N-acetyltransferase 8

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:

  1. 43-63, 21 AA, Helical; Signal-anchor for type II membrane protein. {ECO:0000255}.

Sequence: 227 AA

10 20 30 40 50 60 MAPCHIRKYQ ESDRQWVVGL LSRGMAEHAP ATFRQLLKLP RTLILLLGGP LALLLVSGSW 70 80 90 100 110 120 LLALVFSISL FPALWFLAKK PWTEYVDMTL CTDMSDITKS YLSERGSCFW VAESEEKVVG 130 140 150 160 170 180 MVGALPVDDP TLREKRLQLF HLFVDSEHRR QGIAKALVRT VLQFARDQGY SEVILDTGTI 190 200 210 220 QLSAMALYQS MGFKKTGQSF FCVWARLVAL HTVHFIYHLP SSKVGSL

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) (°)  
ARTLILLLGGALALLLVSGSWLLALVF 6.9 -47.0° 1.4 44.9 -37.9
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:


Click on the image to enlarge

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