ATAT_RAT
ID ATAT_RAT Reviewed; 421 AA.
AC Q6MG11;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:CAE84036.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:CAE84036.1};
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; SER-276 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BX883048; CAE84036.1; -; Genomic_DNA.
DR RefSeq; NP_997663.1; NM_212498.1.
DR AlphaFoldDB; Q6MG11; -.
DR SMR; Q6MG11; -.
DR STRING; 10116.ENSRNOP00000001065; -.
DR iPTMnet; Q6MG11; -.
DR PhosphoSitePlus; Q6MG11; -.
DR jPOST; Q6MG11; -.
DR PaxDb; Q6MG11; -.
DR PRIDE; Q6MG11; -.
DR ABCD; Q6MG11; 1 sequenced antibody.
DR GeneID; 361789; -.
DR KEGG; rno:361789; -.
DR UCSC; RGD:1303066; rat.
DR CTD; 79969; -.
DR RGD; 1303066; Atat1.
DR VEuPathDB; HostDB:ENSRNOG00000000809; -.
DR eggNOG; KOG4601; Eukaryota.
DR InParanoid; Q6MG11; -.
DR OMA; SRQRCGQ; -.
DR OrthoDB; 1312675at2759; -.
DR PhylomeDB; Q6MG11; -.
DR TreeFam; TF315643; -.
DR Reactome; R-RNO-5617833; Cilium Assembly.
DR PRO; PR:Q6MG11; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000809; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; Q6MG11; baseline and differential.
DR Genevisible; Q6MG11; RN.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0097427; C:microtubule bundle; ISO:RGD.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
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:0021542; P:dentate gyrus development; ISO:RGD.
DR GO; GO:0048666; P:neuron development; IEA:UniProtKB-UniRule.
DR GO; GO:0044546; P:NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISO:RGD.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cell junction; Cell projection; Coated pit;
KW Cytoplasm; Cytoskeleton; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000348068"
FT DOMAIN 1..190
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 214..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
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 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:0007744|PubMed:22673903"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 305
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K341"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 323
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
SQ SEQUENCE 421 AA; 47327 MW; 8AE25A0BD01279AA CRC64;
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIVDEL GKASAKAQHL
PAPITSALRM QSNRHVIYVL KDTSARPAGK GAIIGFLKVG YKKLFVLDDR EAHNEVEPLC
ILDFYIHESV QRHGHGRELF QYMLQKERVE PHQLAIDRPS PKLLKFLNKH YNLETTVPQV
NNFVIFEGFF AHQHRSPTPS LRATRHSRAA VVDPIPAAPA RKLPPKRAEG DIKPYSSSDR
EFLKVAVEPP WPLNRAPRRA TPPAHPPPRS SSLGNSPDRG PLRPFVPEQE LLRSLRLCPP
HPTARLLLAT DPGGSPAQRR RTRETPWGLV AQSCHYSRHG GFNTSFLGTG NQERKQGEQE
AEDRSASEDQ VLLQDGSGEE PTHTVAPRAQ APPAQSWMVG GDILNARVIR NLQERRNTRP
W
