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Conserved domains on  [gi|1885011230|ref|NP_001372957|]
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seipin isoform 1 [Homo sapiens]

Protein Classification

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 ...
 122-286 1.97e-89

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: 269.55  E-value: 1.97e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 122 PTVSHLSPVHFYYRTDCDSSTtsLCSFPVANVSLTKGGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTISCYTRGG 201
Cdd:cd23993     1 PSNSHPLPVHNGVQTCLETST--PCTFPGAKVSLTKKSIPVGDMMGQKYDVNLQLYCPESPQNDHLGMFNVLIDVYRGPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 202 RIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGAIIEIHSKRIQLYGAYLRIH 281
Cdd:cd23993    79 EKIFHSSRSIMCLYRSDLMSMQETEVQSGLSRLGVYEEEQLNTVEIEDKYSEESSYPTTSVFLEIESAQIQLYIHPLGIK 158


                  ....*
gi 1885011230 282 AHFTG 286
Cdd:cd23993   159 ARFTG 163
PHA03169 super family cl27451
hypothetical protein; Provisional
 357-412 8.48e-03

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 38.41  E-value: 8.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1885011230 357 PGPEGQEESTPQSDVTEDGESPEDPSGTEGQLSEEEKPDqQPLSGEEELEPEASDG 412
Cdd:PHA03169  138 PSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE-EPEPPTSEPEPDSPGP 192
 
Name Accession Description Interval E-value
Seipin cd23993
Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the ...
 122-286 1.97e-89

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: 269.55  E-value: 1.97e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 122 PTVSHLSPVHFYYRTDCDSSTtsLCSFPVANVSLTKGGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTISCYTRGG 201
Cdd:cd23993     1 PSNSHPLPVHNGVQTCLETST--PCTFPGAKVSLTKKSIPVGDMMGQKYDVNLQLYCPESPQNDHLGMFNVLIDVYRGPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 202 RIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGAIIEIHSKRIQLYGAYLRIH 281
Cdd:cd23993    79 EKIFHSSRSIMCLYRSDLMSMQETEVQSGLSRLGVYEEEQLNTVEIEDKYSEESSYPTTSVFLEIESAQIQLYIHPLGIK 158


                  ....*
gi 1885011230 282 AHFTG 286
Cdd:cd23993   159 ARFTG 163
Seipin pfam06775
Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ...
 103-307 4.42e-85

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: 259.39  E-value: 4.42e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 103 LLLLWVSVFLYGSFYYSYMPTVSHLSPVHFYYRTDCDssttslcsfPVANVSLTkgGRDRVLMYGQPYRVTLELELPESP 182
Cdd:pfam06775   1 LLLLVLSVVAYGLFYYAYVPEPVLSRPLHFQYGTGSN---------PYATVSLT--SRASLLPPGQPYDVSVELTLPESP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 183 VNQDLGMFLVTISCYTRGGRIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGA 262
Cdd:pfam06775  70 YNLELGNFMVRLELLSSNGKVLASSRRPAMLPYRSPLVRLLRTLLLLPPYLLGLREESQTLRVPMFESVVEGRENPPTSA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1885011230 263 IIEIHS-KRIQLYGAYLRIHAHFTGLRYLLYNFPMTCAFIGVASNF 307
Cdd:pfam06775 150 RVEIQSaGLLQIYSAELIFEARLPGLRYLMYNWPITSFVVGTALFW 195
PHA03169 PHA03169
hypothetical protein; Provisional
 357-412 8.48e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 38.41  E-value: 8.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1885011230 357 PGPEGQEESTPQSDVTEDGESPEDPSGTEGQLSEEEKPDqQPLSGEEELEPEASDG 412
Cdd:PHA03169  138 PSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE-EPEPPTSEPEPDSPGP 192
 
Name Accession Description Interval E-value
Seipin cd23993
Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane protein in the ...
 122-286 1.97e-89

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: 269.55  E-value: 1.97e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 122 PTVSHLSPVHFYYRTDCDSSTtsLCSFPVANVSLTKGGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTISCYTRGG 201
Cdd:cd23993     1 PSNSHPLPVHNGVQTCLETST--PCTFPGAKVSLTKKSIPVGDMMGQKYDVNLQLYCPESPQNDHLGMFNVLIDVYRGPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 202 RIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGAIIEIHSKRIQLYGAYLRIH 281
Cdd:cd23993    79 EKIFHSSRSIMCLYRSDLMSMQETEVQSGLSRLGVYEEEQLNTVEIEDKYSEESSYPTTSVFLEIESAQIQLYIHPLGIK 158


                  ....*
gi 1885011230 282 AHFTG 286
Cdd:cd23993   159 ARFTG 163
Seipin pfam06775
Putative adipose-regulatory protein (Seipin); Seipin is a protein of approximately 400 ...
 103-307 4.42e-85

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: 259.39  E-value: 4.42e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 103 LLLLWVSVFLYGSFYYSYMPTVSHLSPVHFYYRTDCDssttslcsfPVANVSLTkgGRDRVLMYGQPYRVTLELELPESP 182
Cdd:pfam06775   1 LLLLVLSVVAYGLFYYAYVPEPVLSRPLHFQYGTGSN---------PYATVSLT--SRASLLPPGQPYDVSVELTLPESP 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 183 VNQDLGMFLVTISCYTRGGRIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGA 262
Cdd:pfam06775  70 YNLELGNFMVRLELLSSNGKVLASSRRPAMLPYRSPLVRLLRTLLLLPPYLLGLREESQTLRVPMFESVVEGRENPPTSA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1885011230 263 IIEIHS-KRIQLYGAYLRIHAHFTGLRYLLYNFPMTCAFIGVASNF 307
Cdd:pfam06775 150 RVEIQSaGLLQIYSAELIFEARLPGLRYLMYNWPITSFVVGTALFW 195
Seipin_BSCL2_like cd23995
Homo sapiens Seipin and similar proteins; Seipin is a homo-oligomeric integral membrane ...
 122-286 1.03e-71

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: 223.65  E-value: 1.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 122 PTVSHLSPVHFYYRTDCDSSttsLCSFPVANVSLTKGGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTISCYTRGG 201
Cdd:cd23995     1 PPVSHERPVHFQYGTCCDAG---VCSFPSATVSLTPGGLSQLLSPGQPYDVSLELELPESPVNRDLGNFMVSLELLSADG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885011230 202 RIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGAIIEIHSKRIQLYGAYLRIH 281
Cdd:cd23995    78 TVLASSSRPAILRYRSPLVRLLRTLLFLPPLLLGLSEETQTLSVPLFEGFVEDPDNPTTSARVELQSRLLQIYSASLRIH 157


                  ....*
gi 1885011230 282 AHFTG 286
Cdd:cd23995   158 ARLSG 162
PHA03169 PHA03169
hypothetical protein; Provisional
 357-412 8.48e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 38.41  E-value: 8.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1885011230 357 PGPEGQEESTPQSDVTEDGESPEDPSGTEGQLSEEEKPDqQPLSGEEELEPEASDG 412
Cdd:PHA03169  138 PSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPE-EPEPPTSEPEPDSPGP 192
 
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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