NAT8_MOUSE
ID NAT8_MOUSE Reviewed; 227 AA.
AC Q9JIY7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAF80486.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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] {ECO:0000312|EMBL:BAB22356.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB22356.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:BAB22356.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH19517.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH19517.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH19517.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=22267734; DOI=10.1074/jbc.m111.310136;
RA Ding Y., Ko M.H., Pehar M., Kotch F., Peters N.R., Luo Y., Salamat S.M.,
RA Puglielli L.;
RT "Biochemical inhibition of the acetyltransferases ATase1 and ATase2 reduces
RT beta-secretase (BACE1) levels and Abeta generation.";
RL J. Biol. Chem. 287:8424-8433(2012).
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, ECO:0000269|PubMed:11397015}.
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 -!- 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 -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:22267734}.
CC -!- SIMILARITY: Belongs to the camello family.
CC {ECO:0000269|PubMed:11397015}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF163317; AAF80486.1; -; mRNA.
DR EMBL; AK002784; BAB22356.1; -; mRNA.
DR EMBL; BC019517; AAH19517.1; -; mRNA.
DR CCDS; CCDS20301.1; -.
DR RefSeq; NP_075944.1; NM_023455.3.
DR RefSeq; XP_006506598.1; XM_006506535.3.
DR RefSeq; XP_006506599.1; XM_006506536.2.
DR RefSeq; XP_006506600.1; XM_006506537.3.
DR AlphaFoldDB; Q9JIY7; -.
DR MINT; Q9JIY7; -.
DR STRING; 10090.ENSMUSP00000032073; -.
DR iPTMnet; Q9JIY7; -.
DR PhosphoSitePlus; Q9JIY7; -.
DR jPOST; Q9JIY7; -.
DR MaxQB; Q9JIY7; -.
DR PaxDb; Q9JIY7; -.
DR PeptideAtlas; Q9JIY7; -.
DR PRIDE; Q9JIY7; -.
DR ProteomicsDB; 287609; -.
DR DNASU; 68396; -.
DR Ensembl; ENSMUST00000032073; ENSMUSP00000032073; ENSMUSG00000030004.
DR GeneID; 68396; -.
DR KEGG; mmu:68396; -.
DR UCSC; uc009cqh.2; mouse.
DR CTD; 9027; -.
DR MGI; MGI:1915646; Nat8.
DR VEuPathDB; HostDB:ENSMUSG00000030004; -.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00950000182932; -.
DR HOGENOM; CLU_013985_10_1_1; -.
DR InParanoid; Q9JIY7; -.
DR OMA; VTLYYSM; -.
DR OrthoDB; 1341682at2759; -.
DR PhylomeDB; Q9JIY7; -.
DR TreeFam; TF324687; -.
DR UniPathway; UPA00204; -.
DR BioGRID-ORCS; 68396; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Nat8; mouse.
DR PRO; PR:Q9JIY7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JIY7; protein.
DR Bgee; ENSMUSG00000030004; Expressed in right kidney and 56 other tissues.
DR Genevisible; Q9JIY7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISA:MGI.
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; IMP: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:0007162; P:negative regulation of cell adhesion; ISA:MGI.
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..227
FT /note="N-acetyltransferase 8"
FT /id="PRO_0000284692"
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..227
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 69..217
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 227 AA; 25638 MW; D93A2DFB1FB61C7E CRC64;
MASFRIRQFQ ERDYKQVVDV FSRGMEEHIP TAFRHLLTLP RTLLLLAVVP LAIVLVSGSW
FLAVVCIFFL FLFLWFLASK PWKNYVSKCL HTDMADITKS YLSVRGSGFW VAESGGQVVG
TVAARPVKDP PLGRKQLQLF RLSVSSQHRG QGIAKALTRT VLQFARDQGY SDVVLVTGLL
QQGAVTLYYS MGFQKTGESF VDILTWLVDV SLIHFIYPLP SAQKYEL
