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Gene Review

STOM  -  stomatin

Homo sapiens

Synonyms: BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, ...
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Disease relevance of STOM


High impact information on STOM

  • Whereas neither the central, stomatin-like domain of MEC-2 nor human stomatin retained the activity of full-length MEC-2, both produced amiloride-sensitive currents with MEC-4d [4].
  • Its product, podocin, is a new member of the stomatin family, which consists of hairpin-like integral membrane proteins with intracellular NH(2)- and COOH-termini [5].
  • Band 3 and stomatin, which reflect the bulk mass of erythrocyte DRM proteins, and all tested non-DRM proteins are excluded from the vacuolar parasite [6].
  • This technique revealed that, in fact, some red cells did show positive stomatin immunoreactivity; and consistent with this result, Western blot analysis of the red cell membranes confirmed that about one twentieth to one fiftieth of the normal amount of stomatin was in fact present [7].
  • The deficiency of stomatin from red cells appears to be due to a loss of stomatin from these red cells on maturation in the bone marrow and in the circulation [7].

Biological context of STOM

  • There is also evidence that stomatin is linked to the cortical actin cytoskeleton, suggesting a role in cortical morphogenesis of the cell [8].
  • The human gene EPB72 coding for the band 7 integral membrane protein, a major protein of the erythrocyte membrane, was isolated from a genomic DNA library and characterized [9].
  • Spanning approximately 30 kb, the human EPB72 gene comprises seven exons ranging from 73 to 2331 bp; intron sizes range from 970 to approximately 11,200 bp [9].
  • A mixed population of Clone 9 cells stably transfected with a plasmid overexpressing the mouse stomatin exhibited 30 +/- 3% reduction in the basal rate of glucose transport compared to control cells or cells stably transfected with the empty vector [10].
  • Although the murine knock-out is without phenotype, we have identified a family showing a splicing defect in the stomatin mRNA, in which affected children showed a catastrophic multisystem disease not inconsistent with the now-known wide tissue distribution of stomatin [11].

Anatomical context of STOM


Associations of STOM with chemical compounds

  • Whereas stomatin was partly soluble in Triton X-100, it was insoluble in the detergents Lubrol and 3-[(3-cholamidopropyl)dimethylamonio]-1-propyl sulfonate (CHAPS) [12].
  • In overhydrated hereditary stomatocytosis (OHSt), Coomassie- and silver-stained polyacrylamide gels show an apparently complete deficit of the 32-kDa membrane protein, stomatin [7].
  • Given the organization of stomatin into homo-oligomers, the presence of multiple palmitate chains is likely to increase greatly the affinity of these oligomers for the membrane and perhaps particular lipid domains within it [14].
  • Cysteine 29 is the major palmitoylation site on stomatin [14].
  • The 31 kDa membrane protein stomatin was metabolically labeled with tritiated palmitic acid in the human amniotic cell line UAC and immunoprecipitated [14].

Other interactions of STOM

  • Stomatin, the flotillins, and CD36 were exclusively present in this lipid-raft fraction [12].
  • We isolated a 40 kDa integral membrane protein (p40) from human erythrocyte ghosts by affinity chromatography, using a C-terminal peptide of stomatin, and obtained partial sequences which enabled us to isolate two full-length cDNAs from human bone marrow and fetal brain cDNA libraries [15].
  • Magnetic-activated cell separation studies, using beads to which an anti-transferrin receptor antibody was conjugated, confirmed that in OHSt there was a correspondence between expression of stomatin and the transferrin receptor [7].
  • Podocin is a stomatin protein family member with a predicted hairpin-like structure localizing to the insertion site of the slit diaphragm of podocytes, the visceral glomerular epithelial cells of the kidney [16].
  • The predicted polypeptide sequence of STOML2 could be delineated into three major domains: an N-terminal alpha-helical region; a domain with significant similarity to a 172 amino acid region of the HSA stomatin polypeptide, composed of an alternating alpha-helical and beta-sheet structure and a C-terminal domain that was mostly alpha-helical [17].

Analytical, diagnostic and therapeutic context of STOM


  1. A novel thermostable membrane protease forming an operon with a stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus horikoshii. Yokoyama, H., Matsui, I. J. Biol. Chem. (2005) [Pubmed]
  2. The gene for human erythrocyte membrane protein band 7.2 (EPB72) maps to 9q33-q34 centromeric to the Philadelphia chromosome translocation breakpoint region. Gallagher, P.G., Upender, M., Ward, D.C., Forget, B.G. Genomics (1993) [Pubmed]
  3. The curious genomic path from leaky red cell to nephrotic kidney. Stewart, G.W., Fricke, B. Nephron. Physiology [electronic resource]. (2003) [Pubmed]
  4. MEC-2 regulates C. elegans DEG/ENaC channels needed for mechanosensation. Goodman, M.B., Ernstrom, G.G., Chelur, D.S., O'Hagan, R., Yao, C.A., Chalfie, M. Nature (2002) [Pubmed]
  5. Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin. Schwarz, K., Simons, M., Reiser, J., Saleem, M.A., Faul, C., Kriz, W., Shaw, A.S., Holzman, L.B., Mundel, P. J. Clin. Invest. (2001) [Pubmed]
  6. Erythrocyte detergent-resistant membrane proteins: their characterization and selective uptake during malarial infection. Murphy, S.C., Samuel, B.U., Harrison, T., Speicher, K.D., Speicher, D.W., Reid, M.E., Prohaska, R., Low, P.S., Tanner, M.J., Mohandas, N., Haldar, K. Blood (2004) [Pubmed]
  7. The "stomatin" gene and protein in overhydrated hereditary stomatocytosis. Fricke, B., Argent, A.C., Chetty, M.C., Pizzey, A.R., Turner, E.J., Ho, M.M., Iolascon, A., von Düring, M., Stewart, G.W. Blood (2003) [Pubmed]
  8. Oligomeric nature of the integral membrane protein stomatin. Snyers, L., Umlauf, E., Prohaska, R. J. Biol. Chem. (1998) [Pubmed]
  9. The organization of the gene (EPB72) encoding the human erythrocyte band 7 integral membrane protein (protein 7.2b). Unfried, I., Entler, B., Prohaska, R. Genomics (1995) [Pubmed]
  10. Association of stomatin (band 7.2b) with Glut1 glucose transporter. Zhang, J.Z., Hayashi, H., Ebina, Y., Prohaska, R., Ismail-Beigi, F. Arch. Biochem. Biophys. (1999) [Pubmed]
  11. Eukaryotic and prokaryotic stomatins: the proteolytic link. Green, J.B., Fricke, B., Chetty, M.C., von Düring, M., Preston, G.F., Stewart, G.W. Blood Cells Mol. Dis. (2004) [Pubmed]
  12. Stomatin is a major lipid-raft component of platelet alpha granules. Mairhofer, M., Steiner, M., Mosgoeller, W., Prohaska, R., Salzer, U. Blood (2002) [Pubmed]
  13. The presence of stomatin in detergent-insoluble domains of neutrophil granule membranes. Feuk-Lagerstedt, E., Samuelsson, M., Mosgoeller, W., Movitz, C., Rosqvist, A., Bergström, J., Larsson, T., Steiner, M., Prohaska, R., Karlsson, A. J. Leukoc. Biol. (2002) [Pubmed]
  14. Cysteine 29 is the major palmitoylation site on stomatin. Snyers, L., Umlauf, E., Prohaska, R. FEBS Lett. (1999) [Pubmed]
  15. Isolation, molecular characterization, and tissue-specific expression of a novel putative G protein-coupled receptor. Mayer, H., Salzer, U., Breuss, J., Ziegler, S., Marchler-Bauer, A., Prohaska, R. Biochim. Biophys. Acta (1998) [Pubmed]
  16. Molecular basis of the functional podocin-nephrin complex: mutations in the NPHS2 gene disrupt nephrin targeting to lipid raft microdomains. Huber, T.B., Simons, M., Hartleben, B., Sernetz, L., Schmidts, M., Gundlach, E., Saleem, M.A., Walz, G., Benzing, T. Hum. Mol. Genet. (2003) [Pubmed]
  17. A novel member of the STOMATIN/EPB72/mec-2 family, stomatin-like 2 (STOML2), is ubiquitously expressed and localizes to HSA chromosome 9p13.1. Owczarek, C.M., Treutlein, H.R., Portbury, K.J., Gulluyan, L.M., Kola, I., Hertzog, P.J. Cytogenet. Cell Genet. (2001) [Pubmed]
  18. The gene coding for erythrocyte protein band 7.2b (EPB72) is located in band q34.1 of human chromosome 9. Westberg, J.A., Entler, B., Prohaska, R., Schröder, J.P. Cytogenet. Cell Genet. (1993) [Pubmed]
  19. Identification of a novel member of the snail/Gfi-1 repressor family, mlt 1, which is methylated and silenced in liver tumors of SV40 T antigen transgenic mice. Tateno, M., Fukunishi, Y., Komatsu, S., Okazaki, Y., Kawai, J., Shibata, K., Itoh, M., Muramatsu, M., Held, W.A., Hayashizaki, Y. Cancer Res. (2001) [Pubmed]
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