ATAT1_CAEEL
ID ATAT1_CAEEL Reviewed; 262 AA.
AC O45100;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=F57H12.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=2646709; DOI=10.1126/science.2646709;
RA Chalfie M., Au M.;
RT "Genetic control of differentiation of the Caenorhabditis elegans touch
RT receptor neurons.";
RL Science 243:1027-1033(1989).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12124626; DOI=10.1038/nature00891;
RA Zhang Y., Ma C., Delohery T., Nasipak B., Foat B.C., Bounoutas A.,
RA Bussemaker H.J., Kim S.K., Chalfie M.;
RT "Identification of genes expressed in C. elegans touch receptor neurons.";
RL Nature 418:331-335(2002).
RN [4]
RP FUNCTION.
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 [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21068373; DOI=10.1073/pnas.1013728107;
RA Shida T., Cueva J.G., Xu Z., Goodman M.B., Nachury M.V.;
RT "The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid
RT ciliogenesis and efficient mechanosensation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21517-21522(2010).
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, ECO:0000269|PubMed:12124626,
CC ECO:0000269|PubMed:20829795, ECO:0000269|PubMed:2646709}.
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 -!- TISSUE SPECIFICITY: Expressed solely in touch receptor neurons.
CC {ECO:0000269|PubMed:12124626, ECO:0000269|PubMed:21068373}.
CC -!- DEVELOPMENTAL STAGE: Expressed in touch receptors from late embryos to
CC adults. {ECO:0000269|PubMed:12124626}.
CC -!- DISRUPTION PHENOTYPE: Mutants are partially insensitive to body touch.
CC {ECO:0000269|PubMed:21068373}.
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; FO081188; CCD69773.1; -; Genomic_DNA.
DR PIR; T32979; T32979.
DR RefSeq; NP_501337.1; NM_068936.4.
DR AlphaFoldDB; O45100; -.
DR SMR; O45100; -.
DR BioGRID; 42710; 1.
DR STRING; 6239.F57H12.7; -.
DR EPD; O45100; -.
DR PaxDb; O45100; -.
DR PeptideAtlas; O45100; -.
DR EnsemblMetazoa; F57H12.7a.1; F57H12.7a.1; WBGene00003178.
DR GeneID; 177596; -.
DR KEGG; cel:CELE_F57H12.7; -.
DR UCSC; F57H12.7; c. elegans.
DR CTD; 177596; -.
DR WormBase; F57H12.7a; CE17128; WBGene00003178; mec-17.
DR eggNOG; KOG4601; Eukaryota.
DR HOGENOM; CLU_025013_1_0_1; -.
DR InParanoid; O45100; -.
DR OMA; DYMFSQE; -.
DR OrthoDB; 1005890at2759; -.
DR PhylomeDB; O45100; -.
DR Reactome; R-CEL-5617833; Cilium Assembly.
DR PRO; PR:O45100; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003178; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; O45100; baseline and differential.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:WormBase.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; IMP:UniProtKB.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IBA:GO_Central.
DR GO; GO:0042490; P:mechanoreceptor differentiation; IMP:WormBase.
DR GO; GO:0048666; P:neuron development; IEA:UniProtKB-UniRule.
DR GO; GO:0006473; P:protein acetylation; IGI:WormBase.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule.
DR GO; GO:0001966; P:thigmotaxis; IMP:WormBase.
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 2: Evidence at transcript level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..262
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000402075"
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 262 AA; 29825 MW; 7A1EBE3387EB549F CRC64;
MQVDADLRPI LGPQLVRLDP MRVKQLQDPI VYEAIDNLAK LSAHCLQLRT PLTTCEKLIN
SDSTLYLSWK YDEEEKVSRL MGFAKVGRKK LFLYDSQMQT YEGEILCLLD FYVHFSCQRQ
GVGQQILDYM FSQEHTEPYQ LALDNPSVTL LGFMSQKYGL IKPVWQNTNF VVFEELFLAL
SAENGIEKPP PDGWRRPMTP RRLGTGMTDT RWLQHAVSGH QSKGNAMAAP VDADMTPQGA
LSNRAHQAKA RKAHILSSKP LW
