RGD Reference Report - Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. - Rat Genome Database

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Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver.

Authors: Lee, SR  Kim, JR  Kwon, KS  Yoon, HW  Levine, RL  Ginsburg, A  Rhee, SG 
Citation: Lee SR, etal., J Biol Chem 1999 Feb 19;274(8):4722-34.
RGD ID: 61776
Web Url: http://www.jbc.org/cgi/content/full/274/8/4722
Pubmed: PMID:9988709   (View Abstract at PubMed)

A thioredoxin reductase (TrxR), named here TrxR2, that did not react with antibodies to the previously identified TrxR (now named TrxR1) was purified from rat liver. Like TrxR1, TrxR2 was a dimeric enzyme containing selenocysteine (Secys) as the COOH-terminal penultimate residue. A cDNA encoding TrxR2 was cloned from rat liver; the open reading frame predicts a polypeptide of 526 amino acids with a COOH-terminal Gly-Cys-Secys-Gly motif provided that an in-frame TGA codon encodes Secys. The 3'-untranslated region of the cDNA contains a canonical Secys insertion sequence element. The deduced amino acid sequence of TrxR2 shows 54% identity to that of TrxR1 and contained 36 additional residues upstream of the experimentally determined NH2-terminal sequence. The sequence of this 36-residue region is typical of that of a mitochondrial leader peptide. Immunoblot analysis confirmed that TrxR2 is localized almost exclusively in mitochondria, whereas TrxR1 is a cytosolic protein. Unlike TrxR1, which was expressed at a level of 0.6 to 1.6 microgram/milligram of total soluble protein in all rat tissues examined, TrxR2 was relatively abundant (0.3 to 0.6 microgram/mg) only in liver, kidney, adrenal gland, and heart. The specific localization of TrxR2 in mitochondria, together with the previous identification of mitochondria-specific thioredoxin and thioredoxin-dependent peroxidase, suggest that these three proteins provide a primary line of defense against H2O2 produced by the mitochondrial respiratory chain.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Txnrd2Ratprotein-containing complex assembly  TAS dimerizationRGD 
Txnrd2Ratresponse to hydrogen peroxide  TAS  RGD 
Txnrd2Ratresponse to oxygen radical involved_inTAS PMID:9988709UniProt 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Txnrd2Ratmitochondrion located_inIDA PMID:9988709UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Txnrd2Ratprotein homodimerization activity enablesIDA PMID:9988709UniProt 
Txnrd2Ratthioredoxin-disulfide reductase (NADPH) activity enablesIDA PMID:9988709UniProt 
Txnrd2Ratthioredoxin-disulfide reductase (NADPH) activity  TAS  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Txnrd2  (thioredoxin reductase 2)

Objects referenced in this article
Gene Txnrd1 thioredoxin reductase 1 Rattus norvegicus

Additional Information