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Molecular cloning and expression of a cDNA encoding a human thioredoxin-like protein

Miranda-Vizuete, A (author)
Karolinska Institute, Huddinge, Sweden
Gustafsson, Jan-.Åke (author)
Karolinska Institutet
Spyrou, Giannis (author)
Karolinska Institute, Huddinge, Sweden
 (creator_code:org_t)
Elsevier, 1998
1998
English.
In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier. - 0006-291X .- 1090-2104. ; 243:1, s. 284-288
  • Journal article (peer-reviewed)
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  • This report describes the cloning of a human cDNA that encodes a new protein (Txl, Thioredoxin-like) that belongs to the expanding family of thioredoxins based on sequence comparison of the deduced amino acid sequence. This cDNA, with a total length of 1,278 bp, consists of 205 bp of 5'-untranslated sequence (including an in frame stop codon), an open reading frame of 870 bp and a 203 bp fragment of 3'-untranslated sequence. The coding sequence predicts a protein of 289 amino acids with two distinct domains: an N-terminal domain of 105 residues homologous to the rest of mammalian thioredoxins containing the conserved active site (CGPC) and a C-terminal domain of 184 residues with no homology with any other protein in the database. Northern blot analysis indicates that the txl probe hybridizes to a 1.3 Kb mRNA and is ubiquitously expressed in human tissues with the highest expression in stomach, testis and bone marrow.

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