NAA10_MOUSE
ID NAA10_MOUSE Reviewed; 235 AA.
AC Q9QY36;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=N-alpha-acetyltransferase 10;
DE EC=2.3.1.255 {ECO:0000250|UniProtKB:P41227};
DE AltName: Full=N-terminal acetyltransferase complex ARD1 subunit homolog A;
DE AltName: Full=NatA catalytic subunit Naa10;
GN Name=Naa10; Synonyms=Ard1, Ard1a, Te2;
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 [MRNA], FUNCTION, AND INTERACTION WITH HIF1A.
RC TISSUE=Embryo, and T-cell;
RX PubMed=12464182; DOI=10.1016/s0092-8674(02)01085-1;
RA Jeong J.-W., Bae M.-K., Ahn M.-Y., Kim S.-H., Sohn T.-K., Bae M.-H.,
RA Yoo M.-A., Song E.-J., Lee K.-J., Kim K.-W.;
RT "Regulation and destabilization of HIF-1alpha by ARD1-mediated
RT acetylation.";
RL Cell 111:709-720(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NAA15, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12888564; DOI=10.1074/jbc.m301218200;
RA Sugiura N., Adams S.M., Corriveau R.A.;
RT "An evolutionarily conserved N-terminal acetyltransferase complex
RT associated with neuronal development.";
RL J. Biol. Chem. 278:40113-40120(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A.;
RT "Comparative sequence analysis of the mouse L1cam locus and the
RT corresponding region of human Xq28.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and
RC 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).
CC -!- FUNCTION: Catalytic subunit of the N-terminal acetyltransferase A
CC (NatA) complex which displays alpha (N-terminal) acetyltransferase
CC activity (PubMed:12888564). Acetylates amino termini that are devoid of
CC initiator methionine (By similarity). The alpha (N-terminal)
CC acetyltransferase activity may be important for vascular, hematopoietic
CC and neuronal growth and development (By similarity). Without NAA15,
CC displays epsilon (internal) acetyltransferase activity towards HIF1A,
CC thereby promoting its degradation (PubMed:12464182). Represses MYLK
CC kinase activity by acetylation, and thus represses tumor cell migration
CC (By similarity). Acetylates, and stabilizes TSC2, thereby repressing
CC mTOR activity and suppressing cancer development (By similarity).
CC Acetylates HSPA1A and HSPA1B at 'Lys-77' which enhances its chaperone
CC activity and leads to preferential binding to co-chaperone HOPX (By
CC similarity). Acetylates HIST1H4A (By similarity). Acts as a negative
CC regulator of sister chromatid cohesion during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:P41227, ECO:0000269|PubMed:12464182,
CC ECO:0000269|PubMed:12888564}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133369; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC ChEBI:CHEBI:133371; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC ChEBI:CHEBI:133375; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A complex (also
CC called the NatA complex) composed of NAA10 and NAA15 (By similarity).
CC Interacts with NAA15 (PubMed:12888564). Component of the N-terminal
CC acetyltransferase A (NatA)/HYPK complex at least composed of NAA10,
CC NAA15 and HYPK, which has N-terminal acetyltransferase activity (By
CC similarity). In complex with NAA15, interacts with HYPK (By
CC similarity). Component of the N-terminal acetyltransferase E (NatE)
CC complex at least composed of NAA10, NAA15 and NAA50 (By similarity).
CC Within the complex interacts with NAA15; the interaction is required
CC for binding to NAAT50 (By similarity). Interacts with NAAT50 (By
CC similarity). The interaction of the NatA complex with NAA50 reduces the
CC acetylation activity of the NatA complex (By similarity). Component of
CC the N-terminal acetyltransferase E (NatE)/HYPK complex at least
CC composed of NAA10, NAA15, NAA50 and HYPK (By similarity). In complex
CC with NAA15, interacts with HYPK; the interaction with HYPK reduces the
CC capacity of the NatA complex to interact with NAA50 (By similarity).
CC Interacts with HIF1A (via its ODD domain); the interaction increases
CC HIF1A protein stability during normoxia, an down-regulates it when
CC induced by hypoxia (PubMed:12464182). Interacts with the ribosome (By
CC similarity). Binds to MYLK (By similarity). Interacts with NAA16 (By
CC similarity). Interacts (via its C-terminal domain) with TSC2, leading
CC to its acetylation (By similarity). Interacts with IKBKB (By
CC similarity). Interacts with HSPA1A and HSPA1B leading to its
CC acetylation (By similarity). {ECO:0000250|UniProtKB:P41227,
CC ECO:0000269|PubMed:12464182, ECO:0000269|PubMed:12888564}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12888564}. Nucleus
CC {ECO:0000250|UniProtKB:P41227}. Note=Also present in the free cytosolic
CC and cytoskeleton-bound polysomes. {ECO:0000250|UniProtKB:P41227}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12888564}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the developing brain from
CC 11.5 dpc through 17 dpc, continues to be expressed at P0, but then is
CC down-regulated. {ECO:0000269|PubMed:12888564}.
CC -!- PTM: Cleaved by caspases during apoptosis.
CC {ECO:0000250|UniProtKB:P41227}.
CC -!- PTM: Phosphorylation by IKBKB/IKKB at Ser-209 destabilises NAA10 and
CC promotes its proteasome-mediated degradation.
CC -!- PTM: Autoacetylated at Lys-136 which stimulates its catalytic activity.
CC {ECO:0000250|UniProtKB:P41227}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK014469; BAB29373.1; -; mRNA.
DR EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30217.1; -.
DR RefSeq; NP_063923.1; NM_019870.3.
DR AlphaFoldDB; Q9QY36; -.
DR SMR; Q9QY36; -.
DR BioGRID; 207880; 39.
DR IntAct; Q9QY36; 37.
DR STRING; 10090.ENSMUSP00000033763; -.
DR iPTMnet; Q9QY36; -.
DR PhosphoSitePlus; Q9QY36; -.
DR EPD; Q9QY36; -.
DR MaxQB; Q9QY36; -.
DR PaxDb; Q9QY36; -.
DR PRIDE; Q9QY36; -.
DR ProteomicsDB; 286135; -.
DR Antibodypedia; 31057; 175 antibodies from 29 providers.
DR DNASU; 56292; -.
DR Ensembl; ENSMUST00000033763; ENSMUSP00000033763; ENSMUSG00000031388.
DR GeneID; 56292; -.
DR KEGG; mmu:56292; -.
DR UCSC; uc009tng.2; mouse.
DR CTD; 8260; -.
DR MGI; MGI:1915255; Naa10.
DR VEuPathDB; HostDB:ENSMUSG00000031388; -.
DR eggNOG; KOG3235; Eukaryota.
DR GeneTree; ENSGT00550000074803; -.
DR InParanoid; Q9QY36; -.
DR OrthoDB; 1489230at2759; -.
DR PhylomeDB; Q9QY36; -.
DR TreeFam; TF300078; -.
DR BRENDA; 2.3.1.255; 3474.
DR BioGRID-ORCS; 56292; 12 hits in 76 CRISPR screens.
DR ChiTaRS; Naa10; mouse.
DR PRO; PR:Q9QY36; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9QY36; protein.
DR Bgee; ENSMUSG00000031388; Expressed in epiblast (generic) and 125 other tissues.
DR ExpressionAtlas; Q9QY36; baseline and differential.
DR Genevisible; Q9QY36; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031415; C:NatA complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016407; F:acetyltransferase activity; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:MGI.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990190; F:peptide-glutamate-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; ISO:MGI.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR GO; GO:2000719; P:negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric; ISS:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; ISO:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..235
FT /note="N-alpha-acetyltransferase 10"
FT /id="PRO_0000074533"
FT DOMAIN 1..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..58
FT /note="Interaction with NAA15"
FT /evidence="ECO:0000250"
FT REGION 196..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 136
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 209
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
SQ SEQUENCE 235 AA; 26520 MW; AD2991C519277F29 CRC64;
MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM
EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH
LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGKH MVLAALENKA
ENKGNVLLSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS
