NAA60_MOUSE
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 03-AUG-2022, entry version 137.
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; Q9DBU2; -.
DR PRIDE; Q9DBU2; -.
DR ProteomicsDB; 287555; -.
DR Antibodypedia; 24137; 158 antibodies from 19 providers.
DR DNASU; 74763; -.
DR Ensembl; ENSMUST00000115860; ENSMUSP00000111526; ENSMUSG00000005982.
DR Ensembl; ENSMUST00000150655; ENSMUSP00000135206; ENSMUSG00000005982.
DR Ensembl; ENSMUST00000186375; ENSMUSP00000140031; ENSMUSG00000005982.
DR GeneID; 74763; -.
DR KEGG; mmu:74763; -.
DR UCSC; uc007xyw.1; mouse.
DR CTD; 79903; -.
DR MGI; MGI:1922013; Naa60.
DR VEuPathDB; HostDB:ENSMUSG00000005982; -.
DR eggNOG; KOG3138; Eukaryota.
DR GeneTree; ENSGT00390000008314; -.
DR InParanoid; Q9DBU2; -.
DR OMA; IYPTIAY; -.
DR OrthoDB; 1619974at2759; -.
DR PhylomeDB; Q9DBU2; -.
DR TreeFam; TF323980; -.
DR BioGRID-ORCS; 74763; 4 hits in 72 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 262 other tissues.
DR ExpressionAtlas; Q9DBU2; baseline and differential.
DR Genevisible; Q9DBU2; MM.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
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:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; 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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR045141; NAA60-like.
DR PANTHER; PTHR14744; PTHR14744; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
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
