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Reviewed, UniProtKB/Swiss-Prot O89049 (TRXR1_RAT)

Last modified June 16, 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Thioredoxin reductase 1, cytoplasmic
      Short name=TR
    EC=1.8.1.9
Alternative name(s):
    Thioredoxin reductase TR1
    NADPH-dependent thioredoxin reductase
Gene names
Name: Txnrd1
Synonyms: Trxr1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity.

Sequence similarities

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

Sequence caution

The sequence AAD43039.1 differs from that shown. Reason: Erroneous termination at position 497. Translated as Sec.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Thioredoxin reductase 1, cytoplasmic
PRO_0000067985

Regions

Nucleotide binding42 – 5918FAD By similarity

Sites

Active site4711Proton acceptor

Amino acid modifications

Non-standard residue4971Selenocysteine
Modified residue111Phosphotyrosine By similarity
Modified residue1311Phosphotyrosine By similarity
Modified residue4221Phosphotyrosine By similarity
Disulfide bond59 ↔ 64Redox-active Ref.5
Cross-link496 ↔ 497Cysteinyl-selenocysteine (Cys-Sec)

Experimental info

Mutagenesis4971U → S: Loss of activity. Ref.4
Mutagenesis4971Missing: Loss of activity. Ref.4
Sequence conflict52 – 532NG → RW in AAF32363. Ref.3
Sequence conflict451 – 4555GFAAA → ALQP Ref.2
Sequence conflict451 – 4555GFAAA → ALQP in AAF32362. Ref.3

Secondary structure

1 .................................................................................... 498
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O89049-1 [UniParc].

Last modified February 26, 2008. Version 4.
Checksum: 2F1EC2A8EAE7BF3E

FASTA49854,386
        10         20         30         40         50         60 
MNDSKDAPKS YDFDLIIIGG GSGGLAAAKE AAKFDKKVMV LDFVTPTPLG TNGGLGGTCV 

        70         80         90        100        110        120 
NVGCIPKKLM HQAALLGQAL KDSRNYGWKL EDTVKHDWEK MTESVQNHIG SLNWGYRVAL 

       130        140        150        160        170        180 
REKKVVYENA YGKFIGPHKI MATNNKGKEK VYSAERFLIA TGERPRYLGI PGDKEYCISS 

       190        200        210        220        230        240 
DDLFSLPYCP GKTLVVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM 

       250        260        270        280        290        300 
EEHGIKFIRQ FVPTKIEQIE AGTPGRLKVT AKSTNSEETI EDEFNTVLLA VGRDSCTRTI 

       310        320        330        340        350        360 
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEGKL ELTPVAIQAG RLLAQRLYGG 

       370        380        390        400        410        420 
STVKCDYDNV PTTVFTPLEY GCCGLSEEKA VEKFGEENIE VYHSFFWPLE WTVPSRDNNK 

       430        440        450        460        470        480 
CYAKVICNLK DNERVVGFHV LGPNAGEVTQ GFAAAKCGLT KQQLDSTIGI HPVCAEIFTT 

       490 
LSVTKRSGGD ILQSGCUG

« Hide

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References

[1]"Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue."
Zhong L., Arner E.S.J., Ljung J., Aaslund F., Holmgren A.
J. Biol. Chem. 273:8581-8591(1998) [PubMed: 9535831] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Neuroblastoma.
[2]"Functional expression of rat thioredoxin reductase: selenocysteine insertion sequence element is essential for the active enzyme."
Fujiwara N., Fujii T., Fujii J., Taniguchi N.
Biochem. J. 340:439-444(1999) [PubMed: 10333487] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SELENOCYSTEINE AT SEC-497.
Tissue: Kidney and Liver.
[3]"Molecular cloning of thioredoxin reductase 1 from rat liver."
Rundlof A., Arner E.S.J.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[4]"Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations."
Zhong L., Holmgren A.
J. Biol. Chem. 275:18121-18128(2000) [PubMed: 10849437] [Abstract]
Cited for: PROTEIN SEQUENCE OF 450-456 AND 487-498, FUNCTION, MUTAGENESIS OF SEC-497, CHARACTERIZATION.
[5]"Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme."
Sandalova T., Zhong L., Lindqvist Y., Holmgren A., Schneider G.
Proc. Natl. Acad. Sci. U.S.A. 98:9533-9538(2001) [PubMed: 11481439] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT CYS-497 IN COMPLEX WITH NADP, DISULFIDE BOND, HOMODIMERIZATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

U63923 mRNA. Translation: AAC35244.2.
AF108213 mRNA. Translation: AAD43039.1. Sequence problems.
AF220760 mRNA. Translation: AAF32362.1.
AF220761 mRNA. Translation: AAF32363.1.
IPIIPI00454559.
UniGeneRn.67581

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1H6VX-ray3.00A/B/C/D/E/F1-498[»]
3EANX-ray2.75A/B/C/D/E/F1-498[»]
3EAOX-ray3.10A/B/C/D/E/F1-498[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000009088. Rattus norvegicus. [Contig view]

Organism-specific databases

RGD61959. Txnrd1.

Phylogenomic databases

HOVERGENO89049.

Enzyme and pathway databases

BRENDA1.8.1.9. 248.

Gene expression databases

ArrayExpressO89049.

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. Reduct_Se.
[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...

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Entry information

Entry nameTRXR1_RAT
AccessionPrimary (citable) accession number: O89049
Secondary accession number(s): Q9JKZ3, Q9JKZ4, Q9R1I3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: February 26, 2008
Last modified: June 16, 2009
This is version 78 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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