seipin isoform X1 [Gopherus flavomarginatus]
seipin( domain architecture ID 10536034)
seipin is a putative adipose-regulatory protein that is involved in lipid droplets formation
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
Seipin | pfam06775 | Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ... |
42-242 | 2.44e-76 | ||||
Putative adipose-regulatory protein (Seipin); 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. : Pssm-ID: 462007 Cd Length: 195 Bit Score: 235.12 E-value: 2.44e-76
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Name | Accession | Description | Interval | E-value | ||||
Seipin | pfam06775 | Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ... |
42-242 | 2.44e-76 | ||||
Putative adipose-regulatory protein (Seipin); 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. Pssm-ID: 462007 Cd Length: 195 Bit Score: 235.12 E-value: 2.44e-76
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Seipin_BSCL2_like | cd23995 | Homo sapiens Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane ... |
57-221 | 5.65e-68 | ||||
Homo sapiens Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the endoplasmic reticulum (ER) that concentrates at junctions with cytoplasmic lipid droplets (LDs). It acts as a cell-autonomous regulator of lipolysis essential for adipocyte differentiation. Seipin is predicted to contain two transmembrane domains at N-terminus and C-terminus, respectively. Human seipin, also called Bernardinelli-Seip congenital lipodystrophy type 2 protein (BSCL2), may contain a third transmembrane domain in the middle region. Mutations in the seipin gene underlie Human congenital generalized lipodystrophy. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V. Human seipin exists as an undecamer, and this oligomerization state is critical for its physiological function. Seipin homologs from fungi, plants and insects are also included in this family. There are three SEIPIN homologs in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3. Pssm-ID: 467829 Cd Length: 162 Bit Score: 212.48 E-value: 5.65e-68
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Name | Accession | Description | Interval | E-value | ||||
Seipin | pfam06775 | Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ... |
42-242 | 2.44e-76 | ||||
Putative adipose-regulatory protein (Seipin); 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. Pssm-ID: 462007 Cd Length: 195 Bit Score: 235.12 E-value: 2.44e-76
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Seipin_BSCL2_like | cd23995 | Homo sapiens Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane ... |
57-221 | 5.65e-68 | ||||
Homo sapiens Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the endoplasmic reticulum (ER) that concentrates at junctions with cytoplasmic lipid droplets (LDs). It acts as a cell-autonomous regulator of lipolysis essential for adipocyte differentiation. Seipin is predicted to contain two transmembrane domains at N-terminus and C-terminus, respectively. Human seipin, also called Bernardinelli-Seip congenital lipodystrophy type 2 protein (BSCL2), may contain a third transmembrane domain in the middle region. Mutations in the seipin gene underlie Human congenital generalized lipodystrophy. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V. Human seipin exists as an undecamer, and this oligomerization state is critical for its physiological function. Seipin homologs from fungi, plants and insects are also included in this family. There are three SEIPIN homologs in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3. Pssm-ID: 467829 Cd Length: 162 Bit Score: 212.48 E-value: 5.65e-68
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Seipin | cd23993 | Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the ... |
57-221 | 4.06e-67 | ||||
Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the endoplasmic reticulum (ER) that concentrates at junctions with cytoplasmic lipid droplets (LDs). It acts as a cell-autonomous regulator of lipolysis essential for adipocyte differentiation. Seipin is predicted to contain two transmembrane domains at N-terminus and C-terminus, respectively. Human seipin, also called Bernardinelli-Seip congenital lipodystrophy type 2 protein (BSCL2), may contain a third transmembrane domain in the middle region. Mutations in the seipin gene underlie human congenital generalized lipodystrophy. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V. Seipin homologs from fungi, plants, and insects are also included in this family. There are three SEIPIN homologs in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3. Saccharomyces cerevisiae Seipin (Sei1) is also called few lipid droplets protein 1 (Fld1p). Similar to their animal homologs, plant and yeast seipins also play roles in lipid droplet (LD) biogenesis. Human seipin exists as an undecamer, and this oligomerization state is critical for its physiological function. In contrast to Human seipin, S. cerevisiae Sei1-mediated LD formation depends on Ldb16, a yeast specific binding partner. Sei1 forms a homodecameric ring that scaffolds and positions Ldb16. Pssm-ID: 467827 Cd Length: 163 Bit Score: 210.23 E-value: 4.06e-67
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Blast search parameters | ||||
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