ID   NAA60_MOUSE             Reviewed;         242 AA.
AC   Q9DBU2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=N-alpha-acetyltransferase 60;
DE            EC=2.3.1.259 {ECO:0000250|UniProtKB:Q9H7X0};
DE   AltName: Full=Histone acetyltransferase type B protein 4 {ECO:0000250|UniProtKB:Q9H7X0};
DE            Short=HAT4 {ECO:0000250|UniProtKB:Q9H7X0};
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9H7X0};
DE   AltName: Full=N-acetyltransferase 15;
DE   AltName: Full=N-alpha-acetyltransferase F;
DE            Short=NatF;
GN   Name=Naa60; Synonyms=Nat15;
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].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Thymus;
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].
RC   STRAIN=NMRI; TISSUE=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).
CC   -!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the
CC       acetylation of N-terminal residues of the transmembrane proteins, with
CC       a strong preference for N-termini facing the cytosol. Displays N-
CC       terminal acetyltransferase activity towards a range of N-terminal
CC       sequences including those starting with Met-Lys, Met-Val, Met-Ala and
CC       Met-Met. Required for normal chromosomal segregation during anaphase.
CC       May also show histone acetyltransferase activity; such results are
CC       however unclear in vivo and would require additional experimental
CC       evidences. {ECO:0000250|UniProtKB:Q9H7X0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-methionyl-[transmembrane protein] =
CC         CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-[transmembrane
CC         protein]; Xref=Rhea:RHEA:50604, Rhea:RHEA-COMP:12745, Rhea:RHEA-
CC         COMP:12746, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:64731, ChEBI:CHEBI:133414; EC=2.3.1.259;
CC         Evidence={ECO:0000250|UniProtKB:Q9H7X0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000250|UniProtKB:Q9H7X0};
CC   -!- SUBUNIT: Monomer and homodimer; monomer in presence of substrate and
CC       homodimer in its absence. {ECO:0000250|UniProtKB:Q9H7X0}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9H7X0}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9H7X0}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9H7X0}. Note=Probably forms a intramembrane
CC       hairpin-like structure in the membrane. {ECO:0000250|UniProtKB:Q9H7X0}.
CC   -!- PTM: Acetylated: autoacetylation is required for optimal
CC       acetyltransferase activity. {ECO:0000250|UniProtKB:Q9H7X0}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. NAA60 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AK004750; BAB23531.1; -; mRNA.
DR   EMBL; AK088736; BAC40538.1; -; mRNA.
DR   EMBL; BC004837; AAH04837.1; -; mRNA.
DR   CCDS; CCDS37239.1; -.
DR   RefSeq; NP_001277618.1; NM_001290689.1.
DR   RefSeq; NP_083366.1; NM_029090.3.
DR   RefSeq; XP_006522742.1; XM_006522679.1.
DR   RefSeq; XP_006522743.1; XM_006522680.2.
DR   AlphaFoldDB; Q9DBU2; -.
DR   SMR; Q9DBU2; -.
DR   STRING; 10090.ENSMUSP00000140031; -.
DR   iPTMnet; Q9DBU2; -.
DR   PhosphoSitePlus; Q9DBU2; -.
DR   MaxQB; Q9DBU2; -.
DR   PaxDb; 10090-ENSMUSP00000140031; -.
DR   ProteomicsDB; 287555; -.
DR   Pumba; Q9DBU2; -.
DR   Antibodypedia; 24137; 180 antibodies from 19 providers.
DR   DNASU; 74763; -.
DR   Ensembl; ENSMUST00000115860.8; ENSMUSP00000111526.2; ENSMUSG00000005982.15.
DR   Ensembl; ENSMUST00000150655.3; ENSMUSP00000135206.2; ENSMUSG00000005982.15.
DR   Ensembl; ENSMUST00000186375.8; ENSMUSP00000140031.2; ENSMUSG00000005982.15.
DR   GeneID; 74763; -.
DR   KEGG; mmu:74763; -.
DR   UCSC; uc007xyw.1; mouse.
DR   AGR; MGI:1922013; -.
DR   CTD; 79903; -.
DR   MGI; MGI:1922013; Naa60.
DR   VEuPathDB; HostDB:ENSMUSG00000005982; -.
DR   eggNOG; KOG3138; Eukaryota.
DR   GeneTree; ENSGT00390000008314; -.
DR   InParanoid; Q9DBU2; -.
DR   OMA; FDYIHHI; -.
DR   OrthoDB; 886671at2759; -.
DR   PhylomeDB; Q9DBU2; -.
DR   TreeFam; TF323980; -.
DR   BioGRID-ORCS; 74763; 4 hits in 78 CRISPR screens.
DR   ChiTaRS; Naa60; mouse.
DR   PRO; PR:Q9DBU2; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9DBU2; Protein.
DR   Bgee; ENSMUSG00000005982; Expressed in ankle joint and 266 other cell types or tissues.
DR   ExpressionAtlas; Q9DBU2; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; ISS:UniProtKB.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR045141; NAA60-like.
DR   PANTHER; PTHR14744; N-ALPHA-ACETYLTRANSFERASE 60; 1.
DR   PANTHER; PTHR14744:SF15; N-ALPHA-ACETYLTRANSFERASE 60; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   Genevisible; Q9DBU2; MM.
PE   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Chromatin regulator; Chromosome partition;
KW   Golgi apparatus; Membrane; Reference proteome; Transferase.
FT   CHAIN           1..242
FT                   /note="N-alpha-acetyltransferase 60"
FT                   /id="PRO_0000321567"
FT   TOPO_DOM        1..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   INTRAMEM        193..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   TOPO_DOM        237..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   DOMAIN          13..182
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          162..173
FT                   /note="Required for homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   BINDING         101..103
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   BINDING         109..114
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   BINDING         143
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   BINDING         150..153
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   MOD_RES         109
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT   MOD_RES         121
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7X0"
SQ   SEQUENCE   242 AA;  27507 MW;  F2307B2007F13F84 CRC64;
     MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK KFFSLAATYR
     GAIVGMIVAE IKNRTKIHKE DGDILASSFS VDTQVAYILS LGVVKEFRKH GIGSLLLESL
     KDHISTTAQD HCKAIYLHVL TTNNTAINFY ENRDFRQHHY LPYYYSIRGV LKDGFTYVLY
     INGGHPPWTI LDYIQHLGSA LANLSPCSIP HRIYRQAHSL LCSFLPWSSI STKGGIEYSR
     TM
//