ATAT_DANRE
ID ATAT_DANRE Reviewed; 297 AA.
AC Q6PH17; Q6NZT0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Alpha-tubulin N-acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT1 {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 Name=atat1 {ECO:0000255|HAMAP-Rule:MF_03130}; Synonyms=mec17;
GN ORFNames=si:ch211-152p11.5, zgc:65893;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20829795; DOI=10.1038/nature09324;
RA Akella J.S., Wloga D., Kim J., Starostina N.G., Lyons-Abbott S.,
RA Morrissette N.S., Dougan S.T., Kipreos E.T., Gaertig J.;
RT "MEC-17 is an alpha-tubulin acetyltransferase.";
RL Nature 467:218-222(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-188 IN COMPLEX WITH ACETYL-COA,
RP AND MUTAGENESIS OF GLN-53.
RX PubMed=23128673; DOI=10.1038/cr.2012.154;
RA Li W., Zhong C., Li L., Sun B., Wang W., Xu S., Zhang T., Wang C., Bao L.,
RA Ding J.;
RT "Molecular basis of the acetyltransferase activity of MEC-17 towards alpha-
RT tubulin.";
RL Cell Res. 22:1707-1711(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-188 OF WILD-TYPE AND OF MUTANT
RP ALA-117 IN COMPLEX WITH ACETYL-COA, SUBUNIT, AND MUTAGENESIS OF LEU-45;
RP ASP-117; ARG-126; SER-131; ASP-151 AND SER-154.
RX PubMed=23105108; DOI=10.1074/jbc.c112.421222;
RA Kormendi V., Szyk A., Piszczek G., Roll-Mecak A.;
RT "Crystal structures of tubulin acetyltransferase reveal a conserved
RT catalytic core and the plasticity of the essential N terminus.";
RL J. Biol. Chem. 287:41569-41575(2012).
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. May be involved in neuron development. Acetylates alpha-
CC tubulin in neurons, but not in cilia. {ECO:0000255|HAMAP-Rule:MF_03130,
CC ECO:0000269|PubMed:20829795}.
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23105108,
CC ECO:0000269|PubMed:23128673}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130}.
CC Membrane, clathrin-coated pit {ECO:0000255|HAMAP-Rule:MF_03130}. Cell
CC junction, focal adhesion {ECO:0000255|HAMAP-Rule:MF_03130}. Cell
CC projection, axon {ECO:0000255|HAMAP-Rule:MF_03130}. Cytoplasm,
CC cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03130}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03130}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PH17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PH17-2; Sequence=VSP_040229;
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC developmental defects at 48 hours post-fertilization (hpf), including
CC cilia curved body shape, short body axis, hydrocephalus, small head and
CC small eyes. Morphants often do not respond, or have slow startle
CC response, when probed with a needle, consistent with neuromuscular
CC defects. {ECO:0000269|PubMed:20829795}.
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; BX511233; CAM56330.1; -; Genomic_DNA.
DR EMBL; BC056749; AAH56749.1; -; mRNA.
DR EMBL; BC065981; AAH65981.1; -; mRNA.
DR RefSeq; NP_001315192.1; NM_001328263.1. [Q6PH17-1]
DR RefSeq; NP_001315193.1; NM_001328264.1.
DR RefSeq; NP_998423.1; NM_213258.2. [Q6PH17-2]
DR PDB; 4H6U; X-ray; 2.45 A; A/B=1-188.
DR PDB; 4H6Z; X-ray; 2.70 A; A/B=1-186.
DR PDB; 4HKF; X-ray; 1.70 A; A=1-188.
DR PDB; 4YRH; X-ray; 2.86 A; A/B=2-185.
DR PDBsum; 4H6U; -.
DR PDBsum; 4H6Z; -.
DR PDBsum; 4HKF; -.
DR PDBsum; 4YRH; -.
DR AlphaFoldDB; Q6PH17; -.
DR SMR; Q6PH17; -.
DR STRING; 7955.ENSDARP00000049367; -.
DR PaxDb; Q6PH17; -.
DR DNASU; 406389; -.
DR Ensembl; ENSDART00000049368; ENSDARP00000049367; ENSDARG00000004472. [Q6PH17-2]
DR Ensembl; ENSDART00000103922; ENSDARP00000094698; ENSDARG00000004472. [Q6PH17-1]
DR GeneID; 406389; -.
DR KEGG; dre:406389; -.
DR CTD; 79969; -.
DR ZFIN; ZDB-GENE-040426-2120; atat1.
DR eggNOG; KOG4601; Eukaryota.
DR GeneTree; ENSGT00390000008276; -.
DR HOGENOM; CLU_949825_0_0_1; -.
DR InParanoid; Q6PH17; -.
DR OMA; SRQRCGQ; -.
DR OrthoDB; 1312675at2759; -.
DR PhylomeDB; Q6PH17; -.
DR TreeFam; TF315643; -.
DR PRO; PR:Q6PH17; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000004472; Expressed in head and 17 other tissues.
DR ExpressionAtlas; Q6PH17; baseline.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IMP:UniProtKB.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IMP:ZFIN.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Cell junction;
KW Cell projection; Coated pit; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..297
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000402067"
FT DOMAIN 1..184
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 226..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118..131
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23105108, ECO:0000269|PubMed:23128673"
FT BINDING 154..163
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23105108, ECO:0000269|PubMed:23128673"
FT SITE 53
FT /note="Crucial for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23128673"
FT VAR_SEQ 189..297
FT /note="AVQLRKVPPRKPEGEIKPYSLMEREVVREEQRVLPWPFVRPGGPPHSPPLLP
FT SSPQSRSLSVGSSPSRAPLRPAAATVLQQGQTPSSPLNDSCRAKRTSSLNRSRLSFH
FT -> GTPPSPLTDQGMYGFFGPTEKSSPKKARGRDQTLFANGKRSGSGGAEGSPLAICSP
FT RGSPPLSPSTSVISSIPFSQCGILPQPGPASPRRGHGPPAGSDPLIPAQRQLQGKTHQF
FT SK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040229"
FT MUTAGEN 45
FT /note="L->A: Reduces activity to 30%."
FT /evidence="ECO:0000269|PubMed:23105108"
FT MUTAGEN 53
FT /note="Q->A: Reduces activity to 1.5%."
FT /evidence="ECO:0000269|PubMed:23128673"
FT MUTAGEN 117
FT /note="D->A: Reduces activity to 3%. Causes the formation
FT of a constitutive dimer in solution."
FT /evidence="ECO:0000269|PubMed:23105108"
FT MUTAGEN 126
FT /note="R->E: Reduces activity to 19%."
FT /evidence="ECO:0000269|PubMed:23105108"
FT MUTAGEN 131
FT /note="S->L: No effect."
FT /evidence="ECO:0000269|PubMed:23105108"
FT MUTAGEN 151
FT /note="D->A: Reduces activity to 1%."
FT /evidence="ECO:0000269|PubMed:23105108"
FT MUTAGEN 154
FT /note="S->A: Reduces activity to 8%."
FT /evidence="ECO:0000269|PubMed:23105108"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:4H6U"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4HKF"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:4HKF"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:4H6U"
FT HELIX 35..52
FT /evidence="ECO:0007829|PDB:4HKF"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:4HKF"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4HKF"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:4HKF"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:4HKF"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4HKF"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4HKF"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:4HKF"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4HKF"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:4HKF"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4HKF"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4HKF"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:4HKF"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:4HKF"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4HKF"
SQ 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
