O45870
Gene name |
T27F6.6 |
Protein name |
Putative neutral sphingomyelinase |
Names |
|
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_T27F6.6 |
EC number |
3.1.4.12: Phosphoric diester hydrolases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O45870
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O45870-F1 | Predicted | AlphaFoldDB |
No variants for O45870
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O45870 | |||||
No associated diseases with O45870
1 regional properties for O45870
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Endonuclease/exonuclease/phosphatase | 64 - 318 | IPR005135 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.4.12 | Phosphoric diester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| caveola | A membrane raft that forms small pit, depression, or invagination that communicates with the outside of a cell and extends inward, indenting the cytoplasm and the cell membrane. Examples include flask-shaped invaginations of the plasma membrane in adipocytes associated with caveolin proteins, and minute pits or incuppings of the cell membrane formed during pinocytosis. Caveolae may be pinched off to form free vesicles within the cytoplasm. |
| cell periphery | The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| phospholipase activity | Catalysis of the hydrolysis of a glycerophospholipid. |
| sphingomyelin phosphodiesterase activity | Catalysis of the reaction: H(2)O + sphingomyelin = ceramide + choline phosphate + H(+). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| ceramide biosynthetic process | The chemical reactions and pathways resulting in the formation of ceramides, any N-acylated sphingoid. |
| sphingolipid catabolic process | The chemical reactions and pathways resulting in the breakdown of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid). |
| sphingomyelin metabolic process | The chemical reactions and pathways involving sphingomyelin, N-acyl-4-sphingenyl-1-O-phosphorylcholine, any of a class of phospholipids in which the amino group of sphingosine is in amide linkage with one of several fatty acids, while the terminal hydroxyl group of sphingosine is esterified to phosphorylcholine. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O60906 | SMPD2 | Sphingomyelin phosphodiesterase 2 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEPSSEQESQ | ESQKVDMEPV | FRRESFAALR | RNNVAARQLR | VVTLNAWCLP | QPWPIGSTDR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VHRLNKIGQY | MIDELYDIVG | LQELWSYYDF | VRLSEQVSSV | YPYFHYFHSG | FTGSGVCVFS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RHPIVSTLTN | RYSLNGFAHH | IHRGDWFGGK | VVGLTEIEID | GDLRVNFYTT | HLHAEYDREN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DLYLPHRTAQ | AFELAQFVRH | TARGADVVIV | TGDLNMEPCD | LGFRLILSHA | KLFDAWRMSH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EVENEDSEGE | LLKFRGIAKG | GTCDRPDNCY | TKRALKNVDD | SKRIDYMLFK | SGRCNVKLEE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| CEITLNQIPG | EDLNYSDHVG | LRARFTIDDR | FRHEKSVNTW | EPNRPLLIEA | IGLVAGGERR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ARTDRIFFFI | LAVICLILIL | GSLFFEVFPM | GFAVLRFALT | VVGVFFVWQG | LIGLTLERKA |
| 430 | |||||
| LKAAKQAIQQ | ILNN |