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Conserved domains on  [gi|2328689126|ref|XP_034109875|]
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LOW QUALITY PROTEIN: seipin-like [Drosophila albomicans]

Protein Classification

seipin( domain architecture ID 10536034)

seipin is a putative adipose-regulatory protein that is involved in lipid droplets formation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Seipin cd23993
Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the ...
 82-242 8.20e-85

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: 254.53  E-value: 8.20e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126  82 PPISHTRPVHMQFKTCLETSTPCTFPHAHVSLTKKQQLL--MVGQAYKVIVNIDMPESPQNLELGMFMVCAEMRDYDSML 159
Cdd:cd23993     1 PSNSHPLPVHNGVQTCLETSTPCTFPGAKVSLTKKSIPVgdMMGQKYDVNLQLYCPESPQNDHLGMFNVLIDVYRGPDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126 160 RGHSCRSAMMRYRSPLVRLFSTWALSPLYVLGWKEEFQKVPVEIFSRYLEERQHPITDVYVEIQSQKIQFYTVTLHIEAD 239
Cdd:cd23993    81 IFHSSRSIMCLYRSDLMSMQETEVQSGLSRLGVYEEEQLNTVEIEDKYSEESSYPTTSVFLEIESAQIQLYIHPLGIKAR 160


                  ...
gi 2328689126 240 FSG 242
Cdd:cd23993   161 FTG 163
 
Name Accession Description Interval E-value
Seipin cd23993
Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the ...
 82-242 8.20e-85

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: 254.53  E-value: 8.20e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126  82 PPISHTRPVHMQFKTCLETSTPCTFPHAHVSLTKKQQLL--MVGQAYKVIVNIDMPESPQNLELGMFMVCAEMRDYDSML 159
Cdd:cd23993     1 PSNSHPLPVHNGVQTCLETSTPCTFPGAKVSLTKKSIPVgdMMGQKYDVNLQLYCPESPQNDHLGMFNVLIDVYRGPDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126 160 RGHSCRSAMMRYRSPLVRLFSTWALSPLYVLGWKEEFQKVPVEIFSRYLEERQHPITDVYVEIQSQKIQFYTVTLHIEAD 239
Cdd:cd23993    81 IFHSSRSIMCLYRSDLMSMQETEVQSGLSRLGVYEEEQLNTVEIEDKYSEESSYPTTSVFLEIESAQIQLYIHPLGIKAR 160


                  ...
gi 2328689126 240 FSG 242
Cdd:cd23993   161 FTG 163
Seipin pfam06775
Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ...
 63-262 4.54e-79

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: 240.90  E-value: 4.54e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126  63 VLIIWLAVFIYAAFYYVYMPPISHTRPVHMQFKTCLEtstpctfPHAHVSLTKKQQLLMVGQAYKVIVNIDMPESPQNLE 142
Cdd:pfam06775   1 LLLLVLSVVAYGLFYYAYVPEPVLSRPLHFQYGTGSN-------PYATVSLTSRASLLPPGQPYDVSVELTLPESPYNLE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126 143 LGMFMVCAEMRDYDSMLRGHSCRSAMMRYRSPLVRLFSTWALSPLYVLGWKEEFQKVPVEIFSRYLEERQHPITDVYVEI 222
Cdd:pfam06775  74 LGNFMVRLELLSSNGKVLASSRRPAMLPYRSPLVRLLRTLLLLPPYLLGLREESQTLRVPMFESVVEGRENPPTSARVEI 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2328689126 223 QSQK-IQFYTVTLHIEADFSGLRYIMFNWPVLSAIVAISTN 262
Cdd:pfam06775 154 QSAGlLQIYSAELIFEARLPGLRYLMYNWPITSFVVGTALF 194
 
Name Accession Description Interval E-value
Seipin cd23993
Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the ...
 82-242 8.20e-85

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: 254.53  E-value: 8.20e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126  82 PPISHTRPVHMQFKTCLETSTPCTFPHAHVSLTKKQQLL--MVGQAYKVIVNIDMPESPQNLELGMFMVCAEMRDYDSML 159
Cdd:cd23993     1 PSNSHPLPVHNGVQTCLETSTPCTFPGAKVSLTKKSIPVgdMMGQKYDVNLQLYCPESPQNDHLGMFNVLIDVYRGPDEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126 160 RGHSCRSAMMRYRSPLVRLFSTWALSPLYVLGWKEEFQKVPVEIFSRYLEERQHPITDVYVEIQSQKIQFYTVTLHIEAD 239
Cdd:cd23993    81 IFHSSRSIMCLYRSDLMSMQETEVQSGLSRLGVYEEEQLNTVEIEDKYSEESSYPTTSVFLEIESAQIQLYIHPLGIKAR 160


                  ...
gi 2328689126 240 FSG 242
Cdd:cd23993   161 FTG 163
Seipin pfam06775
Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ...
 63-262 4.54e-79

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: 240.90  E-value: 4.54e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126  63 VLIIWLAVFIYAAFYYVYMPPISHTRPVHMQFKTCLEtstpctfPHAHVSLTKKQQLLMVGQAYKVIVNIDMPESPQNLE 142
Cdd:pfam06775   1 LLLLVLSVVAYGLFYYAYVPEPVLSRPLHFQYGTGSN-------PYATVSLTSRASLLPPGQPYDVSVELTLPESPYNLE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126 143 LGMFMVCAEMRDYDSMLRGHSCRSAMMRYRSPLVRLFSTWALSPLYVLGWKEEFQKVPVEIFSRYLEERQHPITDVYVEI 222
Cdd:pfam06775  74 LGNFMVRLELLSSNGKVLASSRRPAMLPYRSPLVRLLRTLLLLPPYLLGLREESQTLRVPMFESVVEGRENPPTSARVEI 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2328689126 223 QSQK-IQFYTVTLHIEADFSGLRYIMFNWPVLSAIVAISTN 262
Cdd:pfam06775 154 QSAGlLQIYSAELIFEARLPGLRYLMYNWPITSFVVGTALF 194
Seipin_BSCL2_like cd23995
Homo sapiens Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane ...
 82-242 6.47e-66

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: 205.93  E-value: 6.47e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126  82 PPISHTRPVHMQFKTCLETStPCTFPHAHVSLTKKQQ--LLMVGQAYKVIVNIDMPESPQNLELGMFMVCAEMRDYDSML 159
Cdd:cd23995     1 PPVSHERPVHFQYGTCCDAG-VCSFPSATVSLTPGGLsqLLSPGQPYDVSLELELPESPVNRDLGNFMVSLELLSADGTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2328689126 160 RGHSCRSAMMRYRSPLVRLFSTWALSPLYVLGWKEEFQKVPVEIFSRYLEERQHPITDVYVEIQSQKIQFYTVTLHIEAD 239
Cdd:cd23995    80 LASSSRPAILRYRSPLVRLLRTLLFLPPLLLGLSEETQTLSVPLFEGFVEDPDNPTTSARVELQSRLLQIYSASLRIHAR 159


                  ...
gi 2328689126 240 FSG 242
Cdd:cd23995   160 LSG 162
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
 180-233 2.53e-03

Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a small 61 kDa protein, is a single domain alpha/beta hydrolase. It lacks a C2 domain; therefore, it has no Ca-dependence. Group IVC cPLA2 is also referred to as cPLA2-gamma. The cPLA2-gamma enzyme is predominantly found in cardiac and skeletal muscles, and to a lesser extent in the brain. Human cPLA2-gamma is approximately 30% identical to cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Includes PLA2G4C protein from human and Pla2g4c protein from mouse.


Pssm-ID: 132841 [Multi-domain]  Cd Length: 430  Bit Score: 39.77  E-value: 2.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2328689126 180 STWALSPLYVL-GWKEEFQKVPVEIFSRYLEERQHPITDVYVEIQSQKIQFYTVT 233
Cdd:cd07202    81 STWCMSSLYTEpDWSTKLQTVEDELKRRLQKVSWDFAYALKKEIQAAKSDNFSLT 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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