ATAT_XENTR
ID ATAT_XENTR Reviewed; 297 AA.
AC B2RZF9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, 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}; Synonyms=mec17;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PopA;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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. May be involved in neuron development. {ECO:0000255|HAMAP-
CC 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 -!- 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 -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; BC167141; AAI67141.1; -; mRNA.
DR RefSeq; NP_001120781.1; NM_001127309.1.
DR AlphaFoldDB; B2RZF9; -.
DR SMR; B2RZF9; -.
DR STRING; 8364.ENSXETP00000051980; -.
DR PaxDb; B2RZF9; -.
DR Ensembl; ENSXETT00000063599; ENSXETP00000059679; ENSXETG00000024089.
DR GeneID; 100038151; -.
DR KEGG; xtr:100038151; -.
DR CTD; 79969; -.
DR Xenbase; XB-GENE-478280; atat1.
DR eggNOG; KOG4601; Eukaryota.
DR InParanoid; B2RZF9; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000024089; Expressed in brain and 14 other tissues.
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; 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; Cell junction; Cell projection; Coated pit; Cytoplasm;
KW Cytoskeleton; Membrane; Reference proteome; Transferase.
FT CHAIN 1..297
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000402069"
FT DOMAIN 1..186
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 269..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120..133
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT BINDING 156..165
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT SITE 54
FT /note="Crucial for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
SQ SEQUENCE 297 AA; 34027 MW; E40D1CB60027348F CRC64;
MEFDFDVHKI FLEPITKLDS SLIPSRRPLI ASSEAQKQIM TVIDEIGKAS AKAQRLPAPI
TSASRMQTNK HHLYILKDCT PKTAGRGAVI GFLKVGCKKL FVLDQKGSHI EAEPLCILDF
YIHETLQRHG FGKELFTFML KNEQVDVHHL AIDRPSEKFL SFLRKHFNLW STIPQVNNFV
VFDGFFRDWK ASVKKTPAKR TEGEIKPYSL TDRDFLKQEE GLPWPFSQSQ LNLNRASSLG
SSPTRACSRH SPGEEDFVKS LRNCRPHSLH RTANSEQEDH SQRRRTSSLN RPQSIHH
