NAA20_XENTR
ID NAA20_XENTR Reviewed; 178 AA.
AC Q6P632;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=N-alpha-acetyltransferase 20;
DE EC=2.3.1.254 {ECO:0000250|UniProtKB:P61599};
DE AltName: Full=Methionine N-acetyltransferase;
DE AltName: Full=N-acetyltransferase 5;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5;
DE Short=NatB complex subunit NAT5;
DE AltName: Full=NatB catalytic subunit;
GN Name=naa20; Synonyms=nat5;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the NatB complex which catalyzes
CC acetylation of the N-terminal methionine residues of peptides beginning
CC with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle
CC functions are overrepresented in the pool of NatB substrates. Required
CC for maintaining the structure and function of actomyosin fibers and for
CC proper cellular migration. {ECO:0000250|UniProtKB:P61599}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:50484, Rhea:RHEA-COMP:12694, Rhea:RHEA-
CC COMP:12695, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133356, ChEBI:CHEBI:133358; EC=2.3.1.254;
CC Evidence={ECO:0000250|UniProtKB:P61599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-
CC [protein]; Xref=Rhea:RHEA:50492, Rhea:RHEA-COMP:12698, Rhea:RHEA-
CC COMP:12699, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133361, ChEBI:CHEBI:133362; EC=2.3.1.254;
CC Evidence={ECO:0000250|UniProtKB:P61599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein];
CC Xref=Rhea:RHEA:50480, Rhea:RHEA-COMP:12692, Rhea:RHEA-COMP:12693,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133045, ChEBI:CHEBI:133063; EC=2.3.1.254;
CC Evidence={ECO:0000250|UniProtKB:P61599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein];
CC Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133359, ChEBI:CHEBI:133360; EC=2.3.1.254;
CC Evidence={ECO:0000250|UniProtKB:P61599};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex
CC which is composed of naa20 and naa25. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61599}. Nucleus
CC {ECO:0000250|UniProtKB:P61599}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC062502; AAH62502.1; -; mRNA.
DR RefSeq; NP_989110.1; NM_203779.1.
DR RefSeq; XP_012818293.1; XM_012962839.2.
DR AlphaFoldDB; Q6P632; -.
DR SMR; Q6P632; -.
DR STRING; 8364.ENSXETP00000014577; -.
DR GeneID; 394715; -.
DR KEGG; xtr:394715; -.
DR CTD; 51126; -.
DR Xenbase; XB-GENE-969863; naa20.
DR InParanoid; Q6P632; -.
DR OrthoDB; 1355894at2759; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000037147; Expressed in egg cell and 14 other tissues.
DR ExpressionAtlas; Q6P632; differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031416; C:NatB complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..178
FT /note="N-alpha-acetyltransferase 20"
FT /id="PRO_0000249843"
FT DOMAIN 2..157
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 178 AA; 20366 MW; 1965D5ACB4D3AD3F CRC64;
MTSLRPFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS ERKGGFFVDL FVRVSNQVAV
NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIVPLPH PVRPEDIE
