Selected Publication:

SHR Neuro Cancer Cardio Lipid Metab Microb

Lundin, C; Nordström, R; Wagner, K; Windpassinger, C; Andersson, H; von Heijne, G; Nilsson, I.
Membrane topology of the human seipin protein.
FEBS Lett. 2006; 580(9):2281-2284 Doi: 10.1016/j.febslet.2006.03.040 [OPEN ACCESS]
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Co-authors Med Uni Graz

Wagner Klaus

Windpassinger Christian

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Abstract:

The Berardinelli-Seip congenital lipodystrophy type 2 (BSCL2) gene encodes an integral membrane protein, called seipin, of unknown function localized to the endoplasmic reticulum of eukaryotic cells. Seipin is associated with the heterogeneous genetic disease BSCL2, and mutations in an N-glycosylation motif links the protein to two other disorders, autosomal-dominant distal hereditary motor neuropathy type V and Silver syndrome. Here, we report a topological study of seipin using an in vitro topology mapping assay. Our results suggest that the predominant form of seipin is 462 residues long and has an N(cyt)-C(cyt) orientation with a long luminal loop between the two transmembrane helices.

Find related publications in this database (using NLM MeSH Indexing)

Amino Acid Motifs - genetics

Chromosome Disorders - genetics

Diabetes Mellitus, Lipoatrophic - genetics

Endoplasmic Reticulum - genetics

GTP-Binding Protein gamma Subunits - genetics

Humans - genetics

Intracellular Membranes - metabolism

Protein Modification, Translational - genetics

Protein Structure, Tertiary - genetics

Find related publications in this database (Keywords)

seipin

N-linked glycosylation

oligosaccharyl transferase

topology mapping

BCSL gene

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