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Gene Review

mas  -  masquerade

Drosophila melanogaster

Synonyms: CG15002, Dmel\CG15002, SPH79, c-SPH79
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High impact information on mas

  • We propose that mas acts via its modified serine protease motif, either as a novel adhesion molecule and/or as a competitive antagonist of serine proteases, to stabilize muscle attachment [1].
  • During embryonic development, the mas amino- and carboxy-terminal polypeptides are differentially localized [1].
  • This mutant phenotype suggests that mas normally acts to stabilize cell-matrix interaction and represents a novel functional and limiting component in the adhesion process. mas encodes a 1047-amino-acid preproprotein that is further processed by proteolytic cleavage to generate two polypeptides [1].
  • The evolutionary tree obtained shows that the visual pigment genes and mas oncogene form one cluster and that the receptor genes form another [2].
  • Total loss of mas function is lethal and results in aberrations in the embryonic central and peripheral nervous systems, consistent with a role in axonal guidance [3].

Biological context of mas

  • This Tenebrio masquerade-like serine proteinase homologue (Tm-mas) contains a trypsin-like serine proteinase domain in the C-terminal region, except for the substitution of Ser to Gly at the active site triad, and a disulfide-knotted domain at the amino-terminal region [4].

Anatomical context of mas

  • The55-kDa zymogen form of Tm-mas was detected in the hemolymph when PO activity was not evident [4].

Regulatory relationships of mas

  • This suggests that the purified 45-kDa Tm-mas is an activated form of pro-PO activating factor [4].

Other interactions of mas

  • Furthermore, when Tenebrio hemolymph was incubated with Ca2+ and beta-1,3-glucan, the conversion of pro-PO to PO and the 55-kDa zymogen Tm-mas to the 45-kDa protein, was faster than in the presence of Ca2+ only [4].


  1. Masquerade: a novel secreted serine protease-like molecule is required for somatic muscle attachment in the Drosophila embryo. Murugasu-Oei, B., Rodrigues, V., Yang, X., Chia, W. Genes Dev. (1995) [Pubmed]
  2. Adaptive evolution of G-protein coupled receptor genes. Yokoyama, S., Isenberg, K.E., Wright, A.F. Mol. Biol. Evol. (1989) [Pubmed]
  3. Mutations in masquerade, a novel serine-protease-like molecule, affect axonal guidance and taste behavior in Drosophila. Murugasu-Oei, B., Balakrishnan, R., Yang, X., Chia, W., Rodrigues, V. Mech. Dev. (1996) [Pubmed]
  4. A zymogen form of masquerade-like serine proteinase homologue is cleaved during pro-phenoloxidase activation by Ca2+ in coleopteran and Tenebrio molitor larvae. Lee, K.Y., Zhang, R., Kim, M.S., Park, J.W., Park, H.Y., Kawabata, S., Lee, B.L. Eur. J. Biochem. (2002) [Pubmed]
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