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Conserved domains on  [gi|23831266|sp|Q14693|]
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RecName: Full=Phosphatidate phosphatase LPIN1; AltName: Full=Lipin-1

Protein Classification

phosphatidate phosphatase( domain architecture ID 11151321)

phosphatidate phosphatase is a magnesium-dependent enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 626-851 6.03e-142

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


:

Pssm-ID: 462403  Cd Length: 226  Bit Score: 419.99  E-value: 6.03e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   626 KTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGI 705
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   706 AKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKN 785
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23831266   786 LFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFP 851
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 4.15e-63

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


:

Pssm-ID: 461356  Cd Length: 103  Bit Score: 207.39  E-value: 4.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266     1 MNYVGQlagqVFVTVKELYKGLNPATLSGCIDIIVIRQPNGNLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 23831266    81 GDNGEAFFVQETDNDQEVIPMHLATSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 464-557 7.58e-44

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


:

Pssm-ID: 465292  Cd Length: 98  Bit Score: 153.60  E-value: 7.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   464 IAISLCGGLS--DHREITKDAFLEQAVSYQQFVDNPAIIDDPNLVVKIGSKYYNWTTAAPLLLAMQAFQKPLPKATVESI 541
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 23831266   542 MRD--KMPKKGGRWWFSW 557
Cdd:pfam16876  81 IKEarKNPKKGRRSWFSW 98
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 626-851 6.03e-142

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 462403  Cd Length: 226  Bit Score: 419.99  E-value: 6.03e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   626 KTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGI 705
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   706 AKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKN 785
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23831266   786 LFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFP 851
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 674-830 4.96e-78

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 249.88  E-value: 4.96e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266    674 VIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLL 753
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23831266    754 LSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQE 830
Cdd:smart00775  81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPPQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 4.15e-63

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


Pssm-ID: 461356  Cd Length: 103  Bit Score: 207.39  E-value: 4.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266     1 MNYVGQlagqVFVTVKELYKGLNPATLSGCIDIIVIRQPNGNLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 23831266    81 GDNGEAFFVQETDNDQEVIPMHLATSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 464-557 7.58e-44

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


Pssm-ID: 465292  Cd Length: 98  Bit Score: 153.60  E-value: 7.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   464 IAISLCGGLS--DHREITKDAFLEQAVSYQQFVDNPAIIDDPNLVVKIGSKYYNWTTAAPLLLAMQAFQKPLPKATVESI 541
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 23831266   542 MRD--KMPKKGGRWWFSW 557
Cdd:pfam16876  81 IKEarKNPKKGRRSWFSW 98
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 626-851 6.03e-142

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 462403  Cd Length: 226  Bit Score: 419.99  E-value: 6.03e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   626 KTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGI 705
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   706 AKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKN 785
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23831266   786 LFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFP 851
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 674-830 4.96e-78

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 249.88  E-value: 4.96e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266    674 VIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLL 753
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23831266    754 LSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQE 830
Cdd:smart00775  81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPPQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 4.15e-63

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


Pssm-ID: 461356  Cd Length: 103  Bit Score: 207.39  E-value: 4.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266     1 MNYVGQlagqVFVTVKELYKGLNPATLSGCIDIIVIRQPNGNLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 23831266    81 GDNGEAFFVQETDNDQEVIPMHLATSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 464-557 7.58e-44

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


Pssm-ID: 465292  Cd Length: 98  Bit Score: 153.60  E-value: 7.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23831266   464 IAISLCGGLS--DHREITKDAFLEQAVSYQQFVDNPAIIDDPNLVVKIGSKYYNWTTAAPLLLAMQAFQKPLPKATVESI 541
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 23831266   542 MRD--KMPKKGGRWWFSW 557
Cdd:pfam16876  81 IKEarKNPKKGRRSWFSW 98
 
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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