High impact information on TRA1

• To evaluate the interaction of GRP94 with adenine nucleotides, the ATP binding and hydrolysis activities were directly assayed [1].
• Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent [1].
• On the basis of these data, we propose that the peptide binding activity of GRP94 is adenine nucleotide-independent and that ATP binding and hydrolysis are not inherent properties of GRP94 [1].
• The results suggest that Grp94 scavenged xanthurenic acid-modified proteins, and for this reason become preferentially yellow-stained in the presence of yellow xanthurenic acid [2].
• This study shows that accumulation of xanthurenic acid in the lens epithelial cells leads to an overexpression of endoplasmic reticulum (ER) resident stress chaperones proteins, glucose-regulated protein (Grp94), and calreticulin [2].

Biological context of TRA1

• We measured the amounts of GRP94 and its mRNA in mammary glands from cows at various developmental stages of hormonally induced lactation [3].
• The coding nucleotide sequence and the deduced amino acid sequence of bovine GRP94 shared 94.2-88.4% and 98.1-96.5% identity with those of other mammalian species, respectively [3].
• The primary structure contained a carboxyl-terminal signal sequence for retention in the endoplasmic reticulum, six potential sites for N-linked glycosylation and two potential adenosine 5'-triphosphate binding sites, similar to other mammalian and avian GRP94 homologues [3].
• We isolated and sequenced cDNA clones encoding a 94-kDa glucose-regulated protein (GRP94) from a cDNA library constructed using bovine (Bos taurus) mammary gland poly(A)(+) RNA [3].

Anatomical context of TRA1

• A third major testes protein of 97 kDa was also isolated with this protocol and was found to be homologous to the 94-kDa glucose-regulated protein [4].

Associations of TRA1 with chemical compounds

• GRP94 was detectable in a 50 kDa form in control cells but was detected as a 94 kDa form upon amino acid deprivation which was further enhanced upon inclusion of phenylalanine [5].

Analytical, diagnostic and therapeutic context of TRA1

• In Northern blot hybridization using a cDNA probe from the bovine GRP94 cDNA sequence, a transcript 3.0 kb in size was detected [3].
• Molecular cloning of bovine (Bos taurus) cDNA encoding a 94-kDa glucose-regulated protein and developmental changes in its mRNA and protein content in the mammary gland [3].

References