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Conserved domains on  [gi|755527087|ref|XP_011246764|]
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sphingomyelin phosphodiesterase 3 isoform X1 [Mus musculus]

Protein Classification

sphingomyelin phosphodiesterase( domain architecture ID 18076815)

sphingomyelin phosphodiesterase (sphingomyelinase or SMase) catalyzes the hydrolysis of membrane sphingomyelin to phosphorylcholine and ceramide. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 336-646 1.16e-76

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


:

Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 246.48  E-value: 1.16e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 336 RRHPDEAFDHEVSAFFPANL--DFLCLQEVFDKRAAAKLKEQLHGYFeYILYDVGVYGCHGCcNFKCLNSGLFFASRYPV 413
Cdd:cd09078   16 YNNGDDGQDERLDLIPKALLqyDVVVLQEVFDARARKRLLNGLKKEY-PYQTDVVGRSPSGW-SSKLVDGGVVILSRYPI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 414 MDVAYHCYPNGCSFDALASKGALFLKVQVGSTpqdqrIVGYIACTHLHA---PPEDSAVRCEQLDLLQDWLADFRKstss 490
Cdd:cd09078   94 VEKDQYIFPNGCGADCLAAKGVLYAKINKGGT-----KVYHVFGTHLQAsdgSCLDRAVRQKQLDELRAFIEEKNI---- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 491 tstanpeELVVFDVICGDLNFDNCSS----DDKLEQQHSlftrYKDPCRLGPGE-EKPWAIGTLLDTNGLYDedvctpdn 565
Cdd:cd09078  165 -------PDNEPVIIAGDFNVDKRSSrdeyDDMLEQLHD----YNAPEPITAGEtPLTWDPGTNLLAKYNYP-------- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 566 lqkvleseegrreylafptskspgagqkgrkdllKGNGRRIDYMLHAEEGLCP-DWKAEVEEFSFIT-------QLSGLT 637
Cdd:cd09078  226 ----------------------------------GGGGERLDYILYSNDHLQPsSWSNEVEVPKSPTwsvtngyTFADLS 271


                 ....*....
gi 755527087 638 DHLPVAMRL 646
Cdd:cd09078  272 DHYPVSATF 280
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 172-321 2.74e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


The actual alignment was detected with superfamily member cd21118:

Pssm-ID: 455732 [Multi-domain]  Cd Length: 495  Bit Score: 43.83  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 172 DSPTNTSISAASFSSLVSPQGGDGSRAVPGSIKRTASveyKGDGGRHPSDEAANGPaSGEQADGSLEDScivriGGEEGG 251
Cdd:cd21118  209 GSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGG---QGNGGNNGSSSSNSGN-SGGSNGGSSGNS-----GSGSGG 279

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 252 RPQEADDPAAGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSpSASRESLVKARAGQDSGGSGEPGANSKL 321
Cdd:cd21118  280 SSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGG-GGSQGSKESSGSHGSNGGNGQAEAVGGL 348
 
Name Accession Description Interval E-value
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 336-646 1.16e-76

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 246.48  E-value: 1.16e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 336 RRHPDEAFDHEVSAFFPANL--DFLCLQEVFDKRAAAKLKEQLHGYFeYILYDVGVYGCHGCcNFKCLNSGLFFASRYPV 413
Cdd:cd09078   16 YNNGDDGQDERLDLIPKALLqyDVVVLQEVFDARARKRLLNGLKKEY-PYQTDVVGRSPSGW-SSKLVDGGVVILSRYPI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 414 MDVAYHCYPNGCSFDALASKGALFLKVQVGSTpqdqrIVGYIACTHLHA---PPEDSAVRCEQLDLLQDWLADFRKstss 490
Cdd:cd09078   94 VEKDQYIFPNGCGADCLAAKGVLYAKINKGGT-----KVYHVFGTHLQAsdgSCLDRAVRQKQLDELRAFIEEKNI---- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 491 tstanpeELVVFDVICGDLNFDNCSS----DDKLEQQHSlftrYKDPCRLGPGE-EKPWAIGTLLDTNGLYDedvctpdn 565
Cdd:cd09078  165 -------PDNEPVIIAGDFNVDKRSSrdeyDDMLEQLHD----YNAPEPITAGEtPLTWDPGTNLLAKYNYP-------- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 566 lqkvleseegrreylafptskspgagqkgrkdllKGNGRRIDYMLHAEEGLCP-DWKAEVEEFSFIT-------QLSGLT 637
Cdd:cd09078  226 ----------------------------------GGGGERLDYILYSNDHLQPsSWSNEVEVPKSPTwsvtngyTFADLS 271


                 ....*....
gi 755527087 638 DHLPVAMRL 646
Cdd:cd09078  272 DHYPVSATF 280
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 409-510 5.39e-06

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 46.83  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 409 SRYPVMDVAYHCYPNgcsfDALASKGALFLKVQVGstpqDQRIvgYIACTHLHAPpeDSAVRCEQLDLLQDWLADFRKSt 488
Cdd:COG3568   51 SRYPIVSSGTFDLPD----PGGEPRGALWADVDVP----GKPL--RVVNTHLDLR--SAAARRRQARALAELLAELPAG- 117

                         90       100
                 ....*....|....*....|..
gi 755527087 489 sststanpeELVVfdvICGDLN 510
Cdd:COG3568  118 ---------APVI---LAGDFN 127
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 330-512 1.90e-05

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 45.68  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087  330 KAAARRRRHPDEAFDHEVSAFFPanlDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGccnfkclnsGLFFAS 409
Cdd:pfam03372   9 NADAAGDDRKLDALAALIRAYDP---DVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGGGGG---------GVAILS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087  410 RYPVMDVAYHCYPNGCSFDAlaskgalflkvqVGSTPQDQRIVGYIACTHLHAPPEDSAVRCEQLDLLQDWLADFRKSTS 489
Cdd:pfam03372  77 RYPLSSVILVDLGEFGDPAL------------RGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRS 144

                         170       180
                  ....*....|....*....|...
gi 755527087  490 STStanpeelvvfdVICGDLNFD 512
Cdd:pfam03372 145 EPV-----------ILAGDFNAD 156
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 172-321 2.74e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 43.83  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 172 DSPTNTSISAASFSSLVSPQGGDGSRAVPGSIKRTASveyKGDGGRHPSDEAANGPaSGEQADGSLEDScivriGGEEGG 251
Cdd:cd21118  209 GSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGG---QGNGGNNGSSSSNSGN-SGGSNGGSSGNS-----GSGSGG 279

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 252 RPQEADDPAAGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSpSASRESLVKARAGQDSGGSGEPGANSKL 321
Cdd:cd21118  280 SSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGG-GGSQGSKESSGSHGSNGGNGQAEAVGGL 348
 
Name Accession Description Interval E-value
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 336-646 1.16e-76

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 246.48  E-value: 1.16e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 336 RRHPDEAFDHEVSAFFPANL--DFLCLQEVFDKRAAAKLKEQLHGYFeYILYDVGVYGCHGCcNFKCLNSGLFFASRYPV 413
Cdd:cd09078   16 YNNGDDGQDERLDLIPKALLqyDVVVLQEVFDARARKRLLNGLKKEY-PYQTDVVGRSPSGW-SSKLVDGGVVILSRYPI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 414 MDVAYHCYPNGCSFDALASKGALFLKVQVGSTpqdqrIVGYIACTHLHA---PPEDSAVRCEQLDLLQDWLADFRKstss 490
Cdd:cd09078   94 VEKDQYIFPNGCGADCLAAKGVLYAKINKGGT-----KVYHVFGTHLQAsdgSCLDRAVRQKQLDELRAFIEEKNI---- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 491 tstanpeELVVFDVICGDLNFDNCSS----DDKLEQQHSlftrYKDPCRLGPGE-EKPWAIGTLLDTNGLYDedvctpdn 565
Cdd:cd09078  165 -------PDNEPVIIAGDFNVDKRSSrdeyDDMLEQLHD----YNAPEPITAGEtPLTWDPGTNLLAKYNYP-------- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 566 lqkvleseegrreylafptskspgagqkgrkdllKGNGRRIDYMLHAEEGLCP-DWKAEVEEFSFIT-------QLSGLT 637
Cdd:cd09078  226 ----------------------------------GGGGERLDYILYSNDHLQPsSWSNEVEVPKSPTwsvtngyTFADLS 271


                 ....*....
gi 755527087 638 DHLPVAMRL 646
Cdd:cd09078  272 DHYPVSATF 280
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 409-510 5.39e-06

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 46.83  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 409 SRYPVMDVAYHCYPNgcsfDALASKGALFLKVQVGstpqDQRIvgYIACTHLHAPpeDSAVRCEQLDLLQDWLADFRKSt 488
Cdd:COG3568   51 SRYPIVSSGTFDLPD----PGGEPRGALWADVDVP----GKPL--RVVNTHLDLR--SAAARRRQARALAELLAELPAG- 117

                         90       100
                 ....*....|....*....|..
gi 755527087 489 sststanpeELVVfdvICGDLN 510
Cdd:COG3568  118 ---------APVI---LAGDFN 127
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 330-512 1.90e-05

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 45.68  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087  330 KAAARRRRHPDEAFDHEVSAFFPanlDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGccnfkclnsGLFFAS 409
Cdd:pfam03372   9 NADAAGDDRKLDALAALIRAYDP---DVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGGGGG---------GVAILS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087  410 RYPVMDVAYHCYPNGCSFDAlaskgalflkvqVGSTPQDQRIVGYIACTHLHAPPEDSAVRCEQLDLLQDWLADFRKSTS 489
Cdd:pfam03372  77 RYPLSSVILVDLGEFGDPAL------------RGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLLLLALLAPRS 144

                         170       180
                  ....*....|....*....|...
gi 755527087  490 STStanpeelvvfdVICGDLNFD 512
Cdd:pfam03372 145 EPV-----------ILAGDFNAD 156
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 172-321 2.74e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 43.83  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 172 DSPTNTSISAASFSSLVSPQGGDGSRAVPGSIKRTASveyKGDGGRHPSDEAANGPaSGEQADGSLEDScivriGGEEGG 251
Cdd:cd21118  209 GSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGG---QGNGGNNGSSSSNSGN-SGGSNGGSSGNS-----GSGSGG 279

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755527087 252 RPQEADDPAAGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSpSASRESLVKARAGQDSGGSGEPGANSKL 321
Cdd:cd21118  280 SSSGGSNGWGGSSSSGGSGGSGGGNKPECNNPGNDVRMAGG-GGSQGSKESSGSHGSNGGNGQAEAVGGL 348
 
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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