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Protein

N-acetyltransferase 8

Gene

Nat8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acetylates the free alpha-amino group of cysteine S-conjugates to form mercapturic acids. 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. May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (By similarity).By similarity

Catalytic activityi

Acetyl-CoA + an L-cysteine-S-conjugate = CoA + an N-acetyl L-cysteine-S-conjugate.1 Publication

Pathwayi: glutathione metabolism

This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00204.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyltransferase 8 (EC:2.3.1.-)
Alternative name(s):
Acetyltransferase 2
Short name:
ATase2
Camello-like protein 4
Cysteinyl-conjugate N-acetyltransferase (EC:2.3.1.80)
Short name:
CCNAT
Gene namesi
Name:Nat8
Synonyms:Cml4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621609. Nat8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3535CytoplasmicSequence analysisAdd
BLAST
Transmembranei36 – 5621Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini57 – 222166LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222N-acetyltransferase 8PRO_0000284693Add
BLAST

Proteomic databases

PRIDEiQ9QXT3.

PTM databases

iPTMnetiQ9QXT3.

Interactioni

Subunit structurei

Interacts with PROM1. Interacts with BACE1 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9QXT3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 217156N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the camello family.1 Publication
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG060476.
InParanoidiQ9QXT3.
PhylomeDBiQ9QXT3.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QXT3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFHIRQFQ ERDYEQVVDM FSRGMKEHIP TAFRHLLLLP RTLLLLLGVP
60 70 80 90 100
LALVLVSGSW LLAVVCIFFL LPFLWFLAGQ PWKNYVSKCL HTDMADITKS
110 120 130 140 150
YLSDRGSGFW VAESGGQIVG TVGALPVKDP PSGRKQLQLF RLSVSSQHRG
160 170 180 190 200
QGIAKALVRT VLQFARDQGY TDVVLVTGLL QQGAVTLYYS MGFQKTGESF
210 220
MDILTWLVDV SLIHFIYPLP SS
Length:222
Mass (Da):24,894
Last modified:May 1, 2000 - v1
Checksum:i8D28228022E8DC2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF185570 mRNA. Translation: AAF22298.1.
RefSeqiNP_072157.1. NM_022635.1.
XP_006236851.1. XM_006236789.2.
XP_006236852.1. XM_006236790.2.
UniGeneiRn.204804.

Genome annotation databases

GeneIDi64570.
KEGGirno:64570.
UCSCiRGD:621609. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF185570 mRNA. Translation: AAF22298.1.
RefSeqiNP_072157.1. NM_022635.1.
XP_006236851.1. XM_006236789.2.
XP_006236852.1. XM_006236790.2.
UniGeneiRn.204804.

3D structure databases

ProteinModelPortaliQ9QXT3.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ9QXT3.

Proteomic databases

PRIDEiQ9QXT3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64570.
KEGGirno:64570.
UCSCiRGD:621609. rat.

Organism-specific databases

CTDi9027.
RGDi621609. Nat8.

Phylogenomic databases

HOVERGENiHBG060476.
InParanoidiQ9QXT3.
PhylomeDBiQ9QXT3.

Enzyme and pathway databases

UniPathwayiUPA00204.

Miscellaneous databases

PROiQ9QXT3.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Overexpression of camello, a member of a novel protein family, reduces blastomere adhesion and inhibits gastrulation in Xenopus laevis."
    Popsueva A.E., Luchinskaya N.N., Ludwig A.V., Zinovjeva O.Y., Poteryaev D.A., Feigelman M.M., Ponomarev M.B., Berekelya L., Belyavsky A.V.
    Dev. Biol. 234:483-496(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: KidneyImported.
  2. "Cysteine S-conjugate N-acetyltransferase from rat kidney microsomes."
    Duffel M.W., Jakoby W.B.
    Mol. Pharmacol. 21:444-448(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.

Entry informationi

Entry nameiNAT8_RAT
AccessioniPrimary (citable) accession number: Q9QXT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.