ATAT2_CAEBR
ID ATAT2_CAEBR Reviewed; 263 AA.
AC A8XKM2;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=CBG14763;
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}.
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DR EMBL; HE600983; CAP33196.1; -; Genomic_DNA.
DR RefSeq; XP_002644757.1; XM_002644711.1.
DR AlphaFoldDB; A8XKM2; -.
DR SMR; A8XKM2; -.
DR STRING; 6238.CBG14763; -.
DR EnsemblMetazoa; CBG14763.1; CBG14763.1; WBGene00035165.
DR GeneID; 8586753; -.
DR KEGG; cbr:CBG_14763; -.
DR CTD; 8586753; -.
DR WormBase; CBG14763; CBP09734; WBGene00035165; Cbr-atat-2.
DR eggNOG; KOG4601; Eukaryota.
DR HOGENOM; CLU_025013_2_1_1; -.
DR InParanoid; A8XKM2; -.
DR OMA; FFIGRHP; -.
DR OrthoDB; 1312675at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; ISS: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:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule.
DR GO; GO:0001966; P:thigmotaxis; IEA:EnsemblMetazoa.
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..263
FT /note="Alpha-tubulin N-acetyltransferase 2"
FT /id="PRO_0000402074"
FT DOMAIN 1..181
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 191..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..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; 30477 MW; F7A0E3C642045746 CRC64;
MEIAFDLSSI FTDNIQRLEK ADLLKYSPKQ YWAVAKSIDT LGEMSSKFHG WKRIITMYEK
IIDHDEDQTV YILWDKVDGN KSVLKGILRV GYKTLYLTDN EQNQYMEKAM CILDFFIVPT
EQRSGNGFNM FDAMLKAENV LVEQCAFDKP SAALRQFLEK YYDQKEPVMQ SNKYAVFPNF
FIGRHPTVPF TPRQTKRASR ASSAVSSHTT SRNTSPIGRN RPRHDSVADL MRQDNFPRGR
SVIDPNSPAG FKLTRDQRHE PIW
