ID   ATAT1_CAEBR             Reviewed;         277 AA.
AC   A8XRF5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Alpha-tubulin N-acetyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE            Short=Alpha-TAT 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE            Short=TAT 1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE            EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130};
DE   AltName: Full=Mechanosensory abnormality protein 17;
GN   Name=mec-17 {ECO:0000255|HAMAP-Rule:MF_03130}; ORFNames=CBG17726;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin/mec-12 on
CC       the lumenal side of microtubules. Promotes microtubule destabilization
CC       and accelerates microtubule dynamics; this activity may be independent
CC       of 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. Required for the maintenance of touch receptor neurons and
CC       possibly other type of neurons involved in locomotion.
CC       {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   -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03130}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE600976; CAP35229.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XRF5; -.
DR   SMR; A8XRF5; -.
DR   STRING; 6238.CBG17726; -.
DR   WormBase; CBG17726; CBP04141; WBGene00037281; Cbr-mec-17.
DR   eggNOG; KOG4601; Eukaryota.
DR   HOGENOM; CLU_025013_1_0_1; -.
DR   InParanoid; A8XRF5; -.
DR   OMA; DYMFSQE; -.
DR   OrthoDB; 1005890at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0005874; C:microtubule; IEA:InterPro.
DR   GO; GO:0019799; F:tubulin N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0071929; P:alpha-tubulin acetylation; IBA:GO_Central.
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; IPR038746; Atat.
DR   InterPro; IPR007965; GNAT_ATAT.
DR   PANTHER; PTHR12327; PTHR12327; 1.
DR   Pfam; PF05301; Acetyltransf_16; 1.
DR   PROSITE; PS51730; GNAT_ATAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..277
FT                   /note="Alpha-tubulin N-acetyltransferase 1"
FT                   /id="PRO_0000402073"
FT   DOMAIN          1..177
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT   BINDING         111..124
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
SQ   SEQUENCE   277 AA;  31519 MW;  6C4520ABA492965F CRC64;
     MQVNADLRPI LGPQLVRLDP MRIKQLQDPQ VYDAIDSLAK LSAHCLQLRT PLTTCEKLIN
     SDSTLYLSWK YDEEEKVSRL LGFAKVGRKK LFLYDAQMQT YEGEVLCLLD FYVHFSTQRQ
     GVGKQILDYM FSQEHAEPYQ LALDNPSVTL LGFMSQKYGM NRPVWQNTNF VVFDELFQSL
     SAENGVGTVD FQSCKYRIFN SEKSPPDGWR RPMTPRRLGT GMTDTRWLQH AVSGHQSKGN
     AMAAPVDADM TPQGALSNRA HQAKARKAHI LSSKPLW