ID   NAA60_DANRE             Reviewed;         242 AA.
AC   A3KPA3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
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; ORFNames=zgc:163109;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the acetyltransferase family. NAA60 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC134236; AAI34237.1; -; mRNA.
DR   RefSeq; NP_001076341.1; NM_001082872.1.
DR   AlphaFoldDB; A3KPA3; -.
DR   SMR; A3KPA3; -.
DR   STRING; 7955.ENSDARP00000081428; -.
DR   PaxDb; 7955-ENSDARP00000081428; -.
DR   GeneID; 570640; -.
DR   KEGG; dre:570640; -.
DR   AGR; ZFIN:ZDB-GENE-041111-143; -.
DR   ZFIN; ZDB-GENE-041111-143; nat15.
DR   eggNOG; KOG3138; Eukaryota.
DR   HOGENOM; CLU_013985_5_4_1; -.
DR   InParanoid; A3KPA3; -.
DR   OMA; FDYIHHI; -.
DR   OrthoDB; 886671at2759; -.
DR   PhylomeDB; A3KPA3; -.
DR   TreeFam; TF323980; -.
DR   PRO; PR:A3KPA3; -.
DR   Proteomes; UP000000437; Chromosome 3.
DR   Bgee; ENSDARG00000061185; Expressed in mature ovarian follicle and 28 other cell types or tissues.
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.
PE   2: Evidence at transcript level;
KW   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_0000321569"
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"
SQ   SEQUENCE   242 AA;  27601 MW;  8FC6B77734949A09 CRC64;
     MTDVVPTTAL SEIQLRLLCH DDIDRIKVLC GEWFPIEYPD SWYHDITSNK KFFSLAATFR
     GGIVGMIVAE IKSRTKVHKE DGDILASSFP VDTQVAYILS LGVVKEFRKH GIGSLLLDSL
     KEHISTTAQD HCKAIYLHVL TTNNTAIHFY ENRDFKQHHY LPYYYSIRGV LKDGFTYVLY
     INGGHPPWTI FDYIHHIGSA LASLSPCSIP QRIYRQAQNL LRSFLPWSGI SSKSGIEYSR
     TM
//