ATAT1_DROME
ID ATAT1_DROME Reviewed; 461 AA.
AC Q9VSY4; Q95S14; Q9VSY5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Alpha-tubulin N-acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=TAT 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130};
DE AltName: Full=Acetyltransferase mec-17 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03130};
GN ORFNames=CG3967;
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, 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC -!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the
CC lumenal side of microtubules. Promotes microtubule destabilization and
CC accelerates microtubule dynamics; this activity may be independent of
CC acetylation activity. Acetylates alpha-tubulin with a slow enzymatic
CC rate, due to a catalytic site that is not optimized for acetyl
CC transfer. Enters the microtubule through each end and diffuses quickly
CC throughout the lumen of microtubules. Acetylates only long/old
CC microtubules because of its slow acetylation rate since it does not
CC have time to act on dynamically unstable microtubules before the enzyme
CC is released. {ECO:0000255|HAMAP-Rule:MF_03130}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H(+) + N(6)-
CC acetyl-L-lysyl-[alpha-tubulin]; Xref=Rhea:RHEA:15277, Rhea:RHEA-
CC COMP:11278, Rhea:RHEA-COMP:11279, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:61930; EC=2.3.1.108; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03130};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9VSY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9VSY4-2; Sequence=VSP_035094;
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; AE014296; AAF50275.2; -; Genomic_DNA.
DR EMBL; AE014296; AAF50276.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11967.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11968.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11969.1; -; Genomic_DNA.
DR EMBL; AY061003; AAL28551.1; -; mRNA.
DR RefSeq; NP_001261628.1; NM_001274699.1. [Q9VSY4-2]
DR RefSeq; NP_648309.1; NM_140052.2. [Q9VSY4-1]
DR RefSeq; NP_648310.1; NM_140053.2. [Q9VSY4-1]
DR RefSeq; NP_729487.1; NM_170630.2. [Q9VSY4-1]
DR RefSeq; NP_729488.1; NM_170631.1. [Q9VSY4-1]
DR RefSeq; NP_729489.1; NM_170632.2. [Q9VSY4-2]
DR AlphaFoldDB; Q9VSY4; -.
DR SMR; Q9VSY4; -.
DR BioGRID; 64480; 4.
DR IntAct; Q9VSY4; 1.
DR STRING; 7227.FBpp0076209; -.
DR PaxDb; Q9VSY4; -.
DR PRIDE; Q9VSY4; -.
DR DNASU; 39086; -.
DR EnsemblMetazoa; FBtr0076480; FBpp0076208; FBgn0035989. [Q9VSY4-2]
DR EnsemblMetazoa; FBtr0076481; FBpp0076209; FBgn0035989. [Q9VSY4-1]
DR EnsemblMetazoa; FBtr0076482; FBpp0076210; FBgn0035989. [Q9VSY4-1]
DR EnsemblMetazoa; FBtr0076483; FBpp0076211; FBgn0035989. [Q9VSY4-1]
DR EnsemblMetazoa; FBtr0076484; FBpp0076212; FBgn0035989. [Q9VSY4-1]
DR EnsemblMetazoa; FBtr0331584; FBpp0303974; FBgn0035989. [Q9VSY4-2]
DR GeneID; 39086; -.
DR KEGG; dme:Dmel_CG3967; -.
DR UCSC; CG3967-RA; d. melanogaster. [Q9VSY4-1]
DR UCSC; CG3967-RB; d. melanogaster.
DR CTD; 6898; -.
DR FlyBase; FBgn0035989; CG3967.
DR VEuPathDB; VectorBase:FBgn0035989; -.
DR eggNOG; KOG4601; Eukaryota.
DR GeneTree; ENSGT00390000008276; -.
DR HOGENOM; CLU_025013_4_1_1; -.
DR InParanoid; Q9VSY4; -.
DR OMA; PPCSMAN; -.
DR PhylomeDB; Q9VSY4; -.
DR BioGRID-ORCS; 39086; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG3967; fly.
DR GenomeRNAi; 39086; -.
DR PRO; PR:Q9VSY4; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035989; Expressed in second segment of antenna (Drosophila) and 31 other tissues.
DR ExpressionAtlas; Q9VSY4; baseline and differential.
DR Genevisible; Q9VSY4; DM.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IMP:FlyBase.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0048666; P:neuron development; IEA:UniProtKB-UniRule.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03130; mec17; 1.
DR InterPro; IPR038746; Atat.
DR InterPro; IPR007965; GNAT_ATAT.
DR PANTHER; PTHR12327; PTHR12327; 1.
DR Pfam; PF05301; Acetyltransf_16; 1.
DR PROSITE; PS51730; GNAT_ATAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Reference proteome; Transferase.
FT CHAIN 1..461
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000348069"
FT DOMAIN 2..189
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 196..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123..136
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT BINDING 159..168
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT SITE 57
FT /note="Crucial for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT VAR_SEQ 289..461
FT /note="SGNGNHDIPEIAEQLQRQSLADLEANSYEPEPEVEPEPEPEPEPEPEPEVIT
FT PPSPPPKSHTPTPPSVRSPEVAESIVGDNRRAPAFQLSKQHTGMKNRSFGVGMAVMPSS
FT KMEFDQMEREDFGVVKINRPPGHEVTSPGQDNTDAMSTVSSGGGGLTDQGYYDLKFYHN
FT KLW -> RIK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035094"
SQ SEQUENCE 461 AA; 50560 MW; 567F1C6B08EB9B68 CRC64;
MVEFRFDIKP LFAQPIIKVT SNLLPNTFRG DRRQCLDATS KMTEIIDQLG QLSATSQGLS
KPVTTAQRLR MSDNQTIYLL ADNEAGHNGA VLGLLKVGTK NLYLFDEAGK TRMVEQTPSI
LDFYVHESRQ RAGLGKRLFQ TMLNEEQWTA RKCSVDRPSE KLLSFLSKHY GLKRIIPQAN
NFVLYEGFFN DGESGNGGGN GHANGTPNGL HITNSPNTHL FGATYLGEDS NQRRGSQQQT
TPNARLQQIT QISPSGRYGA KRPTCSMAEI IHAGNSKGGN GNGSAEANSG NGNHDIPEIA
EQLQRQSLAD LEANSYEPEP EVEPEPEPEP EPEPEPEVIT PPSPPPKSHT PTPPSVRSPE
VAESIVGDNR RAPAFQLSKQ HTGMKNRSFG VGMAVMPSSK MEFDQMERED FGVVKINRPP
GHEVTSPGQD NTDAMSTVSS GGGGLTDQGY YDLKFYHNKL W
