NAA60_RAT
ID NAA60_RAT Reviewed; 242 AA.
AC Q3MHC1; Q7TMZ6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RA Luna F., de la Chesnaye E., Ojeda S.R.;
RT "GNAT family mRNA in the developing rat ovary.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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; AY316589; AAP83441.1; -; mRNA.
DR EMBL; BC105304; AAI05305.1; -; mRNA.
DR RefSeq; NP_001014248.2; NM_001014226.2.
DR AlphaFoldDB; Q3MHC1; -.
DR SMR; Q3MHC1; -.
DR STRING; 10116.ENSRNOP00000009936; -.
DR PaxDb; Q3MHC1; -.
DR Ensembl; ENSRNOT00000009936; ENSRNOP00000009936; ENSRNOG00000007280.
DR GeneID; 363545; -.
DR KEGG; rno:363545; -.
DR UCSC; RGD:1308915; rat.
DR CTD; 79903; -.
DR RGD; 1308915; Naa60.
DR eggNOG; KOG3138; Eukaryota.
DR GeneTree; ENSGT00390000008314; -.
DR HOGENOM; CLU_013985_5_4_1; -.
DR InParanoid; Q3MHC1; -.
DR OMA; IYPTIAY; -.
DR OrthoDB; 1619974at2759; -.
DR PhylomeDB; Q3MHC1; -.
DR TreeFam; TF323980; -.
DR PRO; PR:Q3MHC1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000007280; Expressed in liver and 19 other tissues.
DR Genevisible; Q3MHC1; RN.
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_0000321568"
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"
FT CONFLICT 232
FT /note="S -> T (in Ref. 1; AAP83441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 242 AA; 27493 MW; F2307DFB07F13F84 CRC64;
MTEVVPSSAL SEVSLRLLCH DDIDTVKHLC GDWFPIEYPD SWYRDITSNK KFFSLAATYR
GAIVGMIVAE IKNRTKIHKE DGDILASSFS VDTQVAYILS LGVVKEFRKH GIGSLLLESL
KDHISTTAQD HCKAIYLHVL TTNNTAINFY ENRDFRQHHY LPYYYSIRGV LKDGFTYVLY
INGGHPPWTI LDYIQHLGSA LANLSPCSIP HRIYRQAHSL LCSFLPWSSI SSKGGIEYSR
TM
