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N-alpha-acetyltransferase 40 (EC 2.3.1.257) (N-acetyltransferase 11) (N-alpha-acetyltransferase D) (NatD) (Protein acetyltransferase 1)

 NAA40_MOUSE             Reviewed;         237 AA.
Q8VE10; Q3V3R7; Q6PE89; Q9D4I5;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
07-NOV-2018, entry version 125.
RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000312|MGI:MGI:1918249};
EC=2.3.1.257 {ECO:0000250|UniProtKB:Q86UY6};
AltName: Full=N-acetyltransferase 11;
AltName: Full=N-alpha-acetyltransferase D {ECO:0000250|UniProtKB:Q86UY6};
Short=NatD {ECO:0000250|UniProtKB:Q86UY6};
AltName: Full=Protein acetyltransferase 1 {ECO:0000303|PubMed:22231784};
Name=Naa40 {ECO:0000312|MGI:MGI:1918249};
Synonyms=Nat11, Patt1 {ECO:0000303|PubMed:22231784};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD;
TISSUE=Diencephalon, Testis, and Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22231784; DOI=10.1194/jlr.M019257;
Liu Y., Zhou D., Zhang F., Tu Y., Xia Y., Wang H., Zhou B., Zhang Y.,
Wu J., Gao X., He Z., Zhai Q.;
"Liver Patt1 deficiency protects male mice from age-associated but not
high-fat diet-induced hepatic steatosis.";
J. Lipid Res. 53:358-367(2012).
-!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the
acetylation of the N-terminal residues of histones H4 and H2A (By
similarity). In contrast to other N-alpha-acetyltransferase, has a
very specific selectivity for histones H4 and H2A N-terminus and
specifically recognizes the 'Ser-Gly-Arg-Gly sequence' (By
similarity). Acts as a negative regulator of apoptosis (By
similarity). May play a role in hepatic lipid metabolism
(PubMed:22231784). {ECO:0000250|UniProtKB:Q86UY6,
ECO:0000269|PubMed:22231784}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-seryl-[histone
H4] = an N-terminal-N(alpha)-acetyl-L-seryl-[histone H4] + CoA.
{ECO:0000250|UniProtKB:Q86UY6}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + an N-terminal-L-seryl-[histone
H2A] = an N-terminal-N(alpha)-acetyl-L-seryl-[histone H2A] + CoA.
{ECO:0000250|UniProtKB:Q86UY6}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86UY6}.
Nucleus {ECO:0000250|UniProtKB:Q86UY6}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8VE10-1; Sequence=Displayed;
Name=2;
IsoId=Q8VE10-2; Sequence=VSP_024745;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8VE10-3; Sequence=VSP_024744, VSP_024746;
Note=No experimental confirmation available.;
-!- DISRUPTION PHENOTYPE: Liver-specific knockout male mice have
decreased body mass and are protected from age-associated hepatic
steatosis. Male mice show a reduction in the liver triglyceride
and free fatty acid levels. No effect on liver cholesterol level,
liver weight, and liver function is observed.
{ECO:0000269|PubMed:22231784}.
-!- SIMILARITY: Belongs to the acetyltransferase family. NAA40
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB30275.1; Type=Frameshift; Positions=34; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AK016504; BAB30275.1; ALT_FRAME; mRNA.
EMBL; AK033896; BAC28506.1; -; mRNA.
EMBL; AK035418; BAE20496.1; -; mRNA.
EMBL; AK170548; BAE41873.1; -; mRNA.
EMBL; BC020020; AAH20020.1; -; mRNA.
EMBL; BC058212; AAH58212.1; -; mRNA.
CCDS; CCDS50377.1; -. [Q8VE10-1]
RefSeq; NP_081919.1; NM_027643.1. [Q8VE10-1]
UniGene; Mm.329605; -.
UniGene; Mm.474361; -.
ProteinModelPortal; Q8VE10; -.
SMR; Q8VE10; -.
BioGrid; 214405; 1.
STRING; 10090.ENSMUSP00000025675; -.
iPTMnet; Q8VE10; -.
PhosphoSitePlus; Q8VE10; -.
EPD; Q8VE10; -.
PaxDb; Q8VE10; -.
PeptideAtlas; Q8VE10; -.
PRIDE; Q8VE10; -.
Ensembl; ENSMUST00000025675; ENSMUSP00000025675; ENSMUSG00000024764. [Q8VE10-1]
GeneID; 70999; -.
KEGG; mmu:70999; -.
UCSC; uc008gkk.2; mouse. [Q8VE10-3]
UCSC; uc008gkl.2; mouse. [Q8VE10-1]
CTD; 79829; -.
MGI; MGI:1918249; Naa40.
eggNOG; KOG2488; Eukaryota.
eggNOG; ENOG4110YSF; LUCA.
GeneTree; ENSGT00390000014903; -.
HOGENOM; HOG000285996; -.
HOVERGEN; HBG104005; -.
InParanoid; Q8VE10; -.
KO; K20794; -.
OMA; MGWQPKI; -.
OrthoDB; EOG091G0M04; -.
PhylomeDB; Q8VE10; -.
TreeFam; TF315129; -.
ChiTaRS; Naa40; mouse.
PRO; PR:Q8VE10; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024764; Expressed in 270 organ(s), highest expression level in primary oocyte.
CleanEx; MM_NAT11; -.
Genevisible; Q8VE10; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043998; F:H2A histone acetyltransferase activity; ISS:UniProtKB.
GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; ISS:UniProtKB.
GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
GO; GO:0061187; P:regulation of chromatin silencing at rDNA; IBA:GO_Central.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR039949; NAA40.
PANTHER; PTHR20531; PTHR20531; 1.
Pfam; PF00583; Acetyltransf_1; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome; Cytoplasm;
Lipoprotein; Myristate; Nucleus; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 237 N-alpha-acetyltransferase 40.
/FTId=PRO_0000284898.
DOMAIN 63 216 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
REGION 127 129 Substrate binding.
{ECO:0000250|UniProtKB:Q86UY6}.
REGION 140 142 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q86UY6}.
REGION 148 153 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q86UY6}.
BINDING 85 85 Substrate.
{ECO:0000250|UniProtKB:Q86UY6}.
BINDING 138 138 Substrate.
{ECO:0000250|UniProtKB:Q86UY6}.
BINDING 174 174 Substrate.
{ECO:0000250|UniProtKB:Q86UY6}.
BINDING 179 179 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q86UY6}.
BINDING 197 197 Substrate.
{ECO:0000250|UniProtKB:Q86UY6}.
BINDING 211 211 Substrate.
{ECO:0000250|UniProtKB:Q86UY6}.
SITE 139 139 Essential for catalytic activity.
{ECO:0000250|UniProtKB:Q86UY6}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000255}.
VAR_SEQ 1 117 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024744.
VAR_SEQ 1 35 MGRKSSKAKEKKQKRLEERAAMDAVCAKVDAANRL -> MS
ALCPQF (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024745.
VAR_SEQ 118 137 PVAFSHFRFDVECGDEVLYC -> MGLQAPSLGLGAHSSAF
SVS (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024746.
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


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