NAA60_DROME
ID NAA60_DROME Reviewed; 276 AA.
AC Q95SX8; B7Z0F9; Q8IH11; Q9VT42;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=N-alpha-acetyltransferase 60;
DE Short=dNaa60 {ECO:0000303|PubMed:21750686};
DE EC=2.3.1.259 {ECO:0000250|UniProtKB:Q9H7X0};
DE EC=2.3.1.48 {ECO:0000305|PubMed:21981917};
DE AltName: Full=NatF catalytic subunit;
GN Name=Naa60 {ECO:0000312|FlyBase:FBgn0036039}; ORFNames=CG18177;
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] {ECO:0000312|EMBL:AAS65049.1}
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] {ECO:0000305, ECO:0000312|EMBL:AAS65049.1}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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] {ECO:0000305, ECO:0000312|EMBL:AAL25476.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL25476.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 FUNCTION (ISOFORM A), FUNCTION (ISOFORM B), AND CATALYTIC ACTIVITY.
RX PubMed=21981917; DOI=10.1016/j.molcel.2011.07.032;
RA Yang X., Yu W., Shi L., Sun L., Liang J., Yi X., Li Q., Zhang Y., Yang F.,
RA Han X., Zhang D., Yang J., Yao Z., Shang Y.;
RT "HAT4, a Golgi apparatus-anchored B-type histone acetyltransferase,
RT acetylates free histone H4 and facilitates chromatin assembly.";
RL Mol. Cell 44:39-50(2011).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=21750686; DOI=10.1371/journal.pgen.1002169;
RA Van Damme P., Hole K., Pimenta-Marques A., Helsens K., Vandekerckhove J.,
RA Martinho R.G., Gevaert K., Arnesen T.;
RT "NatF contributes to an evolutionary shift in protein N-terminal
RT acetylation and is important for normal chromosome segregation.";
RL PLoS Genet. 7:E1002169-E1002169(2011).
CC -!- FUNCTION: Displays alpha (N-terminal) acetyltransferase activity
CC towards a range of N-terminal sequences including those starting with
CC Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal
CC segregation during anaphase. {ECO:0000269|PubMed:21750686}.
CC -!- FUNCTION: [Isoform A]: Shows histone acetyltransferase activity toward
CC free histones. {ECO:0000305|PubMed:21981917}.
CC -!- FUNCTION: [Isoform B]: Does not show histone acetyltransferase activity
CC toward free histones. {ECO:0000305|PubMed:21981917}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-[transmembrane protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-[transmembrane
CC protein]; Xref=Rhea:RHEA:50604, Rhea:RHEA-COMP:12745, Rhea:RHEA-
CC COMP:12746, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64731, ChEBI:CHEBI:133414; EC=2.3.1.259;
CC Evidence={ECO:0000250|UniProtKB:Q9H7X0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000305|PubMed:21981917};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A {ECO:0000269|PubMed:10731132};
CC IsoId=Q95SX8-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:10731132};
CC IsoId=Q95SX8-2; Sequence=VSP_041889;
CC Name=C {ECO:0000269|PubMed:10731132};
CC IsoId=Q95SX8-3; Sequence=VSP_041889, VSP_041890;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. NAA60 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAF50213.2; -; Genomic_DNA.
DR EMBL; AE014296; AAS65049.1; -; Genomic_DNA.
DR EMBL; AE014296; ACL83284.1; -; Genomic_DNA.
DR EMBL; AY060437; AAL25476.1; -; mRNA.
DR EMBL; BT001491; AAN71246.1; -; mRNA.
DR RefSeq; NP_001137929.1; NM_001144457.3. [Q95SX8-3]
DR RefSeq; NP_648353.3; NM_140096.5. [Q95SX8-2]
DR RefSeq; NP_996032.1; NM_206310.3. [Q95SX8-1]
DR AlphaFoldDB; Q95SX8; -.
DR SMR; Q95SX8; -.
DR BioGRID; 64530; 1.
DR IntAct; Q95SX8; 2.
DR STRING; 7227.FBpp0089006; -.
DR PaxDb; Q95SX8; -.
DR PRIDE; Q95SX8; -.
DR DNASU; 39142; -.
DR EnsemblMetazoa; FBtr0089410; FBpp0088430; FBgn0036039. [Q95SX8-2]
DR EnsemblMetazoa; FBtr0089411; FBpp0089006; FBgn0036039. [Q95SX8-1]
DR EnsemblMetazoa; FBtr0114566; FBpp0113058; FBgn0036039. [Q95SX8-3]
DR GeneID; 39142; -.
DR KEGG; dme:Dmel_CG18177; -.
DR UCSC; CG18177-RA; d. melanogaster. [Q95SX8-1]
DR UCSC; CG18177-RB; d. melanogaster.
DR CTD; 79903; -.
DR FlyBase; FBgn0036039; Naa60.
DR VEuPathDB; VectorBase:FBgn0036039; -.
DR eggNOG; KOG3138; Eukaryota.
DR GeneTree; ENSGT00390000008314; -.
DR InParanoid; Q95SX8; -.
DR OMA; IYPTIAY; -.
DR PhylomeDB; Q95SX8; -.
DR SignaLink; Q95SX8; -.
DR BioGRID-ORCS; 39142; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39142; -.
DR PRO; PR:Q95SX8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036039; Expressed in cleaving embryo and 25 other tissues.
DR Genevisible; Q95SX8; DM.
DR GO; GO:0005737; C:cytoplasm; IC:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; IMP:FlyBase.
DR GO; GO:0043966; P:histone H3 acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IDA:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR045141; NAA60-like.
DR PANTHER; PTHR14744; PTHR14744; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Chromatin regulator;
KW Chromosome partition; Reference proteome; Transferase.
FT CHAIN 1..276
FT /note="N-alpha-acetyltransferase 60"
FT /id="PRO_0000413363"
FT DOMAIN 34..239
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 204..215
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT ACT_SITE 180
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT BINDING 143..145
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT BINDING 151..156
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT BINDING 185
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT BINDING 192..195
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H7X0"
FT VAR_SEQ 102..122
FT /note="Missing (in isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_041889"
FT VAR_SEQ 234..276
FT /note="DHIKHYASMVRHTSSLCAWLAGRVQQVVRWFYHKLLTRFNFIE -> YPFSK
FT YLYALGCIAFLSMISLYFWLPS (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_041890"
SQ SEQUENCE 276 AA; 31869 MW; 45958EEBB2C3FFD3 CRC64;
MAQFTLYNKH SAPPSSESTR VDCEHVPLCS INDVQLRFLV PDDLTEVRQL CQEWFPIDYP
LSWYEDITSS TRFFALAAVY NLAIIGLIVA EIKPYRNVNK EVIANMSDSD ELYTRLSGFP
MQDKGILPDS MGRSADVGYI LSLGVHRSHR RNGIGSLLLD ALMNHLTTAE RHSVKAIFLH
TLTTNQPAIF FYEKRRFTLH SFLPYYYNIR GKGKDGFTYV NYINGGHPPW TLLDHIKHYA
SMVRHTSSLC AWLAGRVQQV VRWFYHKLLT RFNFIE
