ATAT_AEDAE
ID ATAT_AEDAE Reviewed; 272 AA.
AC Q16Y34; Q16Y33;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Alpha-tubulin N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=TAT {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 {ECO:0000255|HAMAP-Rule:MF_03130};
GN ORFNames=AAEL008679;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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=B;
CC IsoId=Q16Y34-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q16Y34-2; Sequence=VSP_040230, VSP_040231;
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; CH477526; EAT39526.1; -; Genomic_DNA.
DR EMBL; CH477526; EAT39527.1; -; Genomic_DNA.
DR EMBL; CH477526; EAT39525.1; -; Genomic_DNA.
DR RefSeq; XP_001653412.1; XM_001653362.1.
DR RefSeq; XP_001653413.1; XM_001653363.1.
DR RefSeq; XP_001653414.1; XM_001653364.1.
DR AlphaFoldDB; Q16Y34; -.
DR SMR; Q16Y34; -.
DR STRING; 7159.AAEL008679-PB; -.
DR PRIDE; Q16Y34; -.
DR GeneID; 5570947; -.
DR KEGG; aag:5570947; -.
DR VEuPathDB; VectorBase:AAEL008679; -.
DR eggNOG; KOG4601; Eukaryota.
DR InParanoid; Q16Y34; -.
DR OMA; PPCSMAN; -.
DR OrthoDB; 1143678at2759; -.
DR PhylomeDB; Q16Y34; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IEA:UniProtKB-UniRule.
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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR038746; Atat.
DR InterPro; IPR007965; GNAT_ATAT.
DR PANTHER; PTHR12327; PTHR12327; 1.
DR Pfam; PF05301; Acetyltransf_16; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51730; GNAT_ATAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alternative splicing; Reference proteome; Transferase.
FT CHAIN 1..272
FT /note="Alpha-tubulin N-acetyltransferase"
FT /id="PRO_0000402070"
FT DOMAIN 1..186
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 216..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120..133
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT BINDING 156..165
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 205
FT /note="S -> R (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_040230"
FT VAR_SEQ 206..272
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_040231"
SQ SEQUENCE 272 AA; 30850 MW; 51601D9ADE442288 CRC64;
MEFRFNCHPL FRQRIVRINN SLLPTGFVAQ HRREALDATA QISEIINFVG QLSAQAQGLS
NPVTTSQKLR NSDHHIYLMF ESNQKHGLVV GILKVGRKSL YVFDQNGETV NVTAPCVLDF
YVHESRQRGG LGRELFDHML KEENIHPEEM AIDRPSEKLL GFLQKHYGLY KKIPQMNNFV
VYEGFFANKH HASDIDGRRM HITASPNTNL FGPTFTTVGE QRRSSSQTRQ QVVSPPVVQQ
PPVGRYAAKR PSCSMAQIIH NSPTTVSTEP NR
