High impact information on Rcn1

• The longer mRNA contains an open reading frame that shares homology with mouse reticulocalbin whereas the shorter one encodes a truncated version lacking the N-terminal signal peptide-like sequence [1].
• Reticulocalbin is a luminal protein of the endoplasmic reticulum with an M(r) of 44,000 as revealed by biochemical analysis and immunofluorescence staining [2].
• Reticulocalbin, a novel endoplasmic reticulum resident Ca(2+)-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence [2].
• Glutathione peroxidase, ferritin, and alphaB-crystallin were upregulated 2-fold, and reticulocalbin was upregulated 6-fold in the resistant cells. alphaA-crystallin was downregulated 5-fold, while aldose reductase and mitochondrial gene products were unchanged [3].
• Some of these identified proteins had structural or enzymatic functions while others had only recently been discovered, including a newly reported Hsp 70 class member and a novel calcium-binding protein, reticulocalbin [4].

Biological context of Rcn1

• This mouse presents a mutation in chromosome 2 which affects the gene Pax6 and other nearby genes, such as the Wt1 gene and the gene of the Reticulocalbin [5].
• Loss of the reticulocalbin gene could contribute to the early lethality of SeyH and SeyDey homozygotes [6].
• The mouse reticulocalbin gene is also shown to map to the region of conserved synteny on mouse chromosome 2 and to be deleted in the Small eye Harwell (SeyH) mutation [6].
• The sequence of this clone revealed a novel protein with 95% identity in amino acid sequence to the mouse reticulocalbin, indicating that this molecule has been evolutionarily conserved in mammals [7].
• Southern blot analysis of mouse genomic DNA revealed that there is a single copy of the reticulocalbin gene per haploid genome [8].

Anatomical context of Rcn1

• When hepatic cytosols and microsomes from calves treated with a combination of GPAs were analyzed by 2-DE, we found changes in the expression of two proteins, which we identified as adenosine kinase and reticulocalbin [9].

Physical interactions of Rcn1

• Thus, reticulocalbin differs from the cytosolic Ca(2+)-binding protein calbindin D28 which also has six EF-hand motif domains, but the gene for which is divided into 11 exons [8].

References