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Gene Review

LMAN2  -  lectin, mannose-binding 2

Homo sapiens

Synonyms: C5orf8, GP36B, Glycoprotein GP36b, Lectin mannose-binding 2, VIP36, ...
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High impact information on LMAN2

  • Furthermore, we provide evidence that internalization of VIP36, a protein that cycles between plasma membrane and Golgi, is mediated by a signal at its C-terminus that matches the internalization consensus sequence [1].
  • VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells [2].
  • We speculate that VIP36 binds to sugar residues of glycosphingolipids and/or glycosylphosphatidyl-inositol anchors and might provide a link between the extracellular/luminal face of glycolipid rafts and the cytoplasmic protein segregation machinery [2].
  • The vesicular integral protein of 36 kDa (VIP36) is an intracellular animal lectin that acts as a putative cargo receptor, which recycles between the Golgi and the endoplasmic reticulum [3].
  • Although it is known that VIP36 interacts with glycoproteins carrying high mannose-type oligosaccharides, detailed analyses of the sugar-binding specificity that discriminates isomeric oligosaccharide structures have not yet been performed [3].

Biological context of LMAN2

  • Cycling of VIP36 is suggested by colocalisation with anterograde cargo trapped in pre-Golgi structures and modification of its N-linked carbohydrate by glycosylation enzymes of medial Golgi cisternae [4].
  • In addition to the well-understood role of mannose 6-phosphate receptor in lysosomal protein sorting, the vesicular integral protein of 36 kDa (VIP36) functions as a sorting receptor by recognizing high-mannose type glycans containing alpha1-->2Man residues for transport from Golgi to the cell surface in polarized epithelial cells [5].

Anatomical context of LMAN2


Associations of LMAN2 with chemical compounds

  • VIPL is a high-mannose type I membrane glycoprotein with similar domain organization as VIP36 [6].
  • Furthermore, after brefeldin A treatment VIP36 is segregated from resident Golgi proteins and codistributes with ER-Golgi recycling proteins [4].

Physical interactions of LMAN2


Regulatory relationships of LMAN2


Other interactions of LMAN2

  • The profiles were generated from linear sequence motifs of the human L-type lectin-like membrane proteins ERGIC-53, ERGL, and VIP36 and by optimal alignment of the entire carbohydrate recognition domain of these proteins [6].

Analytical, diagnostic and therapeutic context of LMAN2


  1. A novel endocytosis signal related to the KKXX ER-retrieval signal. Itin, C., Kappeler, F., Linstedt, A.D., Hauri, H.P. EMBO J. (1995) [Pubmed]
  2. VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. Fiedler, K., Parton, R.G., Kellner, R., Etzold, T., Simons, K. EMBO J. (1994) [Pubmed]
  3. Sugar-binding properties of VIP36, an intracellular animal lectin operating as a cargo receptor. Kamiya, Y., Yamaguchi, Y., Takahashi, N., Arata, Y., Kasai, K., Ihara, Y., Matsuo, I., Ito, Y., Yamamoto, K., Kato, K. J. Biol. Chem. (2005) [Pubmed]
  4. VIP36 localisation to the early secretory pathway. Füllekrug, J., Scheiffele, P., Simons, K. J. Cell. Sci. (1999) [Pubmed]
  5. Intracellular lectins associated with N-linked glycoprotein traffic. Yamashita, K., Hara-Kuge, S., Ohkura, T. Biochim. Biophys. Acta (1999) [Pubmed]
  6. Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum protein. Nufer, O., Mitrovic, S., Hauri, H.P. J. Biol. Chem. (2003) [Pubmed]
  7. Lectins and traffic in the secretory pathway. Hauri, H., Appenzeller, C., Kuhn, F., Nufer, O. FEBS Lett. (2000) [Pubmed]
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