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Seipin is associated with the heterogeneous genetic disease BSCL2, and mutations in an N\u2010glycosylation motif links the protein to two other disorders, autosomal\u2010dominant 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<jats:sub>cyt<\/jats:sub>\u2013C<jats:sub>cyt<\/jats:sub> orientation with a long luminal loop between the two transmembrane helices.<\/jats:p>","DOI":"10.1016\/j.febslet.2006.03.040","type":"journal-article","created":{"date-parts":[[2006,3,28]],"date-time":"2006-03-28T07:10:13Z","timestamp":1143529813000},"page":"2281-2284","source":"Crossref","is-referenced-by-count":119,"title":["Membrane topology of the human seipin protein"],"prefix":"10.1002","volume":"580","author":[{"given":"Carolina","family":"Lundin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rickard","family":"Nordstr\u00f6m","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Klaus","family":"Wagner","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Windpassinger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Helena","family":"Andersson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gunnar","family":"von Heijne","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"IngMarie","family":"Nilsson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,3,27]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.2337\/diabetes.52.6.1573"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/ng1313"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1093\/brain\/awh232"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00439-003-1021-6"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0304-4165(99)00165-8"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/ng1581"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1038\/ng585"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.15.7134"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.molmed.2004.07.009"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00281625"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.9.11.5073"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.126.5.1127"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.65.1.147-154.1991"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.65.8.4107-4113.1991"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1038\/nbt1291-1356"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.2000.4315"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.49.34993"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.5.2816"},{"key":"e_1_2_6_20_1","first-page":"17","article-title":"Structural aspects of transmembrane a-helices","volume":"163","author":"von Heijne G.","year":"1998","journal-title":"Acta Physiol. 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