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Conserved domains on  [gi|317016883|gb|ADU85972|]
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patatin-like phospholipase domain containing 2 [Homo sapiens]

Protein Classification

Pat_PNPLA2 domain-containing protein( domain architecture ID 10163448)

Pat_PNPLA2 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 4-252 0e+00

Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens.


:

Pssm-ID: 132859  Cd Length: 249  Bit Score: 510.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   4 REKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGP 83
Cdd:cd07220    1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  84 LHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVR 163
Cdd:cd07220   81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 164 YVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYR 243
Cdd:cd07220  161 YVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYR 240


                 ....*....
gi 317016883 244 DGLRFLQRN 252
Cdd:cd07220  241 DALRFLKEN 249
 
Name Accession Description Interval E-value
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 4-252 0e+00

Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132859  Cd Length: 249  Bit Score: 510.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   4 REKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGP 83
Cdd:cd07220    1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  84 LHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVR 163
Cdd:cd07220   81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 164 YVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYR 243
Cdd:cd07220  161 YVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYR 240


                 ....*....
gi 317016883 244 DGLRFLQRN 252
Cdd:cd07220  241 DALRFLKEN 249
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 10-178 4.29e-21

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 90.75  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   10 ISFAGCGFLGVYYVGVASCLREHapflVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEA------------- 76
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLflslirkralsll 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   77 ----RKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLG---------ISLTRVSDGENVIISHFNSKDELIQANV 143
Cdd:pfam01734  77 allrGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVvalralltvISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 317016883  144 CSGFIPVYcgLIPPSLQGVRYVDGGISDNLPLYEL 178
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 3-251 8.77e-16

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 77.25  E-value: 8.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   3 PREKTWNISFAGCGFLGVYYVGVASCLREHA-PFlvanaTHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRF- 80
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGiPP-----DVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLs 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  81 -------LGPLHPSFNLVKI--IRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIIShfnsKDELIQANVCSGFIPvy 151
Cdd:COG1752   77 lprrllrLDLGLSPGGLLDGdpLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFD----SGPLADAVRASAAIP-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 152 cGLIPP-SLQGVRYVDGGISDNLPLYELKN-----TITVSPFSGESDICP----QDSSTNIHELRVTNTSIQFNLRNLYp 221
Cdd:COG1752  151 -GVFPPvEIDGRLYVDGGVVNNLPVDPARAlgadrVIAVDLNPPLRKLPSlldiLGRALEIMFNSILRRELALEPADIL- 228

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 317016883 222 lskaLFPP-------EPLVLREMCKQGYRDGLRFLQR 251
Cdd:COG1752  229 ----IEPDlsgisllDFSRAEELIEAGYEAARRALDE 261
 
Name Accession Description Interval E-value
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 4-252 0e+00

Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis of stored triacylglecerols and is also known as adipose triglyceride lipase (ATGL). Members of this family share a patain domain, initially discovered in potato tubers. ATGL is expressed in white and brown adipose tissue in high mRNA levels. Mutations in PNPLA2 encoding adipose triglyceride lipase (ATGL) leads to neutral lipid storage disease (NLSD) which is characterized by the accumulation of triglycerides in multiple tissues. ATGL mutations are also commonly associated with severe forms of skeletal- and cardio-myopathy. This family includes patatin-like proteins: TTS-2.2 (transport-secretion protein 2.2), PNPLA2 (Patatin-like phospholipase domain-containing protein 2), and iPLA2-zeta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132859  Cd Length: 249  Bit Score: 510.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   4 REKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGP 83
Cdd:cd07220    1 LDSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGVCLGECGASVIRVAKEARKRFLGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  84 LHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVR 163
Cdd:cd07220   81 LHPSFNLVKILRDGLLRTLPENAHELASGRLGISLTRVSDGENVLVSDFNSKEELIQALVCSCFIPVYCGLIPPTLRGVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 164 YVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYR 243
Cdd:cd07220  161 YVDGGISDNLPQYELKNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYR 240


                 ....*....
gi 317016883 244 DGLRFLQRN 252
Cdd:cd07220  241 DALRFLKEN 249
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 9-251 1.69e-151

Patatin-like phospholipase domain containing protein family; Members of this family share a patain domain, initially discovered in potato tubers. PNPLA protein members show non-specific hydrolase activity with a variety of substrates such as triacylglycerol, phospholipids, and retinylesters. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly). Nomenclature of PNPLA family could be misleading as some of the mammalian members of this family show hydrolase, but no phospholipase activity.


Pssm-ID: 132843 [Multi-domain]  Cd Length: 243  Bit Score: 432.16  E-value: 1.69e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   9 NISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSF 88
Cdd:cd07204    1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEEACSFILKVVSEARRRSLGPLHPSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  89 NLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGG 168
Cdd:cd07204   81 NLLKILRQGLEKILPDDAHELASGRLHISLTRVSDGENVLVSEFDSKEELIQALVCSCFIPFYCGLIPPKFRGVRYIDGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 169 ISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYRDGLRF 248
Cdd:cd07204  161 LSDNLPILDDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240


                 ...
gi 317016883 249 LQR 251
Cdd:cd07204  241 LER 243
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 9-255 8.19e-117

Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent phospholipase A2; otherwise known as Group IVA-1 PLA2. It contains the lipase consensus sequence (Gly-X-Ser-X-Gly);mutagenesis experiments confirm the role of this serine as a nucleophile. Some members of this group show triacylglycerol lipase activity (EC 3:1:1:3). Members include iPLA-1, iPLA-2, and iPLA-3 from Aedes aegypti and show acylglycerol transacylase/lipase activity. Also includes putative iPLA2-eta from Pediculus humanus corporis which shows patatin-like phospholipase activity.


Pssm-ID: 132857  Cd Length: 245  Bit Score: 343.94  E-value: 8.19e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   9 NISFAGCGFLGVYYVGVASCLREHAPFLVANAthIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSF 88
Cdd:cd07218    2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLLNK--ISGASAGALAACCLLCDLPLGEMTSDFLRVVREARRHSLGPFSPSF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  89 NLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGG 168
Cdd:cd07218   80 NIQTCLLEGLQKFLPDDAHERVSGRLHISLTRVSDGKNVIVSEFESREELLQALLCSCFIPVFSGLLPPKFRGVRYMDGG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 169 ISDNLPLYElKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYRDGLRF 248
Cdd:cd07218  160 FSDNLPTLD-ENTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRF 238


                 ....*..
gi 317016883 249 LQRNGLL 255
Cdd:cd07218  239 LHRNNLI 245
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 8-258 5.01e-108

Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase that mediates triacylglycerol hydrolysis in adipocytes and is an indicator of the nutritional state. PNPLA3 is also known as adiponutrin (ADPN) or iPLA2-epsilon. Human adiponutrins are bound to the cell membrane of adipocytes and show transacylase, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: ADPN (adiponutrin) from mammals, PNPLA3 (Patatin-like phospholipase domain-containing protein 3), and iPLA2-epsilon (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132860  Cd Length: 252  Bit Score: 321.73  E-value: 5.01e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   8 WNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPS 87
Cdd:cd07221    1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDQILQILMDLVRSARSRNIGILHPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  88 FNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDG 167
Cdd:cd07221   81 FNLSKHLRDGLQRHLPDNVHQLISGKMCISLTRVSDGENVLVSDFHSKDEVVDALVCSCFIPFFSGLIPPSFRGVRYVDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 168 GISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYRDGLR 247
Cdd:cd07221  161 GVSDNVPFFDAKTTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240

                        250
                 ....*....|.
gi 317016883 248 FLQRNGLLNRP 258
Cdd:cd07221  241 FLEENGICNRP 251
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 5-387 1.57e-102

Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), plays a role in regulation of adipocyte differentiation. PNPLA5 is expressed in brain tissue in high mRNA levels and low levels in liver tissue. There is no concrete evidence in support of the enzymatic activity of GS2L. This family includes patatin-like proteins: GS2L (GS2-like) and PNPLA5 (Patatin-like phospholipase domain-containing protein 5) reported exclusively in mammals.


Pssm-ID: 132862  Cd Length: 405  Bit Score: 313.39  E-value: 1.57e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   5 EKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPL 84
Cdd:cd07223    7 EGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADFCCSNLLGMVKHLERLSLGIF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  85 HPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRY 164
Cdd:cd07223   87 HPAYAPIEHIRQQLQESLPPNIHILASQRLGISMTRWPDGRNFIVTDFATRDELIQALICTLYFPFYCGIIPPEFRGERY 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 165 VDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYRD 244
Cdd:cd07223  167 IDGALSNNLPFSDCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNCRQGYLD 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 245 GLRFLQRNGLLNRPnPLLAL----PPARPHGPEDK--DQAVESAQAEDYSqLPgedHIL-------EHLPARLNEALLEA 311
Cdd:cd07223  247 ALRFLERRGLTKEP-VLWSLvskePPAPADGPRDTghDQGQKGGLSLNWD-VP---NVLvkdvpnfEQLSPELEAALKKA 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 317016883 312 CVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGR 387
Cdd:cd07223  322 CTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLR 397
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 9-252 6.72e-84

Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin domain, initially discovered in potato tubers. Some members of PNPLA1 subfamily do not have the lipase consensus sequence Gly-X-Ser-X-Gly which is essential for hydrolase activity. This family includes PNPLA1 from Homo sapiens and Gallus gallus. Currently, there is no literature available on the physiological role, structure, or enzymatic activity of PNPLA1. It is expressed in various human tissues in low mRNA levels.


Pssm-ID: 132858  Cd Length: 382  Bit Score: 264.45  E-value: 6.72e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   9 NISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSF 88
Cdd:cd07219   14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDEYLRVLNVGVAEVRKSFLGPLSPSC 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  89 NLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGG 168
Cdd:cd07219   94 KMVQMMRQFLYRVLPEDSYKVATGKLHVSLTRVTDGENVVVSEFTSKEELIEALYCSCFVPVYCGLIPPTYRGVRYIDGG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 169 ISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYRDGLRF 248
Cdd:cd07219  174 FTGMQPCSFWTDSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVLY 253


                 ....
gi 317016883 249 LQRN 252
Cdd:cd07219  254 LRRL 257
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 9-253 2.06e-78

Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene sequence-2), shows both lipase and transacylation activities. GS2 lipase is expressed in various tissues, predominantly in muscle and adipocytes tissue. It is also expressed in keratinocytes and shows retinyl ester hydrolase, acylglycerol, TG hydrolase, and PLA2 activity. This family includes patatin-like proteins: GS2 from mammals, PNPLA4 (Patatin-like phospholipase domain-containing protein 4), and iPLA2-eta (Calcium-independent phospholipase A2) from Homo sapiens.


Pssm-ID: 132861 [Multi-domain]  Cd Length: 246  Bit Score: 245.32  E-value: 2.06e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   9 NISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFI-EVSKEARKRFLGPLHPS 87
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAAVLLTAPEKIEECKEFTyKFAEEVRKQRFGAMTPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  88 FNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDG 167
Cdd:cd07222   81 YDFMARLRKGIESILPTDAHELANDRLHVSITNLKTRKNYLVSNFTSREDLIKVLLASCYVPVYAGLKPVEYKGQKWIDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 168 GISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYPLSKALFPPEPLVLREMCKQGYRDGLR 247
Cdd:cd07222  161 GFTNSLPVLPVGRTITVSPFSGRADICPQDKGQLDLYVRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAVR 240


                 ....*.
gi 317016883 248 FLQRNG 253
Cdd:cd07222  241 FLKKEN 246
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 10-186 2.37e-69

Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin 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). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family.


Pssm-ID: 132837 [Multi-domain]  Cd Length: 172  Bit Score: 219.52  E-value: 2.37e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  10 ISFAGCGFLGVYYVGVASCLREHAPflvaNATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSFN 89
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGP----LIDIIAGTSAGAIVAALLASGRDLEEALLLLLRLSREVRLRFDGAFPPTGR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  90 LVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIIShFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGGI 169
Cdd:cd07198   77 LLGILRQPLLSALPDDAHEDASGKLFISLTRLTDGENVLVS-DTSKGELWSAVRASSSIPGYFGPVPLSFRGRRYGDGGL 155

                        170
                 ....*....|....*..
gi 317016883 170 SDNLPLYELKNTITVSP 186
Cdd:cd07198  156 SNNLPVAELGNTINVSP 172
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 10-186 1.65e-39

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes 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.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 140.24  E-value: 1.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  10 ISFAGCGFLGVYYVGVASCLREHAPFlvANATHIYGASAGALTATALvtgvclgeagakfievskearkrflgpLHPSFN 89
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGLL--DCVTYLAGTSGGAWVAATL---------------------------YPPSSS 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  90 LVKIIRSFLLkvlpadshEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPP----------SL 159
Cdd:cd01819   52 LDNKPRQSLE--------EALSGKLWVSFTPVTAGENVLVSRFVSKEELIRALFASGSWPSYFGLIPPaelytsksnlKE 123

                        170       180       190
                 ....*....|....*....|....*....|..
gi 317016883 160 QGVRYVDGGISDNLPLY-----ELKNTITVSP 186
Cdd:cd01819  124 KGVRLVDGGVSNNLPAPvllrpGRGVTLTISP 155
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 10-251 2.34e-25

Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 132863  Cd Length: 233  Bit Score: 103.96  E-value: 2.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  10 ISFAGCGFLGVYYVGVASCL------REHAPFLvanathiyGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRflgp 83
Cdd:cd07224    2 FSFSAAGLLFPYHLGVLSLLieagviNETTPLA--------GASAGSLAAACSASGLSPEEALEATEELAEDCRSN---- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  84 lHPSFNLVKIIRSFLLKVLPADSHEH-ASGRLGISLTRVS---DGENViiSHFNSKDELIQANVCSGFIPVYCGLIPPSL 159
Cdd:cd07224   70 -GTAFRLGGVLRDELDKTLPDDAHERcNRGRIRVAVTQLFpvpRGLLV--SSFDSKSDLIDALLASCNIPGYLAPWPATM 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 160 -QGVRYVDGGISDNLPLYELKN-TITVSPF-SGESDICPQDSSTNIHELrVTNTSIQFnlrnlypLSKALFPPEPLVLRE 236
Cdd:cd07224  147 fRGKLCVDGGFALFIPPTTAADrTVRVCPFpASRSSIKGQNLDNDDTED-VPYSRRQL-------LNWALEPADDAMLLE 218

                        250
                 ....*....|....*
gi 317016883 237 MCKQGYRDGLRFLQR 251
Cdd:cd07224  219 LFNEGYKDANEWAKE 233
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 10-178 4.29e-21

Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates.


Pssm-ID: 396341  Cd Length: 190  Bit Score: 90.75  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   10 ISFAGCGFLGVYYVGVASCLREHapflVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEA------------- 76
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEA----GIRFDVISGTSAGAINAALLALGRDPEEIEDLLLELDLNLflslirkralsll 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   77 ----RKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLG---------ISLTRVSDGENVIISHFNSKDELIQANV 143
Cdd:pfam01734  77 allrGLIGEGGLFDGDALRELLRKLLGDLTLEELAARLSLLLVvalralltvISTALGTRARILLPDDLDDDEDLADAVL 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 317016883  144 CSGFIPVYcgLIPPSLQGVRYVDGGISDNLPLYEL 178
Cdd:pfam01734 157 ASSALPGV--FPPVRLDGELYVDGGLVDNVPVEAA 189
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 3-251 8.77e-16

Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only];


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 77.25  E-value: 8.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   3 PREKTWNISFAGCGFLGVYYVGVASCLREHA-PFlvanaTHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRF- 80
Cdd:COG1752    2 PARPKIGLVLSGGGARGAAHIGVLKALEEAGiPP-----DVIAGTSAGAIVGALYAAGYSADELEELWRSLDRRDLFDLs 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  81 -------LGPLHPSFNLVKI--IRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIIShfnsKDELIQANVCSGFIPvy 151
Cdd:COG1752   77 lprrllrLDLGLSPGGLLDGdpLRRLLERLLGDRDFEDLPIPLAVVATDLETGREVVFD----SGPLADAVRASAAIP-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 152 cGLIPP-SLQGVRYVDGGISDNLPLYELKN-----TITVSPFSGESDICP----QDSSTNIHELRVTNTSIQFNLRNLYp 221
Cdd:COG1752  151 -GVFPPvEIDGRLYVDGGVVNNLPVDPARAlgadrVIAVDLNPPLRKLPSlldiLGRALEIMFNSILRRELALEPADIL- 228

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 317016883 222 lskaLFPP-------EPLVLREMCKQGYRDGLRFLQR 251
Cdd:COG1752  229 ----IEPDlsgisllDFSRAEELIEAGYEAARRALDE 261
Pat_hypo_Ecoli_yjju_like cd07208
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ...
 12-245 8.12e-14

Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132847 [Multi-domain]  Cd Length: 266  Bit Score: 71.49  E-value: 8.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  12 FAGCGFLGVYYVGVASCLREHA--PFlvanaTHIYGASAGALTATALVTGvclGEAGAKFIEVSKEARKRFLGP-----L 84
Cdd:cd07208    3 LEGGGMRGAYTAGVLDAFLEAGirPF-----DLVIGVSAGALNAASYLSG---QRGRALRINTKYATDPRYLGLrsllrT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  85 HPSFNLVKIIRSFLLKVLPADSH---EHAsGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGliPPSLQG 161
Cdd:cd07208   75 GNLFDLDFLYDELPDGLDPFDFEafaASP-ARFYVVATDADTGEAVYFDKPDILDDLLDALRASSALPGLFP--PVRIDG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 162 VRYVDGGISDNLPLYEL-------------KNTITVSPFSGESDI-------CPQDSSTNIHELRVTNTSIQFnLRNLYP 221
Cdd:cd07208  152 EPYVDGGLSDSIPVDKAiedgadkivviltRPRGYRKKPSKSSPLakllyrkYPNLVEALLRRHSRYNETLEF-IRRLEA 230

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 317016883 222 LSKAL-FPPEPLV-----------LREMCKQGYRDG 245
Cdd:cd07208  231 EGKIFvIAPEKPLkvsrlerdpekLEALYDLGYEDA 266
YjjU COG4667
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];
14-175 4.83e-11

Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism];


Pssm-ID: 443704 [Multi-domain]  Cd Length: 281  Bit Score: 63.26  E-value: 4.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  14 GCGFLGVYYVGVA-SCLREHAPFlvanaTHIYGASAGALTATALVTGvclgEAG-AKFIEVSKEARKRFLGPLH-----P 86
Cdd:COG4667   12 GGGMRGIFTAGVLdALLEEGIPF-----DLVIGVSAGALNGASYLSR----QPGrARRVITDYATDPRFFSLRNflrggN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  87 SFNLVKIIRSFLLKVLPADSHE-HASGR-LGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGliPPSLQGVRY 164
Cdd:COG4667   83 LFDLDFLYDEIPNELLPFDFETfKASPReFYVVATNADTGEAEYFSKKDDDYDLLDALRASSALPLLYP--PVEIDGKRY 160

                        170
                 ....*....|.
gi 317016883 165 VDGGISDNLPL 175
Cdd:COG4667  161 LDGGVADSIPV 171
Pat_ExoU_VipD_like cd07207
ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is ...
 9-176 3.60e-09

ExoU and VipD-like proteins; homologus to patatin, cPLA2, and iPLA2; ExoU, a 74-kDa enzyme, is a potent virulence factor of Pseudomonas aeruginosa. One of the pathogenic mechanisms of P. aeruginosa is to induce cytotoxicity by the injection of effector proteins (e.g. ExoU) using the type III secretion (T3S) system. ExoU is homologus to patatin and also has the conserved catalytic residues of mammalian calcium-independent (iPLA2) and cytosolic (cPLA2) PLA2. In vitro, ExoU cytotoxity is blocked by the inhibitor of cytosolic and Ca2-independent phospholipase A2 (cPLA2 and iPLA2) enzymes, suggesting that phospholipase A2 inhibitors may represent a novel mode of treatment for acute P. aeruginosa infections. ExoU requires eukaryotic superoxide dismutase as a cofactor and cleaves phosphatidylcholine and phosphatidylethanolamine in vitro. VipD, a 69-kDa cytosolic protein, belongs to the members of Legionella pneumophila family and is homologus to ExoU from Pseudomonas. Even though VipD shows high sequence similarity with several functional regions of ExoU (e.g. oxyanion hole, active site serine, active site aspartate), it has been shown to have no phospholipase activity. This family includes ExoU from Pseudomonas aeruginosa and VipD of Legionella pneumophila.


Pssm-ID: 132846  Cd Length: 194  Bit Score: 56.52  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883   9 NISFAGCGFLGVYYVGVASCLREHaPFLVanaTHIYGASAGALTAtALvtgVCLGEAGAKFIEVSKEA-RKRFLGPLHPS 87
Cdd:cd07207    1 NLVFEGGGAKGIAYIGALKALEEA-GILK---KRVAGTSAGAITA-AL---LALGYSAADIKDILKETdFAKLLDSPVGL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  88 -FNLVKIIRSFLL-----------------------KVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANV 143
Cdd:cd07207   73 lFLLPSLFKEGGLykgdaleewlrellkektgnsfaTSLLRDLDDDLGKDLKVVATDLTTGALVVFSAETTPDMPVAKAV 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 317016883 144 -CSGFIPVY---CGLIppslQGVRYVDGGISDNLPLY 176
Cdd:cd07207  153 rASMSIPFVfkpVRLA----KGDVYVDGGVLDNYPVW 185
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 12-249 1.39e-08

Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132848 [Multi-domain]  Cd Length: 215  Bit Score: 54.99  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  12 FAGCGFLGVYYVGVASCLREHAPFLVAnathIYGASAGALTATALVTGVCLGeagakfievSKEARKRFLGpLHPSfnlv 91
Cdd:cd07209    3 LSGGGALGAYQAGVLKALAEAGIEPDI----ISGTSIGAINGALIAGGDPEA---------VERLEKLWRE-LSRE---- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  92 KI-IRSFLLKVLPADS---HEHASGRLGISLTRVSDGENVIISHfNSKDELIQANVCSGFIPVycGLIPPSLQGVRYVDG 167
Cdd:cd07209   65 DVfLRGLLDRALDFDTlrlLAILFAGLVIVAVNVLTGEPVYFDD-IPDGILPEHLLASAALPP--FFPPVEIDGRYYWDG 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883 168 GISDNLPL---YELK-NTITVSPFSGesdicpqDSSTNIHELrvtntsIQFNLRNLYPLSKALFPPEPLVLREMCKQGYR 243
Cdd:cd07209  142 GVVDNTPLspaIDLGaDEIIVVSLSD-------KGRDDRKGT------PPTTLIEILPRLFLRSGLDSERIRHNLELGYL 208


                 ....*.
gi 317016883 244 DGLRFL 249
Cdd:cd07209  209 DTLRAD 214
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
 12-174 3.94e-07

Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 50.24  E-value: 3.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  12 FAGCGFLGVYYVGVASCLREHA--PFLVAnathiyGASAGALTATALVTGVCLGEAGAKFIEVSKEaRKRFLGPLHPSFN 89
Cdd:cd07205    5 LSGGGARGLAHIGVLKALEEAGipIDIVS------GTSAGAIVGALYAAGYSPEEIEERAKLRSTD-LKALSDLTIPTAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  90 LVKI--IRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIIShfnsKDELIQANVCSGFIPvycGLIPP-SLQGVRYVD 166
Cdd:cd07205   78 LLRGdkFLELLDEYFGDRDIEDLWIPFFIVATDLTSGKLVVFR----SGSLVRAVRASMSIP---GIFPPvKIDGQLLVD 150


                 ....*...
gi 317016883 167 GGISDNLP 174
Cdd:cd07205  151 GGVLNNLP 158
Pat_hypo_W_succinogenes_WS1459_like cd07210
Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. ...
 16-175 2.14e-06

Hypothetical patatin similar to WS1459 of Wolinella succinogenes; Patatin-like phospholipase. This family predominantly consists of bacterial patatin glycoproteins. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates.


Pssm-ID: 132849 [Multi-domain]  Cd Length: 221  Bit Score: 48.88  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  16 GFLGVY-YVGVASCLREHAPFLVanatHIYGASAGALTATALVTGVCLGEAGAKFievSKEARKRFLGPLHPSFNL---- 90
Cdd:cd07210    8 GFFGFYaHLGFLAALLEMGLEPS----AISGTSAGALVGGLFASGISPDEMAELL---LSLERKDFWMFWDPPLRGglls 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 317016883  91 VKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIIShfnsKDELIQANVCSGFIPVYCGliPPSLQGVRYVDGGIS 170
Cdd:cd07210   81 GDRFAALLREHLPPDRFEELRIPLAVSVVDLTSRETLLLS----EGDLAEAVAASCAVPPLFQ--PVEIGGRPFVDGGVA 154


                 ....*
gi 317016883 171 DNLPL 175
Cdd:cd07210  155 DRLPF 159
 
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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