NAA30_XENLA
ID NAA30_XENLA Reviewed; 273 AA.
AC Q0IHH1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=N-alpha-acetyltransferase 30;
DE EC=2.3.1.256 {ECO:0000250|UniProtKB:Q147X3};
DE AltName: Full=N-acetyltransferase 12;
DE AltName: Full=N-acetyltransferase MAK3 homolog;
DE AltName: Full=NatC catalytic subunit;
GN Name=naa30; Synonyms=mak3, nat12;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the N-terminal acetyltransferase C
CC (NatC) complex. Catalyzes acetylation of the N-terminal methionine
CC residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly.
CC Necessary for the lysosomal localization and function of ARL8B
CC sugeesting that ARL8B is a NatC substrate.
CC {ECO:0000250|UniProtKB:Q147X3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-
CC [protein]; Xref=Rhea:RHEA:50524, Rhea:RHEA-COMP:12713, Rhea:RHEA-
CC COMP:12714, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133379, ChEBI:CHEBI:133380; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-
CC [protein]; Xref=Rhea:RHEA:50560, Rhea:RHEA-COMP:12724, Rhea:RHEA-
CC COMP:12725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133386, ChEBI:CHEBI:133387; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase C (NatC)
CC complex. {ECO:0000250|UniProtKB:Q147X3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q147X3}. Nucleus
CC {ECO:0000250|UniProtKB:Q147X3}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC123156; AAI23157.1; -; mRNA.
DR RefSeq; NP_001090313.1; NM_001096844.1.
DR AlphaFoldDB; Q0IHH1; -.
DR SMR; Q0IHH1; -.
DR BioGRID; 607929; 1.
DR IntAct; Q0IHH1; 1.
DR DNASU; 779222; -.
DR GeneID; 779222; -.
DR KEGG; xla:779222; -.
DR CTD; 779222; -.
DR Xenbase; XB-GENE-877045; naa30.S.
DR OrthoDB; 1323575at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 779222; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031417; C:NatC complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR044542; NAA30-like.
DR PANTHER; PTHR45896; PTHR45896; 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; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..273
FT /note="N-alpha-acetyltransferase 30"
FT /id="PRO_0000320034"
FT DOMAIN 125..273
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 31074 MW; D5D916DD6A7B90ED CRC64;
MADAPSGPSV LSHYPGAGLA GEQQREEERH KGCHHHQLNG LISPDLRHLK AVSSLKNKLL
EQKTRKDSGL VQPQGRTDTR APNGLERLQG EEEKLSACLA SCSLRGDGEA LGNHVSQGEN
DDTIRYVRYE SELQMADIMR LITRDLSEPY SIYTYRYFIH NWPQLCFLAM VGEECVGAIV
CKLDMHKKMF RRGYIAMLAV DSKYRRKGIG THLVKKAIYA MVEGDCDEVV LETEITNKSA
LKLYENLGFV RDKRLFRYYL NGVDALRLKL WLR
