NAA10_BOVIN
ID NAA10_BOVIN Reviewed; 235 AA.
AC Q2KI14;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=N-alpha-acetyltransferase 10;
DE EC=2.3.1.255 {ECO:0000250|UniProtKB:P41227};
DE AltName: Full=N-terminal acetyltransferase complex ARD1 subunit homolog A;
DE AltName: Full=NatA catalytic subunit Naa10;
GN Name=NAA10; Synonyms=ARD1A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of N-terminal acetyltransferase complexes
CC which display alpha (N-terminal) acetyltransferase activity (By
CC similarity). Acetylates amino termini that are devoid of initiator
CC methionine (By similarity). The alpha (N-terminal) acetyltransferase
CC activity may be important for vascular, hematopoietic and neuronal
CC growth and development (By similarity). Without NAA15, displays epsilon
CC (internal) acetyltransferase activity towards HIF1A, thereby promoting
CC its degradation (By similarity). Represses MYLK kinase activity by
CC acetylation, and thus represses tumor cell migration (By similarity).
CC Acetylates, and stabilizes TSC2, thereby repressing mTOR activity and
CC suppressing cancer development (By similarity). Acetylates HSPA1A and
CC HSPA1B at 'Lys-77' which enhances its chaperone activity and leads to
CC preferential binding to co-chaperone HOPX (By similarity). Acetylates
CC HIST1H4A. Acts as a negative regulator of sister chromatid cohesion
CC during mitosis (By similarity). {ECO:0000250|UniProtKB:P41227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133369; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC ChEBI:CHEBI:133371; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC ChEBI:CHEBI:133375; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A complex (also
CC called the NatA complex) composed of NAA10 and NAA15 (By similarity).
CC Within the complex interacts with NAA15 (By similarity). Component of
CC the N-terminal acetyltransferase A (NatA)/HYPK complex at least
CC composed of NAA10, NAA15 and HYPK, which has N-terminal
CC acetyltransferase activity (By similarity). In complex with NAA15,
CC interacts with HYPK (By similarity). Component of the N-terminal
CC acetyltransferase E (NatE) complex at least composed of NAA10, NAA15
CC and NAA50 (By similarity). Within the complex interacts with NAA15; the
CC interaction is required for binding to NAAT50 (By similarity).
CC Interacts with NAAT50 (By similarity). The interaction of the NatA
CC complex with NAA50 reduces the acetylation activity of the NatA complex
CC (By similarity). Component of the N-terminal acetyltransferase E
CC (NatE)/HYPK complex at least composed of NAA10, NAA15, NAA50 and HYPK
CC (By similarity). In complex with NAA15, interacts with HYPK; the
CC interaction with HYPK reduces the capacity of the NatA complex to
CC interact with NAA50 (By similarity). Interacts with HIF1A (via its ODD
CC domain); the interaction increases HIF1A protein stability during
CC normoxia, an down-regulates it when induced by hypoxia (By similarity).
CC Interacts with the ribosome (By similarity). Binds to MYLK (By
CC similarity). Interacts with NAA16 (By similarity). Interacts (via its
CC C-terminal domain) with TSC2, leading to its acetylation (By
CC similarity). Interacts with IKBKB (By similarity). Interacts with
CC HSPA1A and HSPA1B leading to its acetylation (By similarity).
CC {ECO:0000250|UniProtKB:P41227}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41227}. Nucleus
CC {ECO:0000250|UniProtKB:P41227}. Note=Also present in the free cytosolic
CC and cytoskeleton-bound polysomes. {ECO:0000250|UniProtKB:P41227}.
CC -!- PTM: Cleaved by caspases during apoptosis.
CC {ECO:0000250|UniProtKB:P41227}.
CC -!- PTM: Phosphorylation by IKBKB/IKKB at Ser-209 promotes its proteasome-
CC mediated degradation. {ECO:0000250|UniProtKB:P41227}.
CC -!- PTM: Autoacetylated at Lys-136 which stimulates its catalytic activity.
CC {ECO:0000250|UniProtKB:P41227}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC112807; AAI12808.1; -; mRNA.
DR RefSeq; NP_001039976.1; NM_001046511.1.
DR AlphaFoldDB; Q2KI14; -.
DR SMR; Q2KI14; -.
DR STRING; 9913.ENSBTAP00000053888; -.
DR PaxDb; Q2KI14; -.
DR PeptideAtlas; Q2KI14; -.
DR PRIDE; Q2KI14; -.
DR Ensembl; ENSBTAT00000064306; ENSBTAP00000055621; ENSBTAG00000047702.
DR GeneID; 613636; -.
DR KEGG; bta:613636; -.
DR CTD; 8260; -.
DR VEuPathDB; HostDB:ENSBTAG00000047702; -.
DR VGNC; VGNC:106831; NAA10.
DR eggNOG; KOG3235; Eukaryota.
DR GeneTree; ENSGT00550000074803; -.
DR InParanoid; Q2KI14; -.
DR OMA; MSMQNAN; -.
DR OrthoDB; 1489230at2759; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000047702; Expressed in laryngeal cartilage and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031415; C:NatA complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990190; F:peptide-glutamate-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR GO; GO:2000719; P:negative regulation of maintenance of mitotic sister chromatid cohesion, centromeric; ISS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 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; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..235
FT /note="N-alpha-acetyltransferase 10"
FT /id="PRO_0000249839"
FT DOMAIN 1..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..58
FT /note="Interaction with NAA15"
FT /evidence="ECO:0000250"
FT REGION 175..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 136
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 209
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41227"
SQ SEQUENCE 235 AA; 26521 MW; 31A7ACE949DBAB1D CRC64;
MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM
EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH
LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGSIENKM
EGKGNSLPSS GEACREEKGL VAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS
