ARMET is a soluble ER protein induced by the unfolded protein response via ERSE-II element

Cell Struct Funct. 2007;32(1):41-50. doi: 10.1247/csf.07001. Epub 2007 May 14.


Arginine rich, mutated in early stage of tumors (ARMET) was first identified as a human gene highly mutated in a variety of cancers. However, little is known about the characteristics of the ARMET protein and its expression. We identified ARMET as a gene upregulated by endoplasmic reticulum (ER) stress. Here, we show that the mouse homologue of ARMET is an 18-kDa soluble ER protein that is mature after cleavage of a signal sequence and has four intramolecular disulfide bonds, including two in CXXC sequences. ER stress stimulated ARMET expression, and the expression patterns of ARMET mRNA and protein in mouse tissues were similar to those of Grp78, an Hsp70-family protein required for quality control of proteins in the ER. A reporter gene assay using a mouse ARMET promoter revealed that the unfolded protein response of the ARMET gene is regulated by an ERSE-II element whose sequence is identical to that of the HERP gene. ARMET is the second fully characterized ERSE-II-dependent gene and likely contributes to quality control of proteins in the ER.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • BALB 3T3 Cells / cytology
  • BALB 3T3 Cells / metabolism
  • Base Sequence
  • Cell Line
  • Endoplasmic Reticulum / genetics*
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum Chaperone BiP
  • Gene Expression Regulation
  • Mice
  • Molecular Sequence Data
  • Nerve Growth Factors
  • Promoter Regions, Genetic
  • Proteins / chemistry
  • Proteins / genetics*
  • Proteins / isolation & purification
  • Proteins / metabolism*
  • Response Elements*
  • Solubility


  • Endoplasmic Reticulum Chaperone BiP
  • HSPA5 protein, human
  • Hspa5 protein, mouse
  • MANF protein, mouse
  • Nerve Growth Factors
  • Proteins