NAA40_MOUSE
ID NAA40_MOUSE Reviewed; 237 AA.
AC Q8VE10; Q3V3R7; Q6PE89; Q9D4I5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000312|MGI:MGI:1918249};
DE EC=2.3.1.257 {ECO:0000250|UniProtKB:Q86UY6};
DE AltName: Full=N-acetyltransferase 11;
DE AltName: Full=N-alpha-acetyltransferase D {ECO:0000250|UniProtKB:Q86UY6};
DE Short=NatD {ECO:0000250|UniProtKB:Q86UY6};
DE AltName: Full=Protein acetyltransferase 1 {ECO:0000303|PubMed:22231784};
GN Name=Naa40 {ECO:0000312|MGI:MGI:1918249};
GN Synonyms=Nat11, Patt1 {ECO:0000303|PubMed:22231784};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon, Testis, and Urinary bladder;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Spleen, and Testis;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22231784; DOI=10.1194/jlr.m019257;
RA Liu Y., Zhou D., Zhang F., Tu Y., Xia Y., Wang H., Zhou B., Zhang Y.,
RA Wu J., Gao X., He Z., Zhai Q.;
RT "Liver Patt1 deficiency protects male mice from age-associated but not
RT high-fat diet-induced hepatic steatosis.";
RL J. Lipid Res. 53:358-367(2012).
CC -!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the
CC acetylation of the N-terminal residues of histones H4 and H2A (By
CC similarity). In contrast to other N-alpha-acetyltransferase, has a very
CC specific selectivity for histones H4 and H2A N-terminus and
CC specifically recognizes the 'Ser-Gly-Arg-Gly sequence' (By similarity).
CC Acts as a negative regulator of apoptosis (By similarity). May play a
CC role in hepatic lipid metabolism (PubMed:22231784).
CC {ECO:0000250|UniProtKB:Q86UY6, ECO:0000269|PubMed:22231784}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[histone H4]; Xref=Rhea:RHEA:50596,
CC Rhea:RHEA-COMP:12740, Rhea:RHEA-COMP:12743, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.257;
CC Evidence={ECO:0000250|UniProtKB:Q86UY6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-seryl-[histone H2A];
CC Xref=Rhea:RHEA:50600, Rhea:RHEA-COMP:12742, Rhea:RHEA-COMP:12744,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.257;
CC Evidence={ECO:0000250|UniProtKB:Q86UY6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86UY6}. Nucleus
CC {ECO:0000250|UniProtKB:Q86UY6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VE10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VE10-2; Sequence=VSP_024745;
CC Name=3;
CC IsoId=Q8VE10-3; Sequence=VSP_024744, VSP_024746;
CC -!- DISRUPTION PHENOTYPE: Liver-specific knockout male mice have decreased
CC body mass and are protected from age-associated hepatic steatosis. Male
CC mice show a reduction in the liver triglyceride and free fatty acid
CC levels. No effect on liver cholesterol level, liver weight, and liver
CC function is observed. {ECO:0000269|PubMed:22231784}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. NAA40 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30275.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK016504; BAB30275.1; ALT_FRAME; mRNA.
DR EMBL; AK033896; BAC28506.1; -; mRNA.
DR EMBL; AK035418; BAE20496.1; -; mRNA.
DR EMBL; AK170548; BAE41873.1; -; mRNA.
DR EMBL; BC020020; AAH20020.1; -; mRNA.
DR EMBL; BC058212; AAH58212.1; -; mRNA.
DR CCDS; CCDS50377.1; -. [Q8VE10-1]
DR RefSeq; NP_081919.1; NM_027643.1. [Q8VE10-1]
DR AlphaFoldDB; Q8VE10; -.
DR SMR; Q8VE10; -.
DR BioGRID; 214405; 2.
DR STRING; 10090.ENSMUSP00000025675; -.
DR iPTMnet; Q8VE10; -.
DR PhosphoSitePlus; Q8VE10; -.
DR EPD; Q8VE10; -.
DR MaxQB; Q8VE10; -.
DR PaxDb; Q8VE10; -.
DR PeptideAtlas; Q8VE10; -.
DR PRIDE; Q8VE10; -.
DR ProteomicsDB; 293612; -. [Q8VE10-1]
DR ProteomicsDB; 293613; -. [Q8VE10-2]
DR ProteomicsDB; 293614; -. [Q8VE10-3]
DR Antibodypedia; 43913; 79 antibodies from 24 providers.
DR Ensembl; ENSMUST00000025675; ENSMUSP00000025675; ENSMUSG00000024764. [Q8VE10-1]
DR GeneID; 70999; -.
DR KEGG; mmu:70999; -.
DR UCSC; uc008gkk.2; mouse. [Q8VE10-3]
DR UCSC; uc008gkl.2; mouse. [Q8VE10-1]
DR CTD; 79829; -.
DR MGI; MGI:1918249; Naa40.
DR VEuPathDB; HostDB:ENSMUSG00000024764; -.
DR eggNOG; KOG2488; Eukaryota.
DR GeneTree; ENSGT00390000014903; -.
DR HOGENOM; CLU_051699_4_0_1; -.
DR InParanoid; Q8VE10; -.
DR OMA; AYLHYRF; -.
DR OrthoDB; 1489686at2759; -.
DR PhylomeDB; Q8VE10; -.
DR TreeFam; TF315129; -.
DR BioGRID-ORCS; 70999; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Naa40; mouse.
DR PRO; PR:Q8VE10; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8VE10; protein.
DR Bgee; ENSMUSG00000024764; Expressed in spermatocyte and 254 other tissues.
DR ExpressionAtlas; Q8VE10; baseline and differential.
DR Genevisible; Q8VE10; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043998; F:H2A histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039949; NAA40.
DR PANTHER; PTHR20531; PTHR20531; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Lipoprotein; Myristate;
KW Nucleus; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..237
FT /note="N-alpha-acetyltransferase 40"
FT /id="PRO_0000284898"
FT DOMAIN 63..216
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 127..129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 140..142
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 148..153
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 179
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT SITE 139
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024744"
FT VAR_SEQ 1..35
FT /note="MGRKSSKAKEKKQKRLEERAAMDAVCAKVDAANRL -> MSALCPQF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024745"
FT VAR_SEQ 118..137
FT /note="PVAFSHFRFDVECGDEVLYC -> MGLQAPSLGLGAHSSAFSVS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024746"
SQ SEQUENCE 237 AA; 27229 MW; A3574555906CDEE1 CRC64;
MGRKSSKAKE KKQKRLEERA AMDAVCAKVD AANRLGDPLE AFPVFKKYDR NGLNVSIECK
RVSGLEPATV DWAFDLTKTN MQTMYEQSEW GWKDREKREE MTDDRAWYLI AWENSSIPVA
FSHFRFDVEC GDEVLYCYEV QLESKVRRKG LGKFLIQILQ LMANSTQMKK VMLTVFKHNH
GAYQFFREAL QFEIDDSSPS MSGCCGEDCS YEILSRRTKF GDSQHSHTGG HCGGCCH
