NAA80_MOUSE
ID NAA80_MOUSE Reviewed; 314 AA.
AC Q9R123; Q8QZY5; Q8R014; Q9ERM0;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=N-alpha-acetyltransferase 80 {ECO:0000250|UniProtKB:Q93015};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q93015};
DE AltName: Full=N-acetyltransferase 6 {ECO:0000305};
DE AltName: Full=Protein fusion-2 homolog {ECO:0000303|Ref.1};
DE Short=Protein fus-2 {ECO:0000303|Ref.1};
GN Name=Naa80 {ECO:0000250|UniProtKB:Q93015};
GN Synonyms=Fus2, Nat6 {ECO:0000312|MGI:MGI:1888902};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Duh F.-M., Minna J.D., Lerman M.I.;
RT "The mouse ortholog of the human Fus2 gene.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Csoka A.B.;
RT "Genomic sequence of the mouse Hyal1 locus encoding the mouse Hyal1, Fus2,
RT and Hyal3 genes.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-231.
RC STRAIN=129/Sv;
RA Shuttleworth T.L., Triggs-Raine B.L., Wicklow B.A.;
RT "Isolation and characterization of the murine Hyal1 gene, encoding
RT hyaluronidase 1.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-204.
RC STRAIN=129/Sv;
RX PubMed=11929860; DOI=10.1074/jbc.m108991200;
RA Shuttleworth T.L., Wilson M.D., Wicklow B.A., Wilkins J.A.,
RA Triggs-Raine B.L.;
RT "Characterization of the murine hyaluronidase gene region reveals complex
RT organization and cotranscription of Hyal1 with downstream genes, Fus2 and
RT Hyal3.";
RL J. Biol. Chem. 277:23008-23018(2002).
CC -!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the
CC acetylation of the acidic amino terminus of processed forms of
CC beta- and gamma-actin (ACTB and ACTG, respectively). N-terminal
CC acetylation of processed beta- and gamma-actin regulates actin filament
CC depolymerization and elongation. In vivo, preferentially displays N-
CC terminal acetyltransferase activity towards acid N-terminal sequences
CC starting with Asp-Asp-Asp and Glu-Glu-Glu. In vitro, shows high
CC activity towards Met-Asp-Glu-Leu and Met-Asp-Asp-Asp. May act as a
CC tumor suppressor. {ECO:0000250|UniProtKB:Q93015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-aspartyl-L-aspartyl-L-aspartyl-
CC [protein] = CoA + H(+) + N-terminal N-acetyl-L-aspartyl-L-aspartyl-L-
CC aspartyl-[protein]; Xref=Rhea:RHEA:57328, Rhea:RHEA-COMP:14863,
CC Rhea:RHEA-COMP:14864, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:141602, ChEBI:CHEBI:141604;
CC Evidence={ECO:0000250|UniProtKB:Q93015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-glutamyl-L-glutamyl-L-glutamyl-
CC [protein] = CoA + H(+) + N-terminal N-acetyl-L-glutamyl-L-glutamyl-L-
CC glutamyl-[protein]; Xref=Rhea:RHEA:57324, Rhea:RHEA-COMP:14865,
CC Rhea:RHEA-COMP:14866, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:141603, ChEBI:CHEBI:141606;
CC Evidence={ECO:0000250|UniProtKB:Q93015};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q93015}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF172275; AAD48062.1; -; mRNA.
DR EMBL; AF338323; AAL57174.1; -; Genomic_DNA.
DR EMBL; BC026545; AAH26545.1; -; mRNA.
DR EMBL; AH009891; AAG23428.1; -; Genomic_DNA.
DR EMBL; AF417492; AAM14421.1; -; mRNA.
DR EMBL; AF417493; AAM14423.1; -; mRNA.
DR EMBL; AF417494; AAM14425.1; -; mRNA.
DR EMBL; AF417495; AAM14427.1; -; mRNA.
DR EMBL; AF417497; AAM14431.1; -; mRNA.
DR EMBL; AF417498; AAM14433.1; -; mRNA.
DR CCDS; CCDS23498.1; -.
DR RefSeq; NP_062724.1; NM_019750.4.
DR AlphaFoldDB; Q9R123; -.
DR SMR; Q9R123; -.
DR STRING; 10090.ENSMUSP00000091300; -.
DR iPTMnet; Q9R123; -.
DR PhosphoSitePlus; Q9R123; -.
DR MaxQB; Q9R123; -.
DR PaxDb; Q9R123; -.
DR PRIDE; Q9R123; -.
DR ProteomicsDB; 252645; -.
DR Antibodypedia; 34876; 193 antibodies from 21 providers.
DR DNASU; 56441; -.
DR Ensembl; ENSMUST00000093785; ENSMUSP00000091300; ENSMUSG00000079334.
DR GeneID; 56441; -.
DR KEGG; mmu:56441; -.
DR UCSC; uc009rly.1; mouse.
DR CTD; 24142; -.
DR MGI; MGI:1888902; Naa80.
DR VEuPathDB; HostDB:ENSMUSG00000079334; -.
DR eggNOG; KOG3397; Eukaryota.
DR GeneTree; ENSGT00390000000980; -.
DR HOGENOM; CLU_077855_0_0_1; -.
DR InParanoid; Q9R123; -.
DR OMA; THDQLHF; -.
DR PhylomeDB; Q9R123; -.
DR TreeFam; TF106312; -.
DR BioGRID-ORCS; 56441; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Naa80; mouse.
DR PRO; PR:Q9R123; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9R123; protein.
DR Bgee; ENSMUSG00000079334; Expressed in left lobe of liver and 220 other tissues.
DR ExpressionAtlas; Q9R123; baseline and differential.
DR Genevisible; Q9R123; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:1905502; F:acetyl-CoA binding; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISO:MGI.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030047; P:actin modification; ISS:UniProtKB.
DR GO; GO:0017190; P:N-terminal peptidyl-aspartic acid acetylation; ISS:UniProtKB.
DR GO; GO:0018002; P:N-terminal peptidyl-glutamic acid acetylation; ISS:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; ISO:MGI.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; ISS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039840; NAA80.
DR PANTHER; PTHR13538; PTHR13538; 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; Reference proteome; Transferase;
KW Tumor suppressor.
FT CHAIN 1..314
FT /note="N-alpha-acetyltransferase 80"
FT /id="PRO_0000074537"
FT DOMAIN 90..243
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 260..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q59DX8"
FT BINDING 118..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q59DX8"
FT BINDING 169..171
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q59DX8"
FT BINDING 177..182
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q59DX8"
FT BINDING 207
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q59DX8"
SQ SEQUENCE 314 AA; 34583 MW; C10445FF34332A73 CRC64;
MELILSTSPA KLTLDPARQP ELTLRFNLSK LTLDPARQPE LSLSPRLAEL TLDPTCHPEM
SLSPGPAELT LDPQHQAKEL PVPKLPELIL EPVHCRPELM SACADLINDQ WPRSRASRLH
SLGQSSDAFP LCLMLLSPQP TPGAAPVVVG HARLSRVLDQ PHSLLVETVV VARPLRGRGF
GRRLMEGLEA FARARGFRRL HLTTHDQLYF YAHLGYQLGE PVQGLAFTNR RLSTTVLRAF
SKPPCPQPPC KEPILAAQAV PRSSKGPPLP PPPPLPQSLT ASPPPSPEPL PQSPLETCYR
DLKGCPIFWM EKDI
