Primary Information |
|---|
| BoMiProt ID | Bomi5486 |
|---|
| Protein Name | Endonuclease G, mitochondrial/Endo G |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | P38447 |
|---|
| Milk Fraction | Whey |
|---|
| Ref Sequence ID | NP_787017.1 |
|---|
| Aminoacid Length | 299 |
|---|
| Molecular Weight | 32262 |
|---|
| FASTA Sequence |
Download |
|---|
| Gene Name | ENDOG |
|---|
| Gene ID | 327707 |
|---|
| Protein Existence Status | Reviewed |
|---|
Secondary Information |
|---|
| Protein Function | Endonuclease that preferentially catalyzes the cleavage of double-stranded 5-hydroxymethylcytosine (5hmC)-modified DNA. |
|---|
| PTMs | Disulphide bond, Phosphorylation |
|---|
Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P38447|NUCG_BOVIN Endonuclease G, mitochondrial OS=Bos taurus OX=9913 GN=ENDOG PE=1 SV=1
MQLLRAGLTLALGAGLGAAAESWWRQRADARATPGLLSRLPVLPVAAAAGLPAVPGAPAG
GGPGELAKYGLPGVAQLKSRASYVLCYDPRTRGALWVVEQLRPEGLRGDGNRSSCDFHED
DSVHAYHRAT*130NADYRGSGFDRGHLAAAANHRWSQKAMDDTFYLSNVAPQVPHLNQNAWNN
LEKYSRSLTRTYQNVYVCTGPLFLPRTEADGKSYVKYQVIGKNHVAVPTHFFKVLILEAA
GGQIELRSYVMPNAPVDEAIPLEHFLVPIESIERASGLLFVPNILARAGS*290LKAITAGSK |
|---|
| Predicted Disorder Regions | NA |
|---|
| DisProt Annotation | |
|---|
| TM Helix Prediction | No TM helices |
|---|
| Significance of PTMs | Glycogen synthase kinase 3 beta-mediated phosphorylation of ENDOG at Thr-128 and Ser-288 enhances its interaction with 14-3-3γ, which leads to the release of Tuberin (TSC2) and Phosphatidylinositol 3-kinase catalytic subunit type 3 (Vps34) from 14-3-3γ, followed by mTOR pathway suppression and autophagy initiation. |
|---|
| Bibliography | 1.Wang, W., Li, J., Tan, J. et al. Endonuclease G promotes autophagy by suppressing mTOR signaling and activating the DNA damage response. Nat Commun 12, 476 (2021). https://doi.org/10.1038/s41467-020-20780-2 2.Côté, J., & Ruiz-Carrillo, A. (1993). Primers for mitochondrial DNA replication generated by endonuclease G. Science (New York, N.Y.), 261(5122), 765–769. https://doi.org/10.1126/science.7688144 |