ATAT2_CAEEL
ID ATAT2_CAEEL Reviewed; 263 AA.
AC Q23192;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Alpha-tubulin N-acetyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT 2 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=TAT 2 {ECO:0000255|HAMAP-Rule:MF_03130};
DE EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130};
DE AltName: Full=Mec-17-like protein;
GN Name=atat-2; ORFNames=W06B11.1;
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=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 [3]
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: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 -!- TISSUE SPECIFICITY: Expressed in touch receptor neurons and in a subset
CC of ciliated neurons, including PDE, ADE, CEP, and OLQ neurons.
CC {ECO:0000269|PubMed:21068373}.
CC -!- DISRUPTION PHENOTYPE: Mutants move more slowly off food than wild-type
CC animals, but retain the ability to slow when encountering a bacterial
CC lawn. Mutants exhibit significantly reduced nose touch sensation and
CC are partially insensitive to body touch. {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; FO081143; CCD69460.1; -; Genomic_DNA.
DR PIR; T26219; T26219.
DR RefSeq; NP_508981.1; NM_076580.4.
DR AlphaFoldDB; Q23192; -.
DR SMR; Q23192; -.
DR BioGRID; 45785; 2.
DR DIP; DIP-26342N; -.
DR STRING; 6239.W06B11.1; -.
DR EPD; Q23192; -.
DR PaxDb; Q23192; -.
DR PeptideAtlas; Q23192; -.
DR PRIDE; Q23192; -.
DR EnsemblMetazoa; W06B11.1.1; W06B11.1.1; WBGene00021059.
DR GeneID; 180852; -.
DR UCSC; W06B11.1; c. elegans.
DR CTD; 180852; -.
DR WormBase; W06B11.1; CE28508; WBGene00021059; atat-2.
DR eggNOG; KOG4601; Eukaryota.
DR GeneTree; ENSGT00390000008276; -.
DR HOGENOM; CLU_025013_2_1_1; -.
DR InParanoid; Q23192; -.
DR OMA; FFIGRHP; -.
DR OrthoDB; 1312675at2759; -.
DR PhylomeDB; Q23192; -.
DR BRENDA; 2.3.1.108; 1045.
DR PRO; PR:Q23192; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00021059; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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: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..263
FT /note="Alpha-tubulin N-acetyltransferase 2"
FT /id="PRO_0000402076"
FT DOMAIN 1..181
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 191..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115..128
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
SQ SEQUENCE 263 AA; 30391 MW; 54D52935246015D5 CRC64;
MEIAFDLSTI FTDNIQRLTR TDLLKYGPKR YWAVAQSIDC LGEMSSKFHG WKRVITMYDK
IVDHDEEQTT YIMWEKVNGS KSILKGLLRV GYKTLYLTDN EQNQYMEKAM CILDFFVVPT
EQRSGNGFKM FDEMLKAENV TVDQCAFDKP SAALQQFLEK YYDRKDLVWQ SNKYALCSNF
FIGRHPTVPF TPRQTKRASR ASSAVSSHAS SRNTSPIGRN RPRHDSVADL MRQDMLAGVR
AEVDPNSPTG LKNARDFGHR RIW
