ATAT_MOUSE
ID ATAT_MOUSE Reviewed; 421 AA.
AC Q8K341; B8JJ75; B8JJ77; Q3UZR9; Q8BM67; Q8C1D1; Q8K2M7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC25866.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC25866.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC28808.1},
RC Embryonic head {ECO:0000312|EMBL:BAC25866.1}, and
RC Pituitary {ECO:0000312|EMBL:BAE21786.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH28847.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH30669.1}, and
RC Czech II {ECO:0000312|EMBL:AAH28847.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH30669.1}, and
RC Mammary tumor {ECO:0000312|EMBL:AAH28847.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
RX PubMed=20829795; DOI=10.1038/nature09324;
RA Akella J.S., Wloga D., Kim J., Starostina N.G., Lyons-Abbott S.,
RA Morrissette N.S., Dougan S.T., Kipreos E.T., Gaertig J.;
RT "MEC-17 is an alpha-tubulin acetyltransferase.";
RL Nature 467:218-222(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23720746; DOI=10.1074/jbc.m113.464792;
RA Kim G.W., Li L., Gorbani M., You L., Yang X.J.;
RT "Mice lacking alpha-tubulin acetyltransferase 1 are viable but display
RT alpha-tubulin acetylation deficiency and dentate gyrus distortion.";
RL J. Biol. Chem. 288:20334-20350(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ACETYLATION AT LYS-56;
RP LYS-146; LYS-233 AND LYS-244, AND MUTAGENESIS OF LYS-56; GLY-134; GLY-136;
RP LEU-139; LYS-146; LYS-233 AND LYS-244.
RX PubMed=23275437; DOI=10.1128/mcb.01044-12;
RA Kalebic N., Martinez C., Perlas E., Hublitz P., Bilbao-Cortes D.,
RA Fiedorczuk K., Andolfo A., Heppenstall P.A.;
RT "Tubulin acetyltransferase alphaTAT1 destabilizes microtubules
RT independently of its acetylation activity.";
RL Mol. Cell. Biol. 33:1114-1123(2013).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23748901; DOI=10.1038/ncomms2962;
RA Kalebic N., Sorrentino S., Perlas E., Bolasco G., Martinez C.,
RA Heppenstall P.A.;
RT "alphaTAT1 is the major alpha-tubulin acetyltransferase in mice.";
RL Nat. Commun. 4:1962-1962(2013).
RN [10]
RP FUNCTION, AND INTERACTION WITH AP2A2.
RX PubMed=24097348; DOI=10.1038/nature12571;
RA Montagnac G., Meas-Yedid V., Irondelle M., Castro-Castro A., Franco M.,
RA Shida T., Nachury M.V., Benmerah A., Olivo-Marin J.C., Chavrier P.;
RT "alphaTAT1 catalyses microtubule acetylation at clathrin-coated pits.";
RL Nature 502:567-570(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-305, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 ECO:0000269|PubMed:20829795, ECO:0000269|PubMed:23275437,
CC ECO:0000269|PubMed:23720746, ECO:0000269|PubMed:23748901,
CC ECO:0000269|PubMed:24097348}.
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 (By similarity). Interacts
CC with AP2 alpha-adaptins, including AP2A2, but not with AP1 gamma-
CC adaptin (AP1G1/AP1G2); this interaction is required for efficient
CC alpha-tubulin acetylation, hence clathrin-coated pits are sites of
CC microtubule acetylation. {ECO:0000255|HAMAP-Rule:MF_03130,
CC ECO:0000269|PubMed:24097348}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130,
CC ECO:0000269|PubMed:23275437}. Membrane, clathrin-coated pit
CC {ECO:0000255|HAMAP-Rule:MF_03130}. Cell junction, focal adhesion
CC {ECO:0000255|HAMAP-Rule:MF_03130}. Cell projection, axon
CC {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}.
CC Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03130,
CC ECO:0000269|PubMed:23275437}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}. Note=In
CC primary root dorsal ganglion neurons, localizes with acetylated tubulin
CC in axons. Recruited to the mitotic spindle during cell division.
CC {ECO:0000269|PubMed:23275437}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8K341-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8K341-2; Sequence=VSP_052905;
CC Name=3 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8K341-3; Sequence=VSP_052908, VSP_052909;
CC Name=4 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8K341-4; Sequence=VSP_052906, VSP_052907;
CC Name=5 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8K341-5; Sequence=VSP_052905, VSP_052906, VSP_052907;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in neuronal
CC tissues. In the brain, expressed in the cortex, cerebellum and
CC hippocampus, including the pyramidal layers in CA1 and CA3, as well as
CC the granular cell layers in the lateral blade (suprapyramidal portion)
CC and the medial blade (infrapyramidal portion) of the dentate gyrus. In
CC testis, mainly expressed in the internal cell layers of seminiferous
CC tubules, where spermatocytes and spermatids are located.
CC {ECO:0000269|PubMed:23275437, ECO:0000269|PubMed:23720746}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in embryos during development
CC with particularly high expression in the spinal cord at 13.5 dpc.
CC {ECO:0000269|PubMed:23720746}.
CC -!- PTM: Autoacetylation strongly increases tubulin acetylation.
CC {ECO:0000255|HAMAP-Rule:MF_03130, ECO:0000269|PubMed:23275437}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable and show no overt
CC phenotype. Drastic loss of tubulin acetylation in all tissues anlyzed,
CC including in early embryos. In dorsal hippocampus, but not in ventral
CC hippocampus, the dentate gyrus is slightly deformed, showing a
CC prominent bulge in the lateral blade of the granular cell layers. In
CC addition, the lateral ventricle appears to be dilated
CC (PubMed:23720746). Homozygous mutant males exhibit decreased fertility
CC (PubMed:23748901). Mature spermatozoa from cauda epididymis often show
CC the presence of a cytoplasmic droplet attached to the annulus of the
CC tail, indicative of impaired maturation. The flagella length is also
CC significantly decreased in spermatozoa, especially in those cells with
CC a cytoplasmic droplet. Spermatozoa display significantly lower motility
CC than control sperm. However, sperm flagella display the characteristic
CC 9 + 2 organization of axoneme microtubules (PubMed:23748901).
CC {ECO:0000269|PubMed:23720746, ECO:0000269|PubMed:23748901}.
CC -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03130}.
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DR EMBL; AK028297; BAC25866.1; -; mRNA.
DR EMBL; AK034725; BAC28808.1; -; mRNA.
DR EMBL; AK133694; BAE21786.1; -; mRNA.
DR EMBL; CR974451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028847; AAH28847.1; -; mRNA.
DR EMBL; BC030669; AAH30669.1; -; mRNA.
DR CCDS; CCDS28711.1; -. [Q8K341-5]
DR CCDS; CCDS50096.1; -. [Q8K341-1]
DR CCDS; CCDS50097.1; -. [Q8K341-4]
DR CCDS; CCDS84305.1; -. [Q8K341-2]
DR CCDS; CCDS89088.1; -. [Q8K341-3]
DR RefSeq; NP_001136216.1; NM_001142744.1. [Q8K341-1]
DR RefSeq; NP_001136217.1; NM_001142745.1. [Q8K341-4]
DR RefSeq; NP_001334307.1; NM_001347378.1. [Q8K341-2]
DR RefSeq; NP_082752.3; NM_028476.4. [Q8K341-5]
DR RefSeq; XP_017173163.1; XM_017317674.1.
DR AlphaFoldDB; Q8K341; -.
DR SMR; Q8K341; -.
DR BioGRID; 215858; 1.
DR DIP; DIP-60604N; -.
DR IntAct; Q8K341; 1.
DR STRING; 10090.ENSMUSP00000056383; -.
DR iPTMnet; Q8K341; -.
DR PhosphoSitePlus; Q8K341; -.
DR SwissPalm; Q8K341; -.
DR MaxQB; Q8K341; -.
DR PaxDb; Q8K341; -.
DR PeptideAtlas; Q8K341; -.
DR PRIDE; Q8K341; -.
DR ProteomicsDB; 277060; -. [Q8K341-1]
DR ProteomicsDB; 277061; -. [Q8K341-2]
DR ProteomicsDB; 277062; -. [Q8K341-3]
DR ProteomicsDB; 277063; -. [Q8K341-4]
DR ProteomicsDB; 277064; -. [Q8K341-5]
DR ABCD; Q8K341; 1 sequenced antibody.
DR Antibodypedia; 26411; 137 antibodies from 22 providers.
DR DNASU; 73242; -.
DR Ensembl; ENSMUST00000056034; ENSMUSP00000053853; ENSMUSG00000024426. [Q8K341-5]
DR Ensembl; ENSMUST00000061052; ENSMUSP00000056383; ENSMUSG00000024426. [Q8K341-1]
DR Ensembl; ENSMUST00000077494; ENSMUSP00000076703; ENSMUSG00000024426. [Q8K341-2]
DR Ensembl; ENSMUST00000141662; ENSMUSP00000115004; ENSMUSG00000024426. [Q8K341-4]
DR Ensembl; ENSMUST00000149277; ENSMUSP00000122715; ENSMUSG00000024426. [Q8K341-3]
DR GeneID; 73242; -.
DR KEGG; mmu:73242; -.
DR UCSC; uc008cja.3; mouse. [Q8K341-1]
DR UCSC; uc008cjb.3; mouse. [Q8K341-3]
DR UCSC; uc008cjc.3; mouse. [Q8K341-2]
DR UCSC; uc008cjd.3; mouse. [Q8K341-5]
DR UCSC; uc008cje.3; mouse. [Q8K341-4]
DR CTD; 79969; -.
DR MGI; MGI:1913869; Atat1.
DR VEuPathDB; HostDB:ENSMUSG00000024426; -.
DR eggNOG; KOG4601; Eukaryota.
DR GeneTree; ENSGT00390000008276; -.
DR HOGENOM; CLU_025013_0_0_1; -.
DR InParanoid; Q8K341; -.
DR OMA; SRQRCGQ; -.
DR OrthoDB; 1312675at2759; -.
DR PhylomeDB; Q8K341; -.
DR TreeFam; TF315643; -.
DR BRENDA; 2.3.1.108; 3474.
DR Reactome; R-MMU-5617833; Cilium Assembly.
DR BioGRID-ORCS; 73242; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Atat1; mouse.
DR PRO; PR:Q8K341; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K341; protein.
DR Bgee; ENSMUSG00000024426; Expressed in cortical plate and 207 other tissues.
DR ExpressionAtlas; Q8K341; baseline and differential.
DR Genevisible; Q8K341; MM.
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; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:InterPro.
DR GO; GO:0097427; C:microtubule bundle; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:0071929; P:alpha-tubulin acetylation; IMP:MGI.
DR GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR GO; GO:0048666; P:neuron development; IEA:UniProtKB-UniRule.
DR GO; GO:0044546; P:NLRP3 inflammasome complex assembly; IMP:MGI.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IMP:MGI.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:UniProtKB-UniRule.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
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; Alternative splicing; Cell junction;
KW Cell projection; Coated pit; Cytoplasm; Cytoskeleton; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="Alpha-tubulin N-acetyltransferase 1"
FT /id="PRO_0000348067"
FT DOMAIN 1..190
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130"
FT REGION 196..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 308..387
FT /note="Required for AP2A2-binding"
FT REGION 342..421
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..375
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:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23275437"
FT MOD_RES 146
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23275437"
FT MOD_RES 233
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23275437, ECO:0007744|PubMed:23806337"
FT MOD_RES 244
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03130,
FT ECO:0000269|PubMed:23275437"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG11"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
FT MOD_RES 305
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 323
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5SQI0"
FT VAR_SEQ 195..218
FT /note="RPPTSSLRATRHSRAAVADPIPAA -> P (in isoform 2 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052905"
FT VAR_SEQ 323..333
FT /note="RGTPWGLVAQS -> SSLPRSDESRY (in isoform 4 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052906"
FT VAR_SEQ 324..353
FT /note="GTPWGLVAQSCHYSRHGGFNTSFLGTGNQE -> SHTHTTTVSLDAWYFHRQ
FT PRTEAGGTGSGG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052908"
FT VAR_SEQ 334..421
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052907"
FT VAR_SEQ 354..421
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052909"
FT MUTAGEN 56
FT /note="K->R: Strong reduction in tubulin acetylation, no
FT effect on tubulin-binding; when associated with R-146; R-
FT 233 and R-244."
FT /evidence="ECO:0000269|PubMed:23275437"
FT MUTAGEN 134
FT /note="G->W: Loss of catalytic activity, but function in
FT microtubule stability not affected; when associated with W-
FT 136 and P-139."
FT /evidence="ECO:0000269|PubMed:23275437"
FT MUTAGEN 136
FT /note="G->W: Loss of activity, but function in microtubule
FT stability not affected; when associated with W-134 and P-
FT 139."
FT /evidence="ECO:0000269|PubMed:23275437"
FT MUTAGEN 139
FT /note="L->P: Loss of activity, but function in microtubule
FT stability not affected; when associated with W-134 and W-
FT 136."
FT /evidence="ECO:0000269|PubMed:23275437"
FT MUTAGEN 146
FT /note="K->R: Strong reduction in tubulin acetylation, no
FT effect on tubulin-binding; when associated with R-56; R-233
FT and R-244."
FT /evidence="ECO:0000269|PubMed:23275437"
FT MUTAGEN 233
FT /note="K->R: Strong reduction in tubulin acetylation, no
FT effect on tubulin-binding; when associated with R-56; R-146
FT and R-244."
FT /evidence="ECO:0000269|PubMed:23275437"
FT MUTAGEN 244
FT /note="K->R: Strong reduction in tubulin acetylation, no
FT effect on tubulin-binding; when associated with R-56; R-146
FT and R-233."
FT /evidence="ECO:0000269|PubMed:23275437"
FT CONFLICT 92
FT /note="A -> V (in Ref. 3; AAH30669)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="K -> E (in Ref. 1; BAC28808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47164 MW; E47F1060F183D19C CRC64;
MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIVDEL GKASAKAQHL
PAPITSALRM QSNRHVIYIL KDTSARPAGK GAIIGFLKVG YKKLFVLDDR EAHNEVEPLC
ILDFYIHESV QRHGHGRELF QHMLQKERVE PHQLAIDRPS PKLLKFLNKH YNLETTVPQV
NNFVIFEGFF AHQHRPPTSS LRATRHSRAA VADPIPAAPA RKLPPKRAEG DIKPYSSSDR
EFLKVAVEPP WPLNRAPRRA TPPAHPPPRS SSLGNSPDRG PLRPFVPEQE LLRSLRLCPP
HPTARLLLAT DPGGSPAQRR RTRGTPWGLV AQSCHYSRHG GFNTSFLGTG NQERKQGEQE
AEDRSASEDR VLLLDGSGEE PTQTGAPRAQ APPPQSWTVG GDIMNARVIR NLQERRSTRP
W
