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Gene Review

Mal  -  mal, T-cell differentiation protein

Rattus norvegicus

Synonyms: 17 kDa myelin vesicular protein, MVP17, Mvp17, Myelin and lymphocyte protein, NS 3, ...
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Disease relevance of Mal

  • SAR and pharmacokinetic studies on phenethylamide inhibitors of the hepatitis C virus NS3/NS4A serine protease [1].

High impact information on Mal

  • We have isolated a rat cDNA, initially denominated NS 3, that is mainly expressed in the myelinating cells of the nervous system, the oligodendrocytes and Schwann cells [2].
  • The putative NS 3 protein lacks a N-terminal hydrophobic leader sequence and has no consensus sequence for N-linked glycosylation [2].
  • Sequence analysis showed that NS 3 is the rat homolog of a human gene called MAL that was cloned from, and is expressed in various T-cell lines [2].
  • The expression of Mal mRNA is highly restricted to the brain and testis [3].
  • Probing of a human complementary DNA library with anti-Ma serum resulted in the cloning of a gene that encodes a novel 37 kDa protein (Mal) [3].

Biological context of Mal


Anatomical context of Mal

  • A developmentally regulated protein, MVP17 (myelin vesicular protein of 17 kDa), was identified [4].
  • Expression of full-length constructs of MVP17/rMAL in COS-7 cells resulted in an enlargement of transfected COS-7 cells, consistent with a proposed role of rMAL in vesicular trafficking [6].

Other interactions of Mal

  • The MAL (MAL, MVP17, VIP17) proteolipid, an integral membrane protein present in DIGs in mature oligodendrocytes, has been proposed as a component of the machinery for DIG-mediated transport in a restricted pattern of cell types including myelinating cells [7].


  1. SAR and pharmacokinetic studies on phenethylamide inhibitors of the hepatitis C virus NS3/NS4A serine protease. Malancona, S., Colarusso, S., Ontoria, J.M., Marchetti, A., Poma, M., Stansfield, I., Laufer, R., Di Marco, A., Taliani, M., Verdirame, M., Gonzalez-Paz, O., Matassa, V.G., Narjes, F. Bioorg. Med. Chem. Lett. (2004) [Pubmed]
  2. Characterization of a rat gene, rMAL, encoding a protein with four hydrophobic domains in central and peripheral myelin. Schaeren-Wiemers, N., Valenzuela, D.M., Frank, M., Schwab, M.E. J. Neurosci. (1995) [Pubmed]
  3. Ma1, a novel neuron- and testis-specific protein, is recognized by the serum of patients with paraneoplastic neurological disorders. Dalmau, J., Gultekin, S.H., Voltz, R., Hoard, R., DesChamps, T., Balmaceda, C., Batchelor, T., Gerstner, E., Eichen, J., Frennier, J., Posner, J.B., Rosenfeld, M.R. Brain (1999) [Pubmed]
  4. Cloning and characterization of MVP17: a developmentally regulated myelin protein in oligodendrocytes. Kim, T., Fiedler, K., Madison, D.L., Krueger, W.H., Pfeiffer, S.E. J. Neurosci. Res. (1995) [Pubmed]
  5. Myelin glycosphingolipid/cholesterol-enriched microdomains selectively sequester the non-compact myelin proteins CNP and MOG. Kim, T., Pfeiffer, S.E. J. Neurocytol. (1999) [Pubmed]
  6. Subcellular localization and detergent solubility of MVP17/rMAL, a lipid raft-associated protein in oligodendrocytes and myelin. Kim, T., Pfeiffer, S.E. J. Neurosci. Res. (2002) [Pubmed]
  7. Thyroid hormone regulates the expression of the MAL proteolipid, a component of glycolipid-enriched membranes, in neonatal rat brain. Pombo, P.M., Ibarrola, N., Alonso, M.A., Rodríguez-Peña, A. J. Neurosci. Res. (1998) [Pubmed]
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