Seipin is a protein of approximately 400 residues, in humans, which is the product of a gene homologous to the murine guanine nucleotide-binding protein (G protein) gamma-3 linked gene. This gene is implicated in the regulation of body fat distribution and insulin resistance and particularly in the auto-immune disease Berardinelli-Seip congenital lipodystrophy type 2. Seipin has no similarity with other known proteins or consensus motifs that might predict its function, but it is predicted to contain two transmembrane domains at residues 28-49 and 237-258, in human, and a third transmembrane domain might be present at residues 155-173. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V [[cite:PUB00044745]].
","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Seipin","extract":"Seipin is a homo-oligomeric integral membrane protein in the endoplasmic reticulum (ER) that concentrates at junctions with cytoplasmic lipid droplets (LDs). Alternatively, seipin can be referred to as Berardinelli–Seip congenital lipodystrophy type 2 protein (BSCL2), and it is encoded by the corresponding gene of the same name, i.e. BSCL2. At protein level, seipin is expressed in cortical neurons in the frontal lobes, as well as motor neurons in the spinal cord. It is highly expressed in areas like the brain, testis and adipose tissue. Seipin's function is still unclear but it has been localized close to lipid droplets, and cells knocked out in seipin have anomalous droplets. Hence, recent evidence suggests that seipin plays a crucial role in lipid droplet biogenesis.
","thumbnail":null}],"literature":{"PUB00044745":{"PMID":11479539,"ISBN":null,"volume":"28","issue":"4","year":2001,"title":"Identification of the gene altered in Berardinelli-Seip congenital lipodystrophy on chromosome 11q13.","URL":null,"raw_pages":"365-70","medline_journal":"Nat Genet","ISO_journal":"Nat. Genet.","authors":["Magre J","Delepine M","Khallouf E","Gedde-Dahl T Jr","Van Maldergem L","Sobel E","Papp J","Meier M","Megarbane A","Bachy A","Verloes A","d'Abronzo FH","Seemanova E","Assan R","Baudic N","Bourut C","Czernichow P","Huet F","Grigorescu F","de Kerdanet M","Lacombe D","Labrune P","Lanza M","Loret H","Matsuda F","Navarro J","Nivelon-Chevalier A","Polak M","Robert JJ","Tric P","Tubiana-Rufi N","Vigouroux C","Weissenbach J","Savasta S","Maassen JA","Trygstad O","Bogalho P","Freitas P","Medina JL","Bonnicci F","Joffe BI","Loyson G","Panz VR","Raal FJ","O'Rahilly S","Stephenson T","Kahn CR","Lathrop M","Capeau J; BSCL Working Group."],"DOI_URL":"http://dx.doi.org/10.1038/ng585"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":102,"interactions":0,"matches":4729,"pathways":0,"proteins":4646,"proteomes":2764,"sets":0,"structural_models":{"alphafold":3811},"structures":4,"taxa":7460},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":112,"alignment:full":3418},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}