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Alpha-tubulin N-acetyltransferase 1 (Alpha-TAT) (Alpha-TAT1) (TAT) (EC 2.3.1.108) (Acetyltransferase mec-17 homolog)

 ATAT_DANRE              Reviewed;         297 AA.
Q6PH17; Q6NZT0;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 86.
RecName: Full=Alpha-tubulin N-acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03130};
Short=Alpha-TAT {ECO:0000255|HAMAP-Rule:MF_03130};
Short=Alpha-TAT1 {ECO:0000255|HAMAP-Rule:MF_03130};
Short=TAT {ECO:0000255|HAMAP-Rule:MF_03130};
EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130};
AltName: Full=Acetyltransferase mec-17 homolog {ECO:0000255|HAMAP-Rule:MF_03130};
Name=atat1 {ECO:0000255|HAMAP-Rule:MF_03130}; Synonyms=mec17;
ORFNames=si:ch211-152p11.5, zgc:65893;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Embryo;
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20829795; DOI=10.1038/nature09324;
Akella J.S., Wloga D., Kim J., Starostina N.G., Lyons-Abbott S.,
Morrissette N.S., Dougan S.T., Kipreos E.T., Gaertig J.;
"MEC-17 is an alpha-tubulin acetyltransferase.";
Nature 467:218-222(2010).
[4]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-188 IN COMPLEX WITH
ACETYL-COA, AND MUTAGENESIS OF GLN-53.
PubMed=23128673; DOI=10.1038/cr.2012.154;
Li W., Zhong C., Li L., Sun B., Wang W., Xu S., Zhang T., Wang C.,
Bao L., Ding J.;
"Molecular basis of the acetyltransferase activity of MEC-17 towards
alpha-tubulin.";
Cell Res. 22:1707-1711(2012).
[5]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-188 OF WILD-TYPE AND OF
MUTANT ALA-117 IN COMPLEX WITH ACETYL-COA, SUBUNIT, AND MUTAGENESIS OF
LEU-45; ASP-117; ARG-126; SER-131; ASP-151 AND SER-154.
PubMed=23105108; DOI=10.1074/jbc.C112.421222;
Kormendi V., Szyk A., Piszczek G., Roll-Mecak A.;
"Crystal structures of tubulin acetyltransferase reveal a conserved
catalytic core and the plasticity of the essential N terminus.";
J. Biol. Chem. 287:41569-41575(2012).
-!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the
lumenal side of microtubules. Promotes microtubule destabilization
and accelerates microtubule dynamics; this activity may be
independent of acetylation activity. Acetylates alpha-tubulin with
a slow enzymatic rate, due to a catalytic site that is not
optimized for acetyl transfer. Enters the microtubule through each
end and diffuses quickly throughout the lumen of microtubules.
Acetylates only long/old microtubules because of its slow
acetylation rate since it does not have time to act on dynamically
unstable microtubules before the enzyme is released. May be
involved in neuron development. Acetylates alpha-tubulin in
neurons, but not in cilia. {ECO:0000255|HAMAP-Rule:MF_03130,
ECO:0000269|PubMed:20829795}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA +
[alpha-tubulin]-N(6)-acetyl-L-lysine. {ECO:0000255|HAMAP-
Rule:MF_03130}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23105108,
ECO:0000269|PubMed:23128673}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130}.
Membrane, clathrin-coated pit {ECO:0000255|HAMAP-Rule:MF_03130}.
Cell junction, focal adhesion {ECO:0000255|HAMAP-Rule:MF_03130}.
Cell projection, axon {ECO:0000255|HAMAP-Rule:MF_03130}.
Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03130}.
Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-
Rule:MF_03130}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6PH17-1; Sequence=Displayed;
Name=2;
IsoId=Q6PH17-2; Sequence=VSP_040229;
-!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
developmental defects at 48 hours post-fertilization (hpf),
including cilia curved body shape, short body axis, hydrocephalus,
small head and small eyes. Morphants often do not respond, or have
slow startle response, when probed with a needle, consistent with
neuromuscular defects. {ECO:0000269|PubMed:20829795}.
-!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
{ECO:0000255|HAMAP-Rule:MF_03130}.
-----------------------------------------------------------------------
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EMBL; BX511233; CAM56330.1; -; Genomic_DNA.
EMBL; BC056749; AAH56749.1; -; mRNA.
EMBL; BC065981; AAH65981.1; -; mRNA.
RefSeq; NP_001315192.1; NM_001328263.1. [Q6PH17-1]
RefSeq; NP_001315193.1; NM_001328264.1.
RefSeq; NP_998423.1; NM_213258.2. [Q6PH17-2]
UniGene; Dr.6427; -.
PDB; 4H6U; X-ray; 2.45 A; A/B=1-188.
PDB; 4H6Z; X-ray; 2.70 A; A/B=1-186.
PDB; 4HKF; X-ray; 1.70 A; A=1-188.
PDB; 4YRH; X-ray; 2.86 A; A/B=2-185.
PDBsum; 4H6U; -.
PDBsum; 4H6Z; -.
PDBsum; 4HKF; -.
PDBsum; 4YRH; -.
SMR; Q6PH17; -.
STRING; 7955.ENSDARP00000049367; -.
PaxDb; Q6PH17; -.
DNASU; 406389; -.
Ensembl; ENSDART00000049368; ENSDARP00000049367; ENSDARG00000004472. [Q6PH17-2]
Ensembl; ENSDART00000103922; ENSDARP00000094698; ENSDARG00000004472. [Q6PH17-1]
GeneID; 406389; -.
KEGG; dre:406389; -.
CTD; 79969; -.
ZFIN; ZDB-GENE-040426-2120; atat1.
eggNOG; KOG4601; Eukaryota.
eggNOG; ENOG4111Q8H; LUCA.
GeneTree; ENSGT00390000008276; -.
HOGENOM; HOG000257795; -.
HOVERGEN; HBG055797; -.
InParanoid; Q6PH17; -.
KO; K19573; -.
OMA; TEPLCVL; -.
OrthoDB; EOG091G0F8N; -.
PhylomeDB; Q6PH17; -.
TreeFam; TF315643; -.
PRO; PR:Q6PH17; -.
Proteomes; UP000000437; Chromosome 19.
Bgee; ENSDARG00000004472; -.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:InterPro.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0050662; F:coenzyme binding; ISS:UniProtKB.
GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB.
GO; GO:0019799; F:tubulin N-acetyltransferase activity; IMP:UniProtKB.
GO; GO:0071929; P:alpha-tubulin acetylation; IMP:ZFIN.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
HAMAP; MF_03130; mec17; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR007965; GNAT_ATAT.
Pfam; PF05301; Acetyltransf_16; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51730; GNAT_ATAT; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Alternative splicing; Cell junction;
Cell projection; Coated pit; Complete proteome; Cytoplasm;
Cytoskeleton; Membrane; Reference proteome; Transferase.
CHAIN 1 297 Alpha-tubulin N-acetyltransferase 1.
/FTId=PRO_0000402067.
DOMAIN 1 184 N-acetyltransferase. {ECO:0000255|HAMAP-
Rule:MF_03130}.
REGION 118 131 Acetyl-CoA binding. {ECO:0000255|HAMAP-
Rule:MF_03130,
ECO:0000269|PubMed:23105108,
ECO:0000269|PubMed:23128673}.
REGION 154 163 Acetyl-CoA binding. {ECO:0000255|HAMAP-
Rule:MF_03130,
ECO:0000269|PubMed:23105108,
ECO:0000269|PubMed:23128673}.
SITE 53 53 Crucial for catalytic activity.
{ECO:0000255|HAMAP-Rule:MF_03130,
ECO:0000269|PubMed:23128673}.
VAR_SEQ 189 297 AVQLRKVPPRKPEGEIKPYSLMEREVVREEQRVLPWPFVRP
GGPPHSPPLLPSSPQSRSLSVGSSPSRAPLRPAAATVLQQG
QTPSSPLNDSCRAKRTSSLNRSRLSFH -> GTPPSPLTDQ
GMYGFFGPTEKSSPKKARGRDQTLFANGKRSGSGGAEGSPL
AICSPRGSPPLSPSTSVISSIPFSQCGILPQPGPASPRRGH
GPPAGSDPLIPAQRQLQGKTHQFSK (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_040229.
MUTAGEN 45 45 L->A: Reduces activity to 30%.
{ECO:0000269|PubMed:23105108}.
MUTAGEN 53 53 Q->A: Reduces activity to 1.5%.
{ECO:0000269|PubMed:23128673}.
MUTAGEN 117 117 D->A: Reduces activity to 3%. Causes the
formation of a constitutive dimer in
solution. {ECO:0000269|PubMed:23105108}.
MUTAGEN 126 126 R->E: Reduces activity to 19%.
{ECO:0000269|PubMed:23105108}.
MUTAGEN 131 131 S->L: No effect.
{ECO:0000269|PubMed:23105108}.
MUTAGEN 151 151 D->A: Reduces activity to 1%.
{ECO:0000269|PubMed:23105108}.
MUTAGEN 154 154 S->A: Reduces activity to 8%.
{ECO:0000269|PubMed:23105108}.
STRAND 1 4 {ECO:0000244|PDB:4H6U}.
HELIX 7 10 {ECO:0000244|PDB:4HKF}.
STRAND 13 20 {ECO:0000244|PDB:4HKF}.
HELIX 21 28 {ECO:0000244|PDB:4H6U}.
HELIX 35 52 {ECO:0000244|PDB:4HKF}.
HELIX 62 67 {ECO:0000244|PDB:4HKF}.
STRAND 71 77 {ECO:0000244|PDB:4HKF}.
HELIX 80 83 {ECO:0000244|PDB:4HKF}.
STRAND 86 95 {ECO:0000244|PDB:4HKF}.
STRAND 98 101 {ECO:0000244|PDB:4HKF}.
STRAND 107 110 {ECO:0000244|PDB:4HKF}.
STRAND 113 120 {ECO:0000244|PDB:4HKF}.
HELIX 122 124 {ECO:0000244|PDB:4HKF}.
HELIX 129 141 {ECO:0000244|PDB:4HKF}.
HELIX 145 147 {ECO:0000244|PDB:4HKF}.
STRAND 148 152 {ECO:0000244|PDB:4HKF}.
HELIX 155 165 {ECO:0000244|PDB:4HKF}.
STRAND 174 179 {ECO:0000244|PDB:4HKF}.
HELIX 181 183 {ECO:0000244|PDB:4HKF}.
SEQUENCE 297 AA; 33202 MW; 3F08861B19D635EB CRC64;
MDFPYDLNAL FPERISVLDS NLSAGRKAHG RPDPLPQVTT VIDELGKASS KAQQLPAPIT
SAAKLQANRH HLYLLKDGEQ NGGRGVIVGF LKVGYKKLFL LDQRGAHLET EPLCVLDFYV
TETLQRHGYG SELFDFMLKH KQVEPAQMAY DRPSPKFLSF LEKRYDLRNS VPQVNNFVVF
AGFFQSRSAV QLRKVPPRKP EGEIKPYSLM EREVVREEQR VLPWPFVRPG GPPHSPPLLP
SSPQSRSLSV GSSPSRAPLR PAAATVLQQG QTPSSPLNDS CRAKRTSSLN RSRLSFH


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