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N-acetyltransferase 8 (EC 2.3.1.-) (Acetyltransferase 2) (ATase2) (Camello-like protein 4) (Cysteinyl-conjugate N-acetyltransferase) (CCNAT) (EC 2.3.1.80)

 NAT8_RAT                Reviewed;         222 AA.
Q9QXT3;
17-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
30-AUG-2017, entry version 84.
RecName: Full=N-acetyltransferase 8;
EC=2.3.1.-;
AltName: Full=Acetyltransferase 2;
Short=ATase2;
AltName: Full=Camello-like protein 4;
AltName: Full=Cysteinyl-conjugate N-acetyltransferase;
Short=CCNAT;
EC=2.3.1.80;
Name=Nat8; Synonyms=Cml4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000312|EMBL:AAF22298.1}
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney {ECO:0000312|EMBL:AAF22298.1};
PubMed=11397015; DOI=10.1006/dbio.2001.0261;
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.;
"Overexpression of camello, a member of a novel protein family,
reduces blastomere adhesion and inhibits gastrulation in Xenopus
laevis.";
Dev. Biol. 234:483-496(2001).
[2]
CATALYTIC ACTIVITY.
PubMed=6892478;
Duffel M.W., Jakoby W.B.;
"Cysteine S-conjugate N-acetyltransferase from rat kidney
microsomes.";
Mol. Pharmacol. 21:444-448(1982).
-!- FUNCTION: 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an L-cysteine-S-conjugate = CoA +
an N-acetyl L-cysteine-S-conjugate. {ECO:0000269|PubMed:6892478}.
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- SUBUNIT: Interacts with PROM1. Interacts with BACE1 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
compartment membrane {ECO:0000250}; Single-pass type II membrane
protein {ECO:0000250}. Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
-!- SIMILARITY: Belongs to the camello family.
{ECO:0000269|PubMed:11397015}.
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EMBL; AF185570; AAF22298.1; -; mRNA.
RefSeq; NP_072157.1; NM_022635.1.
RefSeq; XP_006236851.1; XM_006236789.3.
RefSeq; XP_006236852.1; XM_006236790.3.
UniGene; Rn.204804; -.
ProteinModelPortal; Q9QXT3; -.
SMR; Q9QXT3; -.
iPTMnet; Q9QXT3; -.
PhosphoSitePlus; Q9QXT3; -.
PRIDE; Q9QXT3; -.
GeneID; 64570; -.
KEGG; rno:64570; -.
UCSC; RGD:621609; rat.
CTD; 9027; -.
RGD; 621609; Nat8.
HOVERGEN; HBG060476; -.
InParanoid; Q9QXT3; -.
KO; K20838; -.
PhylomeDB; Q9QXT3; -.
UniPathway; UPA00204; -.
PRO; PR:Q9QXT3; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0047198; F:cysteine-S-conjugate N-acetyltransferase activity; ISS:UniProtKB.
GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB.
GO; GO:0008080; F:N-acetyltransferase activity; NAS:UniProtKB.
GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
GO; GO:0001702; P:gastrulation with mouth forming second; ISS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0018003; P:peptidyl-lysine N6-acetylation; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
Pfam; PF00583; Acetyltransf_1; 1.
SUPFAM; SSF55729; SSF55729; 2.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Endoplasmic reticulum; Membrane;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 222 N-acetyltransferase 8.
/FTId=PRO_0000284693.
TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.
TRANSMEM 36 56 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 57 222 Lumenal. {ECO:0000255}.
DOMAIN 62 217 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
SEQUENCE 222 AA; 24894 MW; 8D28228022E8DC2B CRC64;
MASFHIRQFQ ERDYEQVVDM FSRGMKEHIP TAFRHLLLLP RTLLLLLGVP LALVLVSGSW
LLAVVCIFFL LPFLWFLAGQ PWKNYVSKCL HTDMADITKS YLSDRGSGFW VAESGGQIVG
TVGALPVKDP PSGRKQLQLF RLSVSSQHRG QGIAKALVRT VLQFARDQGY TDVVLVTGLL
QQGAVTLYYS MGFQKTGESF MDILTWLVDV SLIHFIYPLP SS


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