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Conserved domains on  [gi|1034605080|ref|XP_016881588|]
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phosphatidate phosphatase LPIN2 isoform X3 [Homo sapiens]

Protein Classification

lipin family protein( domain architecture ID 11151325)

lipin family protein acts as a phosphatidate phosphatase that catalyzes the conversion of phosphatidic acid to diacylglycerol

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, ...
 637-862 2.03e-155

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: 454.66  E-value: 2.03e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 637 KSLRLSSDQIAKLKLHDGPNDVVFSITTQYQGTCRCAGTIYLWNWNDKIIISDIDGTITKSDALGQILPQLGKDWTHQGI 716
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 717 AKLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLMLSPSSLFSAFHREVIEKKPEKFKIECLNDIKN 796
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034605080 797 LFAPSKQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQERTKGNKSSYHRLSELVEHVFP 862
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 7.08e-56

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: 187.75  E-value: 7.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080   1 MNYVGQlagqVIVTVKELYKGINQATLSGCIDVIVVQQQDGSYQCSPFHVRFGKLGVLRSKEKVIDIEINGSAVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1034605080  81 GDNGEAFFVEETEEEYEKLPAYLATSP 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 ...
 469-561 4.84e-42

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: 148.59  E-value: 4.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 469 VTLSLCGGLS--ENGEISKEKFMEHIITYHEFAENPGLIDNPNLVIRIYNRYYNWALAAPMILSLQVFQKSLPKATVESW 546
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*..
gi 1034605080 547 VKD--KMPKKSGRWWFW 561
Cdd:pfam16876  81 IKEarKNPKKGRRSWFS 97
WRNPLPNID pfam15017
Putative WW-binding domain and destruction box; This short conserved region is a putative ...
 875-893 1.79e-03

Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain.


:

Pssm-ID: 464448  Cd Length: 56  Bit Score: 37.32  E-value: 1.79e-03
                          10
                  ....*....|....*....
gi 1034605080 875 PEFSSFCYWRDPIPEVDLD 893
Cdd:pfam15017   1 EEFNSFLFWRNPLPEIDLE 19
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 637-862 2.03e-155

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: 454.66  E-value: 2.03e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 637 KSLRLSSDQIAKLKLHDGPNDVVFSITTQYQGTCRCAGTIYLWNWNDKIIISDIDGTITKSDALGQILPQLGKDWTHQGI 716
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 717 AKLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLMLSPSSLFSAFHREVIEKKPEKFKIECLNDIKN 796
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034605080 797 LFAPSKQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQERTKGNKSSYHRLSELVEHVFP 862
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 685-841 1.26e-93

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: 291.48  E-value: 1.26e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080  685 IIISDIDGTITKSDALGQILPQLGKDWTHQGIAKLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLM 764
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034605080  765 LSPSSLFSAFHREVIEKKPEKFKIECLNDIKNLFAPSKQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQE 841
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 7.08e-56

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: 187.75  E-value: 7.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080   1 MNYVGQlagqVIVTVKELYKGINQATLSGCIDVIVVQQQDGSYQCSPFHVRFGKLGVLRSKEKVIDIEINGSAVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1034605080  81 GDNGEAFFVEETEEEYEKLPAYLATSP 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 ...
 469-561 4.84e-42

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: 148.59  E-value: 4.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 469 VTLSLCGGLS--ENGEISKEKFMEHIITYHEFAENPGLIDNPNLVIRIYNRYYNWALAAPMILSLQVFQKSLPKATVESW 546
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*..
gi 1034605080 547 VKD--KMPKKSGRWWFW 561
Cdd:pfam16876  81 IKEarKNPKKGRRSWFS 97
WRNPLPNID pfam15017
Putative WW-binding domain and destruction box; This short conserved region is a putative ...
 875-893 1.79e-03

Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain.


Pssm-ID: 464448  Cd Length: 56  Bit Score: 37.32  E-value: 1.79e-03
                          10
                  ....*....|....*....
gi 1034605080 875 PEFSSFCYWRDPIPEVDLD 893
Cdd:pfam15017   1 EEFNSFLFWRNPLPEIDLE 19
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 637-862 2.03e-155

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: 454.66  E-value: 2.03e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 637 KSLRLSSDQIAKLKLHDGPNDVVFSITTQYQGTCRCAGTIYLWNWNDKIIISDIDGTITKSDALGQILPQLGKDWTHQGI 716
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 717 AKLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLMLSPSSLFSAFHREVIEKKPEKFKIECLNDIKN 796
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034605080 797 LFAPSKQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQERTKGNKSSYHRLSELVEHVFP 862
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 685-841 1.26e-93

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: 291.48  E-value: 1.26e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080  685 IIISDIDGTITKSDALGQILPQLGKDWTHQGIAKLYHSINENGYKFLYCSARAIGMADMTRGYLHWVNDKGTILPRGPLM 764
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034605080  765 LSPSSLFSAFHREVIEKKPEKFKIECLNDIKNLFAPSKQPFYAAFGNRPNDVYAYTQVGVPDCRIFTVNPKGELIQE 841
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 7.08e-56

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: 187.75  E-value: 7.08e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080   1 MNYVGQlagqVIVTVKELYKGINQATLSGCIDVIVVQQQDGSYQCSPFHVRFGKLGVLRSKEKVIDIEINGSAVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1034605080  81 GDNGEAFFVEETEEEYEKLPAYLATSP 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 ...
 469-561 4.84e-42

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: 148.59  E-value: 4.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034605080 469 VTLSLCGGLS--ENGEISKEKFMEHIITYHEFAENPGLIDNPNLVIRIYNRYYNWALAAPMILSLQVFQKSLPKATVESW 546
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*..
gi 1034605080 547 VKD--KMPKKSGRWWFW 561
Cdd:pfam16876  81 IKEarKNPKKGRRSWFS 97
WRNPLPNID pfam15017
Putative WW-binding domain and destruction box; This short conserved region is a putative ...
 875-893 1.79e-03

Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain.


Pssm-ID: 464448  Cd Length: 56  Bit Score: 37.32  E-value: 1.79e-03
                          10
                  ....*....|....*....
gi 1034605080 875 PEFSSFCYWRDPIPEVDLD 893
Cdd:pfam15017   1 EEFNSFLFWRNPLPEIDLE 19
 
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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