NAA60_XENTR
ID NAA60_XENTR Reviewed; 242 AA.
AC A8E5V7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-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; BC153734; AAI53735.1; -; mRNA.
DR RefSeq; NP_001106444.1; NM_001112973.1.
DR RefSeq; XP_012825451.1; XM_012969997.2.
DR AlphaFoldDB; A8E5V7; -.
DR SMR; A8E5V7; -.
DR STRING; 8364.ENSXETP00000063481; -.
DR PaxDb; A8E5V7; -.
DR DNASU; 100127619; -.
DR Ensembl; ENSXETT00000060272; ENSXETP00000063481; ENSXETG00000031356.
DR GeneID; 100127619; -.
DR KEGG; xtr:100127619; -.
DR CTD; 79903; -.
DR Xenbase; XB-GENE-941561; naa60.
DR eggNOG; KOG3138; Eukaryota.
DR HOGENOM; CLU_013985_5_4_1; -.
DR InParanoid; A8E5V7; -.
DR OMA; IYPTIAY; -.
DR OrthoDB; 1619974at2759; -.
DR PhylomeDB; A8E5V7; -.
DR TreeFam; TF323980; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000031356; Expressed in 4-cell stage embryo and 12 other tissues.
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 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_0000321570"
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; 27575 MW; D9F47EBE43CC3FDB CRC64;
MSEEERPAAL ADTILRFLCH DDIDTVKELC ADWFPIEYPD SWYRDITSNK KFFSLAATYN
GQIVGMIVAE IKGRTKVHKE DGDILASSFS GDTQVAYILS LGVVKEFRKQ GIGSLLLESL
KSHISSTAQD HCKALYLHVL TTNSNAIRFY ENRHFHQHHY LPYYYSIRGV LQDAYTYVLY
LNGGHPPWTV MDYLQHLGSA LAGFSPCTLP QRIYRQAHTL LRSLLPWSSI SAKSGIEYSR
TM
