ATAT_PIG
ID ATAT_PIG Reviewed; 300 AA.
AC Q767K7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Large white;
RX PubMed=14673549; DOI=10.1007/s00251-003-0627-0;
RA Shigenari A., Ando A., Renard C., Chardon P., Shiina T., Kulski J.K.,
RA Yasue H., Inoko H.;
RT "Nucleotide sequencing analysis of the swine 433-kb genomic segment located
RT between the non-classical and classical SLA class I gene clusters.";
RL Immunogenetics 55:695-705(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; AB113356; BAD08430.1; -; Genomic_DNA.
DR EMBL; AB113357; BAD08442.1; -; Genomic_DNA.
DR RefSeq; NP_001116595.1; NM_001123123.1.
DR AlphaFoldDB; Q767K7; -.
DR SMR; Q767K7; -.
DR STRING; 9823.ENSSSCP00000030388; -.
DR PeptideAtlas; Q767K7; -.
DR GeneID; 100144480; -.
DR KEGG; ssc:100144480; -.
DR CTD; 79969; -.
DR eggNOG; KOG4601; Eukaryota.
DR InParanoid; Q767K7; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q767K7; SS.
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..300
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000402066"
FT DOMAIN 1..190
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 229..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
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 210
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 221
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q8K341, ECO:0000255|HAMAP-
FT Rule:MF_03130"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG11"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
FT MOD_RES 282
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K341"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
FT MOD_RES 300
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
SQ SEQUENCE 300 AA; 34073 MW; BDF89213F59A69C2 CRC64;
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIIDEL GKASAKAQHL
PAPITSASRM QSNRHVMYIL KDTSARPAGK GAIVGFLKVG YKKLFVLDDR EAHNEVEPLC
ILDFYIHESL QRHGHGRELF QHMLQKERVE PHQLAIDRPS QKLLKFLNKH YNLETTVPQV
NNFVIFEGFF AHQHPPARKL PPKRAEGDIK PYSSSDREFL KVAVEPPWPL NRAPRRATPP
AHPPPRSSSL GNSPERGPLR PFVPEQELLR SLRLCPPHPT ARLLLATDPG GSPAQRRRTR
