NAT8_RAT
ID NAT8_RAT Reviewed; 222 AA.
AC Q9QXT3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=N-acetyltransferase 8;
DE EC=2.3.1.-;
DE AltName: Full=Acetyltransferase 2;
DE Short=ATase2;
DE AltName: Full=Camello-like protein 4;
DE AltName: Full=Cysteinyl-conjugate N-acetyltransferase;
DE Short=CCNAT;
DE EC=2.3.1.80;
GN Name=Nat8; Synonyms=Cml4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAF22298.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAF22298.1};
RX PubMed=11397015; DOI=10.1006/dbio.2001.0261;
RA Popsueva A.E., Luchinskaya N.N., Ludwig A.V., Zinovjeva O.Y.,
RA Poteryaev D.A., Feigelman M.M., Ponomarev M.B., Berekelya L.,
RA Belyavsky A.V.;
RT "Overexpression of camello, a member of a novel protein family, reduces
RT blastomere adhesion and inhibits gastrulation in Xenopus laevis.";
RL Dev. Biol. 234:483-496(2001).
RN [2]
RP CATALYTIC ACTIVITY.
RX PubMed=6892478;
RA Duffel M.W., Jakoby W.B.;
RT "Cysteine S-conjugate N-acetyltransferase from rat kidney microsomes.";
RL Mol. Pharmacol. 21:444-448(1982).
CC -!- FUNCTION: Acetylates the free alpha-amino group of cysteine S-
CC conjugates to form mercapturic acids. This is the final step in a major
CC route for detoxification of a wide variety of reactive electrophiles
CC which starts with their incorporation into glutathione S-conjugates.
CC The glutathione S-conjugates are then further processed into cysteine
CC S-conjugates and finally mercapturic acids which are water soluble and
CC can be readily excreted in urine or bile. Alternatively, may have a
CC lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6-
CC acetylation of various proteins. Thereby, may regulate apoptosis
CC through the acetylation and the regulation of the expression of PROM1.
CC May also regulate amyloid beta-peptide secretion through acetylation of
CC BACE1 and the regulation of its expression in neurons (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an S-substituted L-cysteine = an N-acetyl-L-
CC cysteine-S-conjugate + CoA + H(+); Xref=Rhea:RHEA:19213,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58717, ChEBI:CHEBI:58718; EC=2.3.1.80;
CC Evidence={ECO:0000269|PubMed:6892478};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC -!- SUBUNIT: Interacts with PROM1. Interacts with BACE1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250}; Single-pass type II membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the camello family.
CC {ECO:0000269|PubMed:11397015}.
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DR EMBL; AF185570; AAF22298.1; -; mRNA.
DR RefSeq; NP_072157.1; NM_022635.1.
DR RefSeq; XP_006236851.1; XM_006236789.3.
DR RefSeq; XP_006236852.1; XM_006236790.3.
DR AlphaFoldDB; Q9QXT3; -.
DR SMR; Q9QXT3; -.
DR iPTMnet; Q9QXT3; -.
DR PhosphoSitePlus; Q9QXT3; -.
DR PRIDE; Q9QXT3; -.
DR Ensembl; ENSRNOT00000021243; ENSRNOP00000021243; ENSRNOG00000063398.
DR Ensembl; ENSRNOT00000097720; ENSRNOP00000080047; ENSRNOG00000063398.
DR Ensembl; ENSRNOT00000099459; ENSRNOP00000080565; ENSRNOG00000063398.
DR Ensembl; ENSRNOT00000102192; ENSRNOP00000083742; ENSRNOG00000063398.
DR GeneID; 64570; -.
DR KEGG; rno:64570; -.
DR UCSC; RGD:621609; rat.
DR CTD; 9027; -.
DR RGD; 621609; Nat8.
DR GeneTree; ENSGT00950000182932; -.
DR InParanoid; Q9QXT3; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; Q9QXT3; -.
DR BioCyc; MetaCyc:MON-10113; -.
DR UniPathway; UPA00204; -.
DR PRO; PR:Q9QXT3; -.
DR Proteomes; UP000002494; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0047198; F:cysteine-S-conjugate N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0018003; P:peptidyl-lysine N6-acetylation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..222
FT /note="N-acetyltransferase 8"
FT /id="PRO_0000284693"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..222
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 62..217
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ 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
