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Conserved domains on  [gi|295148044|ref|NP_001171146|]
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patatin-like phospholipase domain-containing protein 5 isoform 2 [Homo sapiens]

Protein Classification

patatin-like phospholipase domain-containing protein( domain architecture ID 27818)

patatin-like phospholipase domain-containing protein may function as a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Patatin_and_cPLA2 super family cl11396
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 1-291 0e+00

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.


The actual alignment was detected with superfamily member cd07223:

Pssm-ID: 416256  Cd Length: 405  Bit Score: 559.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044   1 MGFLEEEGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVD--------------- 65
Cdd:cd07223    1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADfccsnllgmvkhler 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044     --------------------------------------------------------------------------------
Cdd:cd07223   81 lslgifhpayapiehirqqlqeslppnihilasqrlgismtrwpdgrnfivtdfatrdeliqalictlyfpfycgiippe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  66 -------------------CPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNC 126
Cdd:cd07223  161 frgeryidgalsnnlpfsdCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044 127 RQGYLDALRFLERRGLTKEPVLWTLVSKEPPAPADGNWDAGCDQRWKGGLSLNWKVPHVQVKDVPNFEQLSPELEAALKK 206
Cdd:cd07223  241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044 207 ACTRDPSRWARFWHSGPGQVLTYLLLPCTLPFEYIYFRSRRLVVWLPDVPADLWWMQGLLRNMALEVFSRTKAQLLGPIS 286
Cdd:cd07223  321 ACTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                 ....*
gi 295148044 287 PPATR 291
Cdd:cd07223  401 PPVTR 405
 
Name Accession Description Interval E-value
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 1-291 0e+00

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: 559.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044   1 MGFLEEEGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVD--------------- 65
Cdd:cd07223    1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADfccsnllgmvkhler 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044     --------------------------------------------------------------------------------
Cdd:cd07223   81 lslgifhpayapiehirqqlqeslppnihilasqrlgismtrwpdgrnfivtdfatrdeliqalictlyfpfycgiippe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  66 -------------------CPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNC 126
Cdd:cd07223  161 frgeryidgalsnnlpfsdCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044 127 RQGYLDALRFLERRGLTKEPVLWTLVSKEPPAPADGNWDAGCDQRWKGGLSLNWKVPHVQVKDVPNFEQLSPELEAALKK 206
Cdd:cd07223  241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044 207 ACTRDPSRWARFWHSGPGQVLTYLLLPCTLPFEYIYFRSRRLVVWLPDVPADLWWMQGLLRNMALEVFSRTKAQLLGPIS 286
Cdd:cd07223  321 ACTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                 ....*
gi 295148044 287 PPATR 291
Cdd:cd07223  401 PPVTR 405
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 12-65 5.79e-05

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: 43.37  E-value: 5.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 295148044   12 LSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVD 65
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDPE 50
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 9-65 5.25e-04

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 41.04  E-value: 5.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295148044   9 RWNLSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVD 65
Cdd:COG1752    6 KIGLVLSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAGYSAD 58
 
Name Accession Description Interval E-value
Pat_PNPLA5-mammals cd07223
Patatin-like phospholipase domain containing protein 5; PNPLA5, also known as GS2L (GS2-like), ...
 1-291 0e+00

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: 559.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044   1 MGFLEEEGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVD--------------- 65
Cdd:cd07223    1 MDFLEDEGGWNLSFSGAGYLGLYHVGVTECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSADfccsnllgmvkhler 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044     --------------------------------------------------------------------------------
Cdd:cd07223   81 lslgifhpayapiehirqqlqeslppnihilasqrlgismtrwpdgrnfivtdfatrdeliqalictlyfpfycgiippe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  66 -------------------CPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNC 126
Cdd:cd07223  161 frgeryidgalsnnlpfsdCPSTITVSPFHGTVDICPQSTSANLHELNAFNASFQISTRNFFLGLKCLIPPKPEVVADNC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044 127 RQGYLDALRFLERRGLTKEPVLWTLVSKEPPAPADGNWDAGCDQRWKGGLSLNWKVPHVQVKDVPNFEQLSPELEAALKK 206
Cdd:cd07223  241 RQGYLDALRFLERRGLTKEPVLWSLVSKEPPAPADGPRDTGHDQGQKGGLSLNWDVPNVLVKDVPNFEQLSPELEAALKK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044 207 ACTRDPSRWARFWHSGPGQVLTYLLLPCTLPFEYIYFRSRRLVVWLPDVPADLWWMQGLLRNMALEVFSRTKAQLLGPIS 286
Cdd:cd07223  321 ACTRDFSTWARFCCSVPGKVLTYLLLPCTLPFEYIYFRSRRLVAWLPDVPADLWWMQGLLKSTALEVYSRAKSQLLRLGS 400


                 ....*
gi 295148044 287 PPATR 291
Cdd:cd07223  401 PPVTR 405
Pat_PNPLA_like cd07204
Patatin-like phospholipase domain containing protein family; Members of this family share a ...
 11-139 4.02e-53

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: 174.08  E-value: 4.02e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  11 NLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVD------------------------- 65
Cdd:cd07204    1 NLSFSGCGFLGIYHVGVASALREHAPRLLQNARRIAGASAGAIVAAVVLCGVSMEeacsfilkvvsearrrslgplhpsf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044     --------------------------------------------------------------------------------
Cdd:cd07204   81 nllkilrqglekilpddahelasgrlhisltrvsdgenvlvsefdskeeliqalvcscfipfycglippkfrgvryidgg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  66 ---------CPSTITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALRF 136
Cdd:cd07204  161 lsdnlpildDENTITVSPFSGESDICPQDKSSNLLEVNIANTSIQLSLENLYRLNRALFPPSLEILSRMCQQGYLDALRF 240


                 ...
gi 295148044 137 LER 139
Cdd:cd07204  241 LER 243
Pat_PNPLA2 cd07220
Patatin-like phospholipase domain containing protein 2; PNPLA2 plays a key role in hydrolysis ...
 7-139 3.79e-32

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: 119.85  E-value: 3.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044   7 EGRWNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCG------------------------- 61
Cdd:cd07220    2 DSGWNISFAGCGFLGVYHVGVASCLLEHAPFLVANARKIYGASAGALTATALVTGvclgecgasvirvakearkrflgpl 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  62 ------------------------------------------------------------------------------KS 63
Cdd:cd07220   82 hpsfnlvkilrdgllrtlpenahelasgrlgisltrvsdgenvlvsdfnskeeliqalvcscfipvycglipptlrgvRY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  64 VD------CP-----STITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLD 132
Cdd:cd07220  162 VDggisdnLPqyelkNTITVSPFSGESDICPRDSSTNFHELRFTNTSIQFNLRNLYRLSKALFPPEPQVLAEMCKQGYRD 241


                 ....*..
gi 295148044 133 ALRFLER 139
Cdd:cd07220  242 ALRFLKE 248
Pat_PNPLA3 cd07221
Patatin-like phospholipase domain containing protein 3; PNPLA3 is a triacylglycerol lipase ...
 10-146 1.14e-29

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: 113.33  E-value: 1.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  10 WNLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVD------------------------ 65
Cdd:cd07221    1 WSLSFAGCGFLGFYHVGVTRCLSERAPHLLRDARMFFGASAGALHCVTFLSGLPLDqilqilmdlvrsarsrnigilhps 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  66 --------------------------------------------------------C------------PS--------- 68
Cdd:cd07221   81 fnlskhlrdglqrhlpdnvhqlisgkmcisltrvsdgenvlvsdfhskdevvdalvCscfipffsglipPSfrgvryvdg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  69 -------------TITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALR 135
Cdd:cd07221  161 gvsdnvpffdaktTITVSPFYGEYDICPKVKSTNFLHVDFTKLSLRLCTENLYLLTRALFPPDVKVLGEICLRGYLDAFR 240

                        250
                 ....*....|.
gi 295148044 136 FLERRGLTKEP 146
Cdd:cd07221  241 FLEENGICNRP 251
Pat_iPLA2 cd07218
Calcium-independent phospholipase A2; Classified as Group IVA-1 PLA2; Calcium-independent ...
 11-142 4.31e-24

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: 98.19  E-value: 4.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  11 NLSFSGAGYLGAHHVGATECLRQRAPRLLQgaRRIYGSSSGALNAVSIVC------------------------------ 60
Cdd:cd07218    2 NLSFAGCGFLGIYHVGVAVCLKKYAPHLLL--NKISGASAGALAACCLLCdlplgemtsdflrvvrearrhslgpfspsf 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  61 -----------------------------------GKSVD---------------CPS---------------------- 68
Cdd:cd07218   80 niqtclleglqkflpddahervsgrlhisltrvsdGKNVIvsefesreellqallCSCfipvfsgllppkfrgvrymdgg 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  69 -----------TITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALRFL 137
Cdd:cd07218  160 fsdnlptldenTITVSPFCGESDICPRDNSSQLFHINWANTSIELSRQNIYRLVRILFPPRPEVLSSLCQQGFDDALRFL 239


                 ....*
gi 295148044 138 ERRGL 142
Cdd:cd07218  240 HRNNL 244
Pat_PNPLA1 cd07219
Patatin-like phospholipase domain containing protein 1; Members of this family share a patatin ...
 11-139 4.00e-15

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: 75.31  E-value: 4.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  11 NLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNAVSIVCGKSVD---------------------CPS- 68
Cdd:cd07219   14 SISFSGSGFLSFYQAGVVDALRDLAPRMLETAHRVAGTSAGSVIAALVVCGISMDeylrvlnvgvaevrksflgplSPSc 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044     --------------------------------------------------------------------------------
Cdd:cd07219   94 kmvqmmrqflyrvlpedsykvatgklhvsltrvtdgenvvvseftskeeliealycscfvpvycglipptyrgvryidgg 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  69 ------------TITVSPFHGTVDICPQSTSPNLHELNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDALRF 136
Cdd:cd07219  174 ftgmqpcsfwtdSITISTFSGQQDICPRDCPAIFHDFRIFNCSFQFSLENIARMTHALFPPDLMVLHDYYYRGYQDTVLY 253


                 ...
gi 295148044 137 LER 139
Cdd:cd07219  254 LRR 256
Patatin cd07198
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ...
 12-65 1.33e-14

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: 70.45  E-value: 1.33e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 295148044  12 LSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVD 65
Cdd:cd07198    1 LVLSGGGALGIYHVGVAKALRERGPL----IDIIAGTSAGAIVAALLASGRDLE 50
Pat_PNPLA4 cd07222
Patatin-like phospholipase domain containing protein 4; PNPLA4, also known as GS2 (gene ...
 11-141 9.19e-11

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: 60.81  E-value: 9.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  11 NLSFSGAGYLGAHHVGATECLRQRAPRLLQGARRIYGSSSGALNA----------------------------------- 55
Cdd:cd07222    1 NLSFAACGFLGIYHLGAAKALLRHGKKLLKRVKRFAGASAGSLVAavlltapekieeckeftykfaeevrkqrfgamtpg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  56 ----------------------------VSIV--------------------------C-------GKSVDCPS------ 68
Cdd:cd07222   81 ydfmarlrkgiesilptdahelandrlhVSITnlktrknylvsnftsredlikvllasCyvpvyagLKPVEYKGqkwidg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044  69 -------------TITVSPFHGTVDICPQS-TSPNLHeLNVFNFSFQISTENFFLGLICLIPPSLEVVADNCRQGYLDAL 134
Cdd:cd07222  161 gftnslpvlpvgrTITVSPFSGRADICPQDkGQLDLY-VRFANQDIMLSLANLVRLNQALFPPNRRKLESYYQMGFDDAV 239


                 ....*..
gi 295148044 135 RFLERRG 141
Cdd:cd07222  240 RFLKKEN 246
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 12-58 1.15e-05

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: 44.71  E-value: 1.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 295148044  12 LSFSGAGYLGAHHVGATECLRQRAPrlLQGARRIYGSSSGALNAVSI 58
Cdd:cd01819    1 LSFSGGGFRGMYHAGVLSALAERGL--LDCVTYLAGTSGGAWVAATL 45
Patatin pfam01734
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ...
 12-65 5.79e-05

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: 43.37  E-value: 5.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 295148044   12 LSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVD 65
Cdd:pfam01734   1 LVLSGGGARGAYHLGVLKALGEAGIR----FDVISGTSAGAINAALLALGRDPE 50
Pat_hypo_Ecoli_Z1214_like cd07209
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ...
 12-63 8.91e-05

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: 43.05  E-value: 8.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 295148044  12 LSFSGAGYLGAHHVGATECLRQRAPRLlqgaRRIYGSSSGALNAVSIVCGKS 63
Cdd:cd07209    1 LVLSGGGALGAYQAGVLKALAEAGIEP----DIISGTSIGAINGALIAGGDP 48
RssA COG1752
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ...
 9-65 5.25e-04

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


Pssm-ID: 441358 [Multi-domain]  Cd Length: 261  Bit Score: 41.04  E-value: 5.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 295148044   9 RWNLSFSGAGYLGAHHVGATECLRQRAPRllqgARRIYGSSSGALNAVSIVCGKSVD 65
Cdd:COG1752    6 KIGLVLSGGGARGAAHIGVLKALEEAGIP----PDVIAGTSAGAIVGALYAAGYSAD 58
Pat_like cd07224
Patatin-like phospholipase; Patatin-like phospholipase. This family consists of various ...
 13-65 2.29e-03

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: 38.86  E-value: 2.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 295148044  13 SFSGAGYLGAHHVGATECLrQRAPRLLQGArRIYGSSSGALNAVSIVCGKSVD 65
Cdd:cd07224    3 SFSAAGLLFPYHLGVLSLL-IEAGVINETT-PLAGASAGSLAAACSASGLSPE 53
Pat_TGL3-4-5_SDP1 cd07206
Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are ...
 8-90 3.85e-03

Triacylglycerol lipase 3, 4, and 5 and Sugar-Dependent 1 lipase; Triacylglycerol lipases are involved in triacylglycerol mobilization and degradation; they are found in lipid particles. TGL4 is 30% homologus to TGL3, whereas TGL5 is 26% homologus to TGL3. Sugar-Dependent 1 (SDP1) lipase has a patatin-like acyl-hydrolase domain that initiates the breakdown of storage oil in germinating Arabidopsis seeds. This family includes subfamilies of proteins: TGL3, TGL4, TGL5, and SDP1.


Pssm-ID: 132845  Cd Length: 298  Bit Score: 38.35  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295148044   8 GRWNLSFSGAGYLGAHHVGATECLRQRapRLLqgARRIYGSSSGALNAvSIVC--------------------GKSVdcp 67
Cdd:cd07206   68 GRTALMLSGGASLGLFHLGVVKALWEQ--DLL--PRVISGSSAGAIVA-ALLGthtdeeligdltfqeayertGRII--- 139

                         90       100
                 ....*....|....*....|....*
gi 295148044  68 sTITVSPF--HGTVDICPQSTSPNL 90
Cdd:cd07206  140 -NITVAPAepHQNSRLLNALTSPNV 163
 
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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