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Membrane topology of the human seipin protein
Author(s) -
Lundin Carolina,
Nordström Rickard,
Wagner Klaus,
Windpassinger Christian,
Andersson Helena,
von Heijne Gunnar,
Nilsson IngMarie
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.040
Subject(s) - topology (electrical circuits) , membrane topology , membrane protein , chemistry , membrane , mathematics , biochemistry , combinatorics
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.