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Gene Review:

Sec1 - secretory blood group 1

Mus musculus

Synonyms: Alpha(1,2)FT 3, Fucosyltransferase 10, Fut10, Fut3, GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 3, ...

Lin, B. et al., Riento, K. et al., Gissen, P. et al., Rajasekariah, P. et al., Lehtonen, S. et al., et al.

Rajasekariah, Eyre, Stanley, Walls, Sutherland,

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High impact information on Sec1

Vps33p homologues contain a Sec1 domain and belong to the family of Sec1/Munc18 (SM) proteins that regulate fusion of membrane-bound organelles and interact with other vps proteins and also SNARE proteins that execute membrane fusion in all cells [1].
We have previously identified three mammalian Sec1/Munc-18 homologues in adipocytes (Tellam, J. T., McIntosh, S., and James, D. E. (1995) J. Biol. Chem. 270, 5857-5863) [2].
Three SM (Sec1/Munc18) proteins are present in mouse platelets (Munc18a, 18b and 18c) and each potentially regulates exocytosis via modulation of their cognate syntaxin binding partner [3].
We have analyzed the expression patterns of vesicle-docking proteins of the syntaxin family in mouse kidney, focusing on syntaxin 3 and its interaction partner, the Sec1-related Munc-18-2 [4].
We have isolated a novel cDNA clone from human leucocyte cDNA library, encoding a Sec1p-like vacuolar protein sorting (h1Vps45) which is believed to be implicated in vesicular transportation [5].

Biological context of Sec1

MFUT-I, -II, and -III exhibited sequence homology with the human H (78.4%), Se (79.0%), and Sec1 (74.9%) gene products, respectively [6].

Anatomical context of Sec1

Sec1-related proteins are involved in docking and fusion of transport vesicles in eukaryotic cells [7].
Here we report the cloning and molecular characterization of a Sec1-related protein expressed in the MDCK epithelial cell line [7].
Recovery of somatosensory orientation after unilateral electrolytic lesions of globus pallidus was studied in two inbred strains of mice (C57BL/6, Sec 1/ReJ) [8].

Physical interactions of Sec1

These results identified Munc-18-2 as a predominantly epithelial vesicle-transport protein with a polarized distribution and provided novel in vivo evidence for the association of Sec1-related proteins with members of the syntaxin family [7].

References

Comparative evolutionary analysis of VPS33 homologues: genetic and functional insights. Gissen, P., Johnson, C.A., Gentle, D., Hurst, L.D., Doherty, A.J., O'Kane, C.J., Kelly, D.A., Maher, E.R. Hum. Mol. Genet. (2005) [Pubmed]
Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4. Tellam, J.T., Macaulay, S.L., McIntosh, S., Hewish, D.R., Ward, C.W., James, D.E. J. Biol. Chem. (1997) [Pubmed]
Platelets from Munc18c heterozygous mice exhibit normal stimulus-induced release. Schraw, T.D., Crawford, G.L., Ren, Q., Choi, W., Thurmond, D.C., Pessin, J., Whiteheart, S.W. Thromb. Haemost. (2004) [Pubmed]
Syntaxin 3 and Munc-18-2 in epithelial cells during kidney development. Lehtonen, S., Riento, K., Olkkonen, V.M., Lehtonen, E. Kidney Int. (1999) [Pubmed]
Molecular cloning and characterization of a cDNA encoding the human leucocyte vacuolar protein sorting (h1Vps45). Rajasekariah, P., Eyre, H.J., Stanley, K.K., Walls, R.S., Sutherland, G.R. Int. J. Biochem. Cell Biol. (1999) [Pubmed]
Characterization of three members of murine alpha1,2-fucosyltransferases: change in the expression of the Se gene in the intestine of mice after administration of microbes. Lin, B., Saito, M., Sakakibara, Y., Hayashi, Y., Yanagisawa, M., Iwamori, M. Arch. Biochem. Biophys. (2001) [Pubmed]
A sec1-related vesicle-transport protein that is expressed predominantly in epithelial cells. Riento, K., Jäntti, J., Jansson, S., Hielm, S., Lehtonen, E., Ehnholm, C., Keränen, S., Olkkonen, V.M. Eur. J. Biochem. (1996) [Pubmed]
Strain differences in recovery from sensorimotor neglect after unilateral globus pallidus lesions in mice. Siegfried, B., Gozzo, S. Physiol. Behav. (1982) [Pubmed]

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