(data stored in ACNUC5340 zone)

SWISSPROT: 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   11-DEC-2019, entry version 83.
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; Holometabola; 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}.
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   SMR; Q16Y34; -.
DR   STRING; 7159.AAEL008679-PB; -.
DR   EnsemblMetazoa; AAEL008679-RA; AAEL008679-PA; AAEL008679. [Q16Y34-2]
DR   EnsemblMetazoa; AAEL008679-RB; AAEL008679-PB; AAEL008679. [Q16Y34-1]
DR   EnsemblMetazoa; AAEL008679-RC; AAEL008679-PC; AAEL008679. [Q16Y34-2]
DR   GeneID; 5570947; -.
DR   KEGG; aag:5570947; -.
DR   eggNOG; KOG4601; Eukaryota.
DR   eggNOG; ENOG4111Q8H; LUCA.
DR   HOGENOM; HOG000257795; -.
DR   InParanoid; Q16Y34; -.
DR   KO; K19573; -.
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;
DR   PRODOM; Q16Y34.
DR   SWISS-2DPAGE; Q16Y34.
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          120..133
FT                   /note="Acetyl-CoA binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   REGION          156..165
FT                   /note="Acetyl-CoA binding"
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
//

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