UniProt data
UniProt name: NAT8_HUMAN (Q9UHE5)
Gene name: NAT8 {ECO:0000312|HGNC:HGNC:18069}
Organism: Homo sapiens (Human).
Function: Acetylates the free alpha-amino group of cysteine S- conjugates to form mercapturic acids (PubMed:20392701). This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S- conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. Alternatively, may have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6- acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1 (PubMed:24556617). May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (PubMed:19011241). {ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:20392701, ECO:0000269|PubMed:24556617}.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Transmembrane domains:
- 43-63, 21 AA, Helical; Signal-anchor for type II membrane protein. {ECO:0000255}.
Sequence: 227 AA
CATM prediction
The sequence of NAT8_HUMAN returned 1 potential models
The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.
| # | Sequence and interface | d | θ | Z' | ω' | Score |
|---|---|---|---|---|---|---|
| 40 50 60 | + | + | + |
(Å) | (°) | (Å) | (°) | ||
| Model 1 | ARTLILLLGGALALLLVSGSWLLALVF | 6.9 | -47.0° | 1.4 | 44.9 | -37.9 |
| Prolines* | PRTLILLLGGPLALLLVSGSWLLALVF |
* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.
Click on the model number to visualize its details below.
MODEL 1 DETAILS
Precited structure:
Download model 1 structure: PDB, PyMOL session
List of hydrogen bonds:
| Donor | Acceptor | Distance |
|---|---|---|
| B, 45, LEU, HA | A, 44, ILE, O | 3.28Å |
| B, 48, GLY, HA1 | A, 45, LEU, O | 2.89Å |
| B, 49, GLY, HA2 | A, 48, GLY, O | 3.09Å |
| A, 45, LEU, HA | B, 44, ILE, O | 3.28Å |
| A, 48, GLY, HA1 | B, 45, LEU, O | 2.89Å |
| A, 49, GLY, HA2 | B, 48, GLY, O | 3.09Å |

