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Reviewed, UniProtKB/Swiss-Prot Q9VNT5 (TRXR2_DROME)

Last modified November 3, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Thioredoxin reductase 2, mitochondrial
      Short name=TrxR-2
    EC=1.8.1.9
Gene names
Name: Trxr-2
ORF Names: CG11401
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length516 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms. UniProtKB P91938

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH. UniProtKB P91938

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity. UniProtKB P91938

Subcellular location

Mitochondrion.

Miscellaneous

The active site is a redox-active disulfide bond. UniProtKB P91938

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG18142Q9VGD91EBI-178020,EBI-123747

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 516Thioredoxin reductase 2, mitochondrialPRO_0000030293

Regions

Nucleotide binding62 – 7918FAD By similarity

Sites

Active site4891Proton acceptor By similarity UniProtKB P91938

Amino acid modifications

Disulfide bond79 ↔ 84Redox-active By similarity UniProtKB P91938

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Sequences

Sequence LengthMass (Da)Tools
Q9VNT5-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D82A89CBF6A4B7E8

FASTA51656,277
        10         20         30         40         50         60 
MSTIKFLRSS THNALRSSLG WCRLAASRPR YDYDLVVLGG GSAGLACAKE AAGCGARVLC 

        70         80         90        100        110        120 
FDYVKPTPVG TKWGIGGTCV NVGCIPKKLM HQASLLGEAV HEAVAYGWNV DDTNIRPDWR 

       130        140        150        160        170        180 
KLVRSVQNHI KSVNWVTRVD LRDKKVEYVN SMATFRDSHT IEYVAMPGAE HRQVTSEYVV 

       190        200        210        220        230        240 
VAVGGRPRYP DIPGAVELGI TSDDIFSYER EPGRTLVVGA GYVGLECACF LKGLGYEPTV 

       250        260        270        280        290        300 
MVRSIVLRGF DRQMSELLAA MMTERGIPFL GTTIPKAVER QADGRLLVRY RNTTTQMDGS 

       310        320        330        340        350        360 
DVFDTVLWAI GRKGLIEDLN LDAAGVKTHD DKIVVDAAEA TSVPHIFAVG DIIYGRPELT 

       370        380        390        400        410        420 
PVAILSGRLL ARRLFAGSTQ LMDYADVATT VFTPLEYSCV GMSEETAIEL RGADNIEVFH 

       430        440        450        460        470        480 
GYYKPTEFFI PQKSVRHCYL KAVAEVSGDQ KILGLHYIGP VAGEVIQGFA AALKTGLTVK 

       490        500        510 
TLLNTVGIHP TTAEEFTRLS ITKRSGRDPT PASCCS

« Hide

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References

« Hide 'large scale' references
[1]"Drosophila melanogaster thioredoxin reductase 2."
Kanzok S., Becker K., Schirmer R.H.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Testis.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF236866 Genomic DNA. Translation: AAF64152.1.
AE014296 Genomic DNA. Translation: AAF51835.1.
AY121613 mRNA. Translation: AAM51940.1.
RefSeqNP_524216.1.
UniGeneDm.2498

3D structure databases

HSSPHSSP built from PDB template 1ONF based on UniProtKB Q94655.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:19796N.
IntActQ9VNT5. 1 interaction.
STRINGQ9VNT5.

Proteomic databases

PRIDEQ9VNT5.

Genome annotation databases

EnsemblFBtr0078514; FBpp0078166; FBgn0037170; Drosophila melanogaster. [Genome view]
GeneID40475.
KEGGdme:Dmel_CG11401.
NMPDRfig|7227.3.peg.11057.
UCSCZK637.10. c. elegans.

Organism-specific databases

CTD40475.
FlyBaseFBgn0037170. Trxr-2.

Phylogenomic databases

HOGENOMQ9VNT5.
OMAHEAVAYG.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-017848-MON.
BRENDA1.8.1.9. 48.

Gene expression databases

BgeeQ9VNT5.
GermOnlineCG11401. Drosophila melanogaster.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF23. Reduct_Se. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01438. TGR. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio818953.

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Entry information

Entry nameTRXR2_DROME
AccessionPrimary (citable) accession number: Q9VNT5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents