NAT9_DROME
ID NAT9_DROME Reviewed; 200 AA.
AC Q9V9V9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Alpha/beta-tubulin-N-acetyltransferase 9 {ECO:0000305|PubMed:33479178};
DE EC=2.3.1.- {ECO:0000269|PubMed:33479178};
DE AltName: Full=Microtubule-associated Nat9 {ECO:0000312|FlyBase:FBgn0039859};
GN Name=Mnat9 {ECO:0000303|PubMed:33479178, ECO:0000312|FlyBase:FBgn0039859};
GN ORFNames=CG11539 {ECO:0000312|FlyBase:FBgn0039859};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ALPHA- AND BETA-TUBULIN,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 115-ARG--GLY-120.
RX PubMed=33479178; DOI=10.1073/pnas.2010140118;
RA Mok J.W., Choi K.W.;
RT "Novel function of N-acetyltransferase for microtubule stability and JNK
RT signaling in Drosophila organ development.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: N-acetyltransferase that mediates the acetylation of the N-
CC terminal residues of alpha- and beta-tubulin (PubMed:33479178).
CC Required for microtubule stability and inhibition of JNK signaling to
CC promote cell survival during development, possibly acting independently
CC of its N-acetyltransferase activity (PubMed:33479178). Necessary for
CC the stabilization of spindle microtubules and for mitosis progression
CC (PubMed:33479178). Regulates microtubule stability by inhibiting
CC Spastin-mediated depolymerization and promoting Eb1-mediated
CC polymerization (PubMed:33479178). {ECO:0000269|PubMed:33479178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-[tubulin] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-methionyl-[tubulin];
CC Xref=Rhea:RHEA:69607, Rhea:RHEA-COMP:17729, Rhea:RHEA-COMP:17730,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64731, ChEBI:CHEBI:133414;
CC Evidence={ECO:0000269|PubMed:33479178};
CC -!- SUBUNIT: Interacts with microtubules as well as alpha/beta-tubulin
CC heterodimers. {ECO:0000269|PubMed:33479178}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33479178}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:33479178}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:33479178}. Note=In
CC syncytial embryos, localization varies during mitosis
CC (PubMed:33479178). During interphase and prophase, detected around the
CC nucleus including surrounding tubulins (PubMed:33479178). During
CC metaphase and anaphase, highly enriched at the spindle poles and around
CC the spindle microtubules (PubMed:33479178). During telophase, detected
CC in the midbody region containing spindle microtubules
CC (PubMed:33479178). {ECO:0000269|PubMed:33479178}.
CC -!- DEVELOPMENTAL STAGE: Detected in syncytial embryos and larvae (at
CC protein level). {ECO:0000269|PubMed:33479178}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the posterior
CC compartment of the wing disk, results in adult wings that are reduced
CC in size, display abnormally thin veins and form blisters in the
CC posterior part of the wing (PubMed:33479178). Defects are mainly due to
CC activation of the JNK signaling pathway leading to increased apoptosis
CC in the developing wing (PubMed:33479178). RNAi-mediated knockdown in
CC the dorsoventral (DV) boundary and anterior-posterior (AP) boundary
CC regions of the wing disk, induces notching along the adult wing margin
CC and a reduction in the AP boundary region between the L3 and L4 veins
CC (PubMed:33479178). RNAi-mediated knockdown in the adult thorax causes
CC defects in the abdominal segments (PubMed:33479178). RNAi-mediated
CC knockdown in the adult eyes induces ectopic tissue growth and reduced
CC eye size (PubMed:33479178). RNAi-mediated knockdown in embryos, results
CC in various abnormal mitotic patterns, such as defective chromosome
CC alignments, short spindles and a loss of chromosomes (PubMed:33479178).
CC {ECO:0000269|PubMed:33479178}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF57173.1; -; Genomic_DNA.
DR EMBL; BT029052; ABJ16985.1; -; mRNA.
DR RefSeq; NP_001263148.1; NM_001276219.1.
DR RefSeq; NP_651877.1; NM_143620.2.
DR AlphaFoldDB; Q9V9V9; -.
DR SMR; Q9V9V9; -.
DR BioGRID; 68569; 14.
DR IntAct; Q9V9V9; 2.
DR STRING; 7227.FBpp0085227; -.
DR PaxDb; Q9V9V9; -.
DR DNASU; 43726; -.
DR EnsemblMetazoa; FBtr0085868; FBpp0085227; FBgn0039859.
DR EnsemblMetazoa; FBtr0337033; FBpp0307962; FBgn0039859.
DR GeneID; 43726; -.
DR KEGG; dme:Dmel_CG11539; -.
DR UCSC; CG11539-RA; d. melanogaster.
DR FlyBase; FBgn0039859; Mnat9.
DR VEuPathDB; VectorBase:FBgn0039859; -.
DR eggNOG; KOG4135; Eukaryota.
DR GeneTree; ENSGT00390000012745; -.
DR HOGENOM; CLU_073102_0_0_1; -.
DR InParanoid; Q9V9V9; -.
DR OMA; EARHVPK; -.
DR OrthoDB; 1507385at2759; -.
DR PhylomeDB; Q9V9V9; -.
DR BioGRID-ORCS; 43726; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43726; -.
DR PRO; PR:Q9V9V9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039859; Expressed in Malpighian tubule and 24 other tissues.
DR ExpressionAtlas; Q9V9V9; baseline and differential.
DR Genevisible; Q9V9V9; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IMP:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:FlyBase.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:FlyBase.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:FlyBase.
DR GO; GO:0006473; P:protein acetylation; IBA:GO_Central.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:FlyBase.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039135; NAT9-like.
DR PANTHER; PTHR13256; PTHR13256; 1.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..200
FT /note="Alpha/beta-tubulin-N-acetyltransferase 9"
FT /id="PRO_0000286876"
FT DOMAIN 34..181
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT MUTAGEN 115..120
FT /note="RGKGFG->AGKAFA: In AAA; overexpression results in a
FT weak thorax cleft."
FT /evidence="ECO:0000269|PubMed:33479178"
FT MUTAGEN 115..120
FT /note="Missing: In AcDel; overexpression results in a weak
FT thorax cleft. Microtubule polymerization activity is
FT slightly reduced."
FT /evidence="ECO:0000269|PubMed:33479178"
SQ SEQUENCE 200 AA; 23629 MW; DCBB5B2B3922AA95 CRC64;
MHLNENTKIL GHRVILVPYE ARHVPKYHEW MSNETLRELT ASEELTLEEE HEMQRSWRED
SDKLTFIVLD AETYSRDQDE IAAMVGDTNL FLHQDPDSQI PTAEAEIMIA EPYARGKGFG
REAMLLMLKY AQSQPQLKLD KFEVKIDMDN AASLHLFKSF MFVETRRVEI FHEVTLERPI
TPDWINWLDQ QVDLRMQCYQ
