ATAT_XENLA
ID ATAT_XENLA Reviewed; 418 AA.
AC Q5FWM1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC089285; AAH89285.1; -; mRNA.
DR RefSeq; NP_001089986.1; NM_001096517.1.
DR AlphaFoldDB; Q5FWM1; -.
DR SMR; Q5FWM1; -.
DR DNASU; 735057; -.
DR GeneID; 735057; -.
DR KEGG; xla:735057; -.
DR CTD; 735057; -.
DR Xenbase; XB-GENE-865161; atat1.S.
DR OrthoDB; 1312675at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 735057; Expressed in egg cell and 19 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..418
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000402068"
FT DOMAIN 1..186
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 237..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
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 418 AA; 47438 MW; 37FCA53CC6F1E5E1 CRC64;
MEFEFDVHKI FLEPITKLDN NLIPPRRPLI SSSEAQKQIM TVIDEIGKAS AKAQRLPASI
TSASRMQANK HHLYILKDCT PKTAGRGAVI GFLKVGYKKL FILDQKGSHI EAEPLCILDF
YIHESLQRHG FGKELFSFML RNEQVDVQHL AIDRPSEKFL SFLRKHFNLW STIPQVNNFV
VFEGFFRDRK ASVKKTPAKR TEGEIKPYSL TDRDFLKQEE GLPWPLSQAQ INLNRASSLG
SSPTRACSRP PPGEEDFVKS LRNCRPHSLQ RAASSEQEDH SQRRRTSEMN LSRGLLAQKN
GYSRYLSPPP PLLTQGPYAA AQIKEQQSRT DSSAQEGRTQ DRPNGSNSQH QNDLISSKQH
VQDLHMELAA GRTMSDLKEG QNATKSPWCD HPSYTVLGTV LNAAWVKKKQ ELRSTRPW
