes to redox potential value By similarity

Amino acid modifications

Disulfide bond

40 ↔ 43

Redox-active Ref.6 UniProtKB P47938

Natural variations

Alternative sequence

1 – 16

16

MMILL…HFHLQ → MVYQVKDK in isoform Short.

VSP_006423

Secondary structure

1

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.

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114

Helix Strand Turn

Details...

Helix

17 – 26

10

Beta strand

29 – 36

8

Helix

41 – 56

16

Turn

57 – 60

4

Beta strand

61 – 67

7

Turn

68 – 70

3

Helix

72 – 77

6

Beta strand

82 – 90

9

Beta strand

93 – 100

8

Helix

103 – 112

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long (A) (B) [UniParc]. Last modified January 10, 2003. Version 2. Checksum: D67E87151114C4CE	FASTA	114	12,696
	10 20 30 40 50 60 MMILLRDSTN LHFHLQADLD GQLTKASGKL VVLDFFATWC GPCKMISPKL VELSTQFADN 70 80 90 100 110 VVVLKVDVDE CEDIAMEYNI SSMPTFVFLK NGVKVEEFAG ANAKRLEDVI KANI
	Isoform Short [UniParc]. Checksum: 255341DD95839FB8	FASTA	106	11,737
	10 20 30 40 50 60 MVYQVKDKAD LDGQLTKASG KLVVLDFFAT WCGPCKMISP KLVELSTQFA DNVVVLKVDV 70 80 90 100 DECEDIAMEY NISSMPTFVF LKNGVKVEEF AGANAKRLED VIKANI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

RefSeq

NP_523526.1. NM_078802.4.
NP_723475.1. NM_164863.3.

UniGene

Dm.2664.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9V429.

SMR

Q9V429. Positions 16-114.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9V429. 1 interaction.

MINT

MINT-747162.

Proteomic databases

PaxDb

Q9V429.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

34281.

KEGG

dme:Dmel_CG31884.

UCSC

CG31884-RA. d. melanogaster.

Organism-specific databases

CTD

34281.

FlyBase

FBgn0040070. Trx-2.

Phylogenomic databases

eggNOG

COG0526.

InParanoid

Q9V429.

KO

K03671.

OMA

CKAMEPR.

OrthoDB

EOG4KD53Q.

Gene expression databases

Bgee

Q9V429.

GermOnline

CG31884. Drosophila melanogaster.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]

PANTHER

PTHR10438. PTHR10438. 1 hit.

Pfam

PF00085. Thioredoxin. 1 hit.
[Graphical view]

PIRSF

PIRSF000077. Thioredoxin. 1 hit.

PRINTS

PR00421. THIOREDOXIN.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

TIGRFAMs

TIGR01068. thioredoxin. 1 hit.

PROSITE

PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9V429.

GenomeRNAi

34281.

NextBio

787726.

Entry information

Entry name

THIO2_DROME

Accession

Primary (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:	April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project