P49887
Gene name |
SULT1E1 (EST) |
Protein name |
Sulfotransferase 1E1 |
Names |
ST1E1, Estrogen sulfotransferase, ST1E3, Sulfotransferase, estrogen-preferring |
Species |
Cavia porcellus (Guinea pig) |
KEGG Pathway |
cpoc:100135625 |
EC number |
2.8.2.4: Sulfotransferases |
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 P49887
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P49887-F1 | Predicted | AlphaFoldDB |
No variants for P49887
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P49887 | |||||
No associated diseases with P49887
1 regional properties for P49887
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Sulfotransferase domain | 39 - 288 | IPR000863 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.8.2.4 | Sulfotransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| nuclear membrane | Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| estrone sulfotransferase activity | Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate. |
| flavonol 3-sulfotransferase activity | Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + quercetin = adenosine 3',5'-diphosphate + H(+) + quercetin 3-sulfate. |
| steroid binding | Binding to a steroid, any of a large group of substances that have in common a ring system based on 1,2-cyclopentanoperhydrophenanthrene. |
| steroid sulfotransferase activity | Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| 3'-phosphoadenosine 5'-phosphosulfate metabolic process | The chemical reactions and pathways involving 3'-phosphoadenosine 5'-phosphosulfate, a naturally occurring mixed anhydride. It is an intermediate in the formation of a variety of sulfo compounds in biological systems. |
| estrogen catabolic process | The chemical reactions and pathways resulting in the breakdown of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants. |
| estrogen metabolic process | The chemical reactions and pathways involving estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants. |
| ethanol catabolic process | The chemical reactions and pathways resulting in the breakdown of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation. |
| positive regulation of fat cell differentiation | Any process that activates or increases the frequency, rate or extent of adipocyte differentiation. |
| sulfation | The addition of a sulfate group to a molecule. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MMDSSEHDYY | EYFDEFRGIL | LYKQFIKYWD | NVEAFQARPD | DLVIAAYPKS | GTTWISEVVC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MIYAEGDVKK | CRQDAIFNRV | PFLECRNDKM | MNGVKQLEEM | NSPRIIKTHL | PPRLLPASFW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EKRCKMICIC | RNAKDVAVSY | YYFFLMVANH | PDPGSFPEFV | EKFMQGQVPY | GSWYDHVKSW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| WEKSTDPRIL | FIFYEDMKED | IRKEVLKLIH | FLGRKPSEEL | VDKIIKHTSF | QEMKNNPSTN |
| 250 | 260 | 270 | 280 | 290 | |
| YTMLPEEIMN | QKVSPFMRKG | ISGDWKNHFT | VALNESFDKH | YQQQMKGSTL | QLRTEI |