ATAT_MACMU
ID ATAT_MACMU Reviewed; 323 AA.
AC Q5TM63;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
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 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=Alpha-TAT1 {ECO:0000255|HAMAP-Rule:MF_03130};
DE Short=TAT {ECO:0000255|HAMAP-Rule:MF_03130};
DE EC=2.3.1.108 {ECO:0000255|HAMAP-Rule:MF_03130};
DE AltName: Full=Acetyltransferase mec-17 homolog {ECO:0000255|HAMAP-Rule:MF_03130};
GN Name=ATAT1 {ECO:0000255|HAMAP-Rule:MF_03130};
GN Synonyms=MEC17 {ECO:0000255|HAMAP-Rule:MF_03130};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15269276; DOI=10.1093/molbev/msh216;
RA Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT "Rhesus macaque class I duplicon structures, organization, and evolution
RT within the alpha block of the major histocompatibility complex.";
RL Mol. Biol. Evol. 21:2079-2091(2004).
CC -!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the
CC lumenal side of microtubules. Promotes microtubule destabilization and
CC accelerates microtubule dynamics; this activity may be independent of
CC 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 normal sperm flagellar function. Promotes
CC directional cell locomotion and chemotaxis, through AP2A2-dependent
CC acetylation of alpha-tubulin at clathrin-coated pits that are
CC concentrated at the leading edge of migrating cells. May facilitate
CC primary cilium assembly. {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 -!- SUBUNIT: Component of the BBSome complex. Interacts with AP2 alpha-
CC adaptins, including AP2A2, but not with AP1 gamma-adaptin
CC (AP1G1/AP1G2); this interaction is required for efficient alpha-tubulin
CC acetylation, hence clathrin-coated pits are sites of microtubule
CC acetylation. {ECO:0000255|HAMAP-Rule:MF_03130}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130}.
CC Membrane, clathrin-coated pit {ECO:0000255|HAMAP-Rule:MF_03130}. Cell
CC junction, focal adhesion {ECO:0000255|HAMAP-Rule:MF_03130}. Cell
CC projection, axon {ECO:0000255|HAMAP-Rule:MF_03130}. Cytoplasm,
CC cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03130}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03130}.
CC -!- PTM: Autoacetylation strongly increases tubulin acetylation.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; AB128049; BAD69763.1; -; Genomic_DNA.
DR RefSeq; NP_001108432.1; NM_001114960.1.
DR AlphaFoldDB; Q5TM63; -.
DR SMR; Q5TM63; -.
DR GeneID; 100141388; -.
DR KEGG; mcc:100141388; -.
DR CTD; 79969; -.
DR InParanoid; Q5TM63; -.
DR OrthoDB; 1312675at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB.
DR GO; GO:0019799; F:tubulin N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0071929; P:alpha-tubulin acetylation; ISS:UniProtKB.
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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR038746; Atat.
DR InterPro; IPR007965; GNAT_ATAT.
DR PANTHER; PTHR12327; PTHR12327; 1.
DR Pfam; PF05301; Acetyltransf_16; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51730; GNAT_ATAT; 1.
PE 3: Inferred from homology;
KW Acetylation; Acyltransferase; Cell junction; Cell projection; Coated pit;
KW Cytoplasm; Cytoskeleton; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..323
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000402065"
FT DOMAIN 1..190
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 196..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..137
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT BINDING 160..169
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT SITE 58
FT /note="Crucial for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT MOD_RES 56
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 146
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 233
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 244
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG11"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
FT MOD_RES 305
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K341"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
FT MOD_RES 323
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
SQ SEQUENCE 323 AA; 36358 MW; 4056F17B4D109A76 CRC64;
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL GKASAKAQNL
SAPITSASRM QSNRHVVYIL KDSSGRPAGK GAIIGFIKVG YKKLFVLDDR EAHNEVEPLC
ILDFYIHESV QRHGHGRELF QYMLQKERVE PHQLAIDRPS QKLLKFLNKH YNLETTVPQV
NNFVIFEGFF AHQHRPPAPS LRATRHSRAA AVDPTPTAPA RKLPPKRAEG DIKPYSSSDR
EFLKVAVEPP WPLNRAPRRA TPPAHPPPRS SSLGNSPERG PLRPFVPEQE LLRSLRLCPP
HPTARLLLAA DPGGSPAQRR RTR
