ATAT_BOVIN
ID ATAT_BOVIN Reviewed; 225 AA.
AC Q58CX6; A5PK64;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q58CX6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58CX6-2; Sequence=VSP_040228;
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; BT021821; AAX46668.1; -; mRNA.
DR EMBL; BC142375; AAI42376.1; -; mRNA.
DR AlphaFoldDB; Q58CX6; -.
DR SMR; Q58CX6; -.
DR STRING; 9913.ENSBTAP00000009111; -.
DR Ensembl; ENSBTAT00000009133; ENSBTAP00000009133; ENSBTAG00000006941. [Q58CX6-1]
DR VEuPathDB; HostDB:ENSBTAG00000006941; -.
DR eggNOG; KOG4601; Eukaryota.
DR GeneTree; ENSGT00390000008276; -.
DR HOGENOM; CLU_025013_2_1_1; -.
DR InParanoid; Q58CX6; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000006941; Expressed in uterine horn and 106 other tissues.
DR ExpressionAtlas; Q58CX6; baseline and differential.
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 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Alternative splicing; Cell junction;
KW Cell projection; Coated pit; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..225
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000402064"
FT DOMAIN 1..190
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 195..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Basic and acidic 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 210
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT VAR_SEQ 181..225
FT /note="NNFVIFEGFFAHQHPPARKLPPKRAEGDIKPYSSSDRESGLPQGW -> RSF
FT RE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040228"
SQ SEQUENCE 225 AA; 25675 MW; 48206BE229574170 CRC64;
MEFPFDVDAL LPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIVDEL GKASAKAQHL
PAPITSASRM QSNRHVMYIL KDTSARPAGK GAIVGFLKVG YKKLFVLDDR EAHNEVEPLC
ILDFYIHESL QRHGHGRELF QHMLQKERVE PHQLAIDRPS QKLLKFLNKH YNLETTVPQV
NNFVIFEGFF AHQHPPARKL PPKRAEGDIK PYSSSDRESG LPQGW
