ID   NAT9_MOUSE              Reviewed;         241 AA.
AC   Q3UG98; Q8C1G5; Q9D151;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Alpha/beta-tubulin-N-acetyltransferase 9 {ECO:0000250|UniProtKB:Q9BTE0};
DE            EC=2.3.1.308 {ECO:0000250|UniProtKB:Q9BTE0};
GN   Name=Nat9;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Testis;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   PROTEIN SEQUENCE OF 215-241, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Spleen, and Testis;
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).
CC   -!- FUNCTION: N-acetyltransferase that mediates the acetylation of the N-
CC       terminal residues of alpha- and beta-tubulin.
CC       {ECO:0000250|UniProtKB:Q9BTE0}.
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; EC=2.3.1.308;
CC         Evidence={ECO:0000250|UniProtKB:Q9BTE0};
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25613.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK003948; BAB23087.1; -; mRNA.
DR   EMBL; AK020083; BAC25613.1; ALT_FRAME; mRNA.
DR   EMBL; AK082469; BAC38501.1; -; mRNA.
DR   EMBL; AK148048; BAE28311.1; -; mRNA.
DR   EMBL; AL606487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011315; AAH11315.1; -; mRNA.
DR   CCDS; CCDS25622.1; -.
DR   RefSeq; NP_079676.1; NM_025400.3.
DR   RefSeq; XP_006533984.1; XM_006533921.3.
DR   RefSeq; XP_006533985.1; XM_006533922.2.
DR   AlphaFoldDB; Q3UG98; -.
DR   SMR; Q3UG98; -.
DR   BioGRID; 211273; 3.
DR   MINT; Q3UG98; -.
DR   STRING; 10090.ENSMUSP00000099329; -.
DR   GlyGen; Q3UG98; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3UG98; -.
DR   PhosphoSitePlus; Q3UG98; -.
DR   SwissPalm; Q3UG98; -.
DR   EPD; Q3UG98; -.
DR   MaxQB; Q3UG98; -.
DR   PaxDb; 10090-ENSMUSP00000099329; -.
DR   PeptideAtlas; Q3UG98; -.
DR   ProteomicsDB; 252778; -.
DR   Pumba; Q3UG98; -.
DR   Antibodypedia; 19466; 83 antibodies from 19 providers.
DR   DNASU; 66176; -.
DR   Ensembl; ENSMUST00000103038.8; ENSMUSP00000099327.2; ENSMUSG00000015542.18.
DR   Ensembl; ENSMUST00000103039.2; ENSMUSP00000099328.2; ENSMUSG00000015542.18.
DR   Ensembl; ENSMUST00000103040.11; ENSMUSP00000099329.5; ENSMUSG00000015542.18.
DR   Ensembl; ENSMUST00000103041.8; ENSMUSP00000099330.2; ENSMUSG00000015542.18.
DR   GeneID; 66176; -.
DR   KEGG; mmu:66176; -.
DR   UCSC; uc007mgr.1; mouse.
DR   AGR; MGI:1913426; -.
DR   CTD; 26151; -.
DR   MGI; MGI:1913426; Nat9.
DR   VEuPathDB; HostDB:ENSMUSG00000015542; -.
DR   eggNOG; KOG4135; Eukaryota.
DR   GeneTree; ENSGT00390000012745; -.
DR   HOGENOM; CLU_073102_1_1_1; -.
DR   InParanoid; Q3UG98; -.
DR   OMA; WHVPRYH; -.
DR   OrthoDB; 7623at2759; -.
DR   PhylomeDB; Q3UG98; -.
DR   TreeFam; TF315021; -.
DR   BioGRID-ORCS; 66176; 4 hits in 81 CRISPR screens.
DR   PRO; PR:Q3UG98; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q3UG98; Protein.
DR   Bgee; ENSMUSG00000015542; Expressed in spermatocyte and 247 other cell types or tissues.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR039135; NAT9-like.
DR   PANTHER; PTHR13256:SF16; ALPHA_BETA-TUBULIN-N-ACETYLTRANSFERASE 9; 1.
DR   PANTHER; PTHR13256; N-ACETYLTRANSFERASE 9; 1.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   Genevisible; Q3UG98; MM.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Reference proteome;
KW   Transferase.
FT   CHAIN           1..241
FT                   /note="Alpha/beta-tubulin-N-acetyltransferase 9"
FT                   /id="PRO_0000286875"
FT   DOMAIN          34..181
FT                   /note="N-acetyltransferase"
FT   CONFLICT        15
FT                   /note="V -> A (in Ref. 1; BAE28311)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="E -> K (in Ref. 1; BAC25613)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   241 AA;  27663 MW;  BC3E0C2C20E5554E CRC64;
     MKLNQNTMLV GKKVVLVPYT SEHVPRYHEW MKSEELRHLT ASEQLTLQQE YEMQCSWCED
     EDKCTFIVLD AEKWQAQPRP PEESCMVGDV NLFLTDLEDP TLGEIEVMIA EPSYRRQGLG
     TEASLLIMSY GVTKLGLTKF EAKIGQENEP SIRMFQKLHF KQVAMSNVFQ EVTLRLAVSE
     PERKWILEQT SHMEERPYRT RKAEPVTATL SEQKSWNCPL PRPDGCMGDT SAVSSVCARL
     S
//