NAA80_DROME
ID NAA80_DROME Reviewed; 178 AA.
AC Q59DX8; Q8IG82; Q9VH73;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=N-alpha-acetyltransferase 80 {ECO:0000303|PubMed:29581307};
DE Short=DmNAA80 {ECO:0000303|PubMed:29581307};
DE EC=2.3.1.- {ECO:0000269|PubMed:29581307};
GN Name=Naa80 {ECO:0000303|PubMed:29581307, ECO:0000312|FlyBase:FBgn0037747};
GN ORFNames=CG8481 {ECO:0000312|FlyBase:FBgn0037747};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA Svirskas R., Rubin G.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0007744|PDB:5WJD, ECO:0007744|PDB:5WJE}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 20-178 IN COMPLEX WITH ACETYL-COA
RP AND SUBSTRATE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TRP-46; ARG-53;
RP LYS-83; GLU-97 AND SER-98.
RX PubMed=29581307; DOI=10.1073/pnas.1719251115;
RA Goris M., Magin R.S., Foyn H., Myklebust L.M., Varland S., Ree R.,
RA Drazic A., Bhambra P., Stoeve S.I., Baumann M., Haug B.E., Marmorstein R.,
RA Arnesen T.;
RT "Structural determinants and cellular environment define processed actin as
RT the sole substrate of the N-terminal acetyltransferase NAA80.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:4405-4410(2018).
CC -!- FUNCTION: N-alpha-acetyltransferase that acetylates the amino terminal
CC acidic residue of proteins devoid of initiator methionine
CC (PubMed:29581307). Preferentially acts on proteins starting with Asp-
CC Asp-Asp and Glu-Glu-Glu sequences (PubMed:29581307). In vitro, shows
CC high activity towards N-terminal sequences starting with Met-Asp-Glu-
CC Leu, Met-Glu-Glu-Glu and Met-Asp-Asp-Asp (PubMed:29581307).
CC {ECO:0000269|PubMed:29581307}.
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:0000269|PubMed:29581307};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.55 mM for Asp-Asp-Asp-Ile peptide {ECO:0000269|PubMed:29581307};
CC KM=0.60 mM for Glu-Glu-Glu-Ile peptide {ECO:0000269|PubMed:29581307};
CC KM=1.03 mM for Met-Asp-Asp-Asp peptide {ECO:0000269|PubMed:29581307};
CC KM=1.03 mM for Met-Glu-Glu-Glu peptide {ECO:0000269|PubMed:29581307};
CC KM=0.38 mM for Met-Asp-Glu-Leu peptide {ECO:0000269|PubMed:29581307};
CC Note=kcat is 0.6 min(-1) for Asp-Asp-Asp-Ile peptide
CC (PubMed:29581307). kcat is 0.6 min(-1) for Glu-Glu-Glu-Ile peptide
CC (PubMed:29581307). kcat is 3.47 min(-1) for Met-Asp-Asp-Asp peptide
CC (PubMed:29581307). kcat is 3.45 min(-1) for Met-Glu-Glu-Glu peptide
CC (PubMed:29581307). kcat is 16.86 min(-1) for Met-Asp-Glu-Leu peptide
CC (PubMed:29581307). {ECO:0000269|PubMed:29581307};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q59DX8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q59DX8-2; Sequence=VSP_059904;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AE014297; AAF54446.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52942.1; -; Genomic_DNA.
DR EMBL; AY060239; AAL25278.1; -; mRNA.
DR EMBL; BT001904; AAN71693.1; -; mRNA.
DR EMBL; BT044285; ACH92350.1; -; mRNA.
DR RefSeq; NP_001014612.1; NM_001014612.3. [Q59DX8-1]
DR RefSeq; NP_649942.1; NM_141685.5. [Q59DX8-2]
DR PDB; 5WJD; X-ray; 2.00 A; A=20-178.
DR PDB; 5WJE; X-ray; 1.76 A; A=20-178.
DR PDBsum; 5WJD; -.
DR PDBsum; 5WJE; -.
DR AlphaFoldDB; Q59DX8; -.
DR SMR; Q59DX8; -.
DR IntAct; Q59DX8; 2.
DR STRING; 7227.FBpp0100038; -.
DR PaxDb; Q59DX8; -.
DR DNASU; 41195; -.
DR EnsemblMetazoa; FBtr0082134; FBpp0081612; FBgn0037747. [Q59DX8-2]
DR EnsemblMetazoa; FBtr0100583; FBpp0100038; FBgn0037747. [Q59DX8-1]
DR GeneID; 41195; -.
DR KEGG; dme:Dmel_CG8481; -.
DR UCSC; CG8481-RA; d. melanogaster.
DR UCSC; CG8481-RB; d. melanogaster. [Q59DX8-1]
DR CTD; 24142; -.
DR FlyBase; FBgn0037747; Naa80.
DR VEuPathDB; VectorBase:FBgn0037747; -.
DR eggNOG; KOG3397; Eukaryota.
DR GeneTree; ENSGT00390000000980; -.
DR HOGENOM; CLU_077855_1_0_1; -.
DR InParanoid; Q59DX8; -.
DR OMA; EYCAPIS; -.
DR OrthoDB; 1518613at2759; -.
DR PhylomeDB; Q59DX8; -.
DR BioGRID-ORCS; 41195; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41195; -.
DR PRO; PR:Q59DX8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037747; Expressed in second segment of antenna (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q59DX8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1905502; F:acetyl-CoA binding; IBA:GO_Central.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017190; P:N-terminal peptidyl-aspartic acid acetylation; IDA:UniProtKB.
DR GO; GO:0018002; P:N-terminal peptidyl-glutamic acid acetylation; IDA:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Reference proteome;
KW Transferase.
FT CHAIN 1..178
FT /note="N-alpha-acetyltransferase 80"
FT /id="PRO_0000445573"
FT DOMAIN 26..178
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29581307,
FT ECO:0000312|PDB:5WJE"
FT BINDING 53..56
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29581307,
FT ECO:0000312|PDB:5WJE"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29581307,
FT ECO:0000312|PDB:5WJE"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29581307,
FT ECO:0000312|PDB:5WJE"
FT BINDING 99..101
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:29581307,
FT ECO:0000312|PDB:5WJD, ECO:0000312|PDB:5WJE"
FT BINDING 107..112
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:29581307,
FT ECO:0000312|PDB:5WJD, ECO:0000312|PDB:5WJE"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29581307,
FT ECO:0000312|PDB:5WJE"
FT BINDING 138
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:29581307,
FT ECO:0000312|PDB:5WJD, ECO:0000312|PDB:5WJE"
FT VAR_SEQ 1..11
FT /note="MRYIKSEPYYE -> M (in isoform 2)"
FT /id="VSP_059904"
FT MUTAGEN 46
FT /note="W->A: Reduced acetyltransferase activity; when
FT associated with A-53."
FT /evidence="ECO:0000269|PubMed:29581307"
FT MUTAGEN 53
FT /note="R->A: Reduced acetyltransferase activity; when
FT associated with A-46."
FT /evidence="ECO:0000269|PubMed:29581307"
FT MUTAGEN 83
FT /note="K->A: Reduced acetyltransferase activity; when
FT associated with A-98."
FT /evidence="ECO:0000269|PubMed:29581307"
FT MUTAGEN 97
FT /note="E->A,Q: Does not affect acetyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29581307"
FT MUTAGEN 98
FT /note="S->A: Reduced acetyltransferase activity; when
FT associated with A-83."
FT /evidence="ECO:0000269|PubMed:29581307"
FT CONFLICT 14
FT /note="P -> S (in Ref. 4; AAN71693)"
FT /evidence="ECO:0000305"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:5WJE"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:5WJE"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:5WJE"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:5WJE"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:5WJE"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:5WJE"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:5WJE"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:5WJE"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5WJE"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:5WJE"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:5WJE"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:5WJE"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5WJD"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:5WJE"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:5WJE"
SQ SEQUENCE 178 AA; 20373 MW; A21900F99B56FB79 CRC64;
MRYIKSEPYY EGLPPFNVSG SPFNVVPIHN YPELMKDTCA LINAEWPRSE TARMRSLEAS
CDSLPCSLVL TTEGMCRVIA HLKLSPINSK KKACFVESVV VDKRHRGQGF GKLIMKFAED
YCRVVLDLKT IYLSTIDQDG FYERIGYEYC APITMYGPRH CELPSLQNAK KKYMKKVL
