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Q6PH17 (ATAT_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-tubulin N-acetyltransferase 1

Short name=Alpha-TAT
Short name=Alpha-TAT1
Short name=TAT
EC=2.3.1.108
Alternative name(s):
Acetyltransferase mec-17 homolog
Gene names
Name:atat1
Synonyms:mec17
ORF Names:si:ch211-152p11.5, zgc:65893
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May promote directional cell locomotion and chemotaxis By similarity. May be required for normal sperm flagellar function By similarity. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development. Acetylates alpha-tubulin in neurons, but not in cilia. Ref.3

Catalytic activity

Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N(6)-acetyl-L-lysine. HAMAP-Rule MF_03130

Subunit structure

Monomer. Ref.5

Subcellular location

Cytoplasm By similarity. Membraneclathrin-coated pit By similarity. Cell junctionfocal adhesion By similarity. Cell projectionaxon By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonspindle By similarity HAMAP-Rule MF_03130.

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. Ref.3

Sequence similarities

Belongs to the acetyltransferase ATAT1 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PH17-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6PH17-2)

The sequence of this isoform differs from the canonical sequence as follows:
     189-297: AVQLRKVPPR...SLNRSRLSFH → GTPPSPLTDQ...LQGKTHQFSK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Alpha-tubulin N-acetyltransferase 1 HAMAP-Rule MF_03130
PRO_0000402067

Regions

Region118 – 13114Acetyl-CoA binding HAMAP-Rule MF_03130
Region154 – 16310Acetyl-CoA binding HAMAP-Rule MF_03130

Sites

Site531Crucial for catalytic activity

Natural variations

Alternative sequence189 – 297109AVQLR…RLSFH → GTPPSPLTDQGMYGFFGPTE KSSPKKARGRDQTLFANGKR SGSGGAEGSPLAICSPRGSP PLSPSTSVISSIPFSQCGIL PQPGPASPRRGHGPPAGSDP LIPAQRQLQGKTHQFSK in isoform 2.
VSP_040229

Experimental info

Mutagenesis451L → A: Reduces activity to 30%. Ref.5
Mutagenesis531Q → A: Reduces activity to 1.5%. Ref.4
Mutagenesis1171D → A: Reduces activity to 3%. Causes the formation of a constitutive dimer in solution. Ref.5
Mutagenesis1261R → E: Reduces activity to 19%. Ref.5
Mutagenesis1311S → L: No effect. Ref.5
Mutagenesis1511D → A: Reduces activity to 1%. Ref.5
Mutagenesis1541S → A: Reduces activity to 8%. Ref.5

Secondary structure

.................................... 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3F08861B19D635EB

FASTA29733,202
        10         20         30         40         50         60 
MDFPYDLNAL FPERISVLDS NLSAGRKAHG RPDPLPQVTT VIDELGKASS KAQQLPAPIT 

        70         80         90        100        110        120 
SAAKLQANRH HLYLLKDGEQ NGGRGVIVGF LKVGYKKLFL LDQRGAHLET EPLCVLDFYV 

       130        140        150        160        170        180 
TETLQRHGYG SELFDFMLKH KQVEPAQMAY DRPSPKFLSF LEKRYDLRNS VPQVNNFVVF 

       190        200        210        220        230        240 
AGFFQSRSAV QLRKVPPRKP EGEIKPYSLM EREVVREEQR VLPWPFVRPG GPPHSPPLLP 

       250        260        270        280        290 
SSPQSRSLSV GSSPSRAPLR PAAATVLQQG QTPSSPLNDS CRAKRTSSLN RSRLSFH 

« Hide

Isoform 2 [UniParc].

Checksum: E6E63F28DE12E566
Show »

FASTA30533,198

References

« Hide 'large scale' references
[1]"The zebrafish reference genome sequence and its relationship to the human genome."
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. expand/collapse author list , 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.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Embryo.
[3]"MEC-17 is an alpha-tubulin acetyltransferase."
Akella J.S., Wloga D., Kim J., Starostina N.G., Lyons-Abbott S., Morrissette N.S., Dougan S.T., Kipreos E.T., Gaertig J.
Nature 467:218-222(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]"Molecular basis of the acetyltransferase activity of MEC-17 towards alpha-tubulin."
Li W., Zhong C., Li L., Sun B., Wang W., Xu S., Zhang T., Wang C., Bao L., Ding J.
Cell Res. 22:1707-1711(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-188 IN COMPLEX WITH ACETYL-COA, MUTAGENESIS OF GLN-53.
[5]"Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus."
Kormendi V., Szyk A., Piszczek G., Roll-Mecak A.
J. Biol. Chem. 287:41569-41575(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-188 OF WILD-TYPE AND OF MUTANT ALA-117 IN COMPLEX WITH ACETYL-COA, SUBUNIT, MUTAGENESIS OF LEU-45; ASP-117; ARG-126; SER-131; ASP-151 AND SER-154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX511233 Genomic DNA. Translation: CAM56330.1.
BC056749 mRNA. Translation: AAH56749.1.
BC065981 mRNA. Translation: AAH65981.1.
RefSeqNP_998423.1. NM_213258.1. [Q6PH17-2]
XP_005170079.1. XM_005170022.1. [Q6PH17-1]
UniGeneDr.6427.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4H6UX-ray2.45A/B1-188[»]
4H6ZX-ray2.70A/B1-186[»]
4HKFX-ray1.70A1-188[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000049367.

Protocols and materials databases

DNASU406389.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000049368; ENSDARP00000049367; ENSDARG00000004472. [Q6PH17-2]
ENSDART00000103922; ENSDARP00000094698; ENSDARG00000004472. [Q6PH17-1]
GeneID406389.
KEGGdre:406389.

Organism-specific databases

CTD79969.
ZFINZDB-GENE-040426-2120. atat1.

Phylogenomic databases

eggNOGNOG249793.
GeneTreeENSGT00390000008276.
HOGENOMHOG000257795.
HOVERGENHBG055797.
InParanoidQ6NZT0.
OMAKEENIHP.
OrthoDBEOG76739W.
PhylomeDBQ6PH17.
TreeFamTF315643.

Gene expression databases

BgeeQ6PH17.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
HAMAPMF_03130. mec17.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR007965. Alpha-TAT.
[Graphical view]
PANTHERPTHR12327. PTHR12327. 1 hit.
PfamPF05301. Mec-17. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

NextBio20817998.

Entry information

Entry nameATAT_DANRE
AccessionPrimary (citable) accession number: Q6PH17
Secondary accession number(s): Q6NZT0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references