ID   NAA15_MOUSE             Reviewed;         865 AA.
AC   Q80UM3; Q811Z9; Q9JID5;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=N-alpha-acetyltransferase 15, NatA auxiliary subunit;
DE   AltName: Full=N-terminal acetyltransferase 1;
DE   AltName: Full=NMDA receptor-regulated protein 1;
DE   AltName: Full=Protein tubedown-1;
GN   Name=Naa15; Synonyms=Narg1, Nat1, Tbdn-1, Tubedown;
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 [MRNA], INTERACTION WITH XRCC6 AND XRCC5, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RC   TISSUE=Heart;
RX   PubMed=12145306; DOI=10.1074/jbc.m206482200;
RA   Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S., Ornitz D.M.,
RA   Towler D.A.;
RT   "Regulation of osteocalcin gene expression by a novel Ku antigen
RT   transcription factor complex.";
RL   J. Biol. Chem. 277:37280-37291(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN THE N-TERMINAL
RP   ACETYLTRANSFERASE A COMPLEX, INTERACTION WITH NAA10, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=12888564; DOI=10.1074/jbc.m301218200;
RA   Sugiura N., Adams S.M., Corriveau R.A.;
RT   "An evolutionarily conserved N-terminal acetyltransferase complex
RT   associated with neuronal development.";
RL   J. Biol. Chem. 278:40113-40120(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=ICR; TISSUE=Trophoblast stem cell;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 158-865, CHARACTERIZATION, ACETYLATION, AND
RP   FUNCTION.
RC   STRAIN=ICR; TISSUE=Embryo;
RX   PubMed=10842358;
RX   DOI=10.1002/(sici)1097-0177(200006)218:2<300::aid-dvdy5>3.0.co;2-k;
RA   Gendron R.L., Adams L.C., Paradis H.;
RT   "Tubedown-1, a novel acetyltransferase associated with blood vessel
RT   development.";
RL   Dev. Dyn. 218:300-315(2000).
RN   [5]
RP   IDENTIFICATION, INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11297529; DOI=10.1074/jbc.m100011200;
RA   Sugiura N., Patel R.G., Corriveau R.A.;
RT   "N-methyl-D-aspartate receptors regulate a group of transiently expressed
RT   genes in the developing brain.";
RL   J. Biol. Chem. 276:14257-14263(2001).
RN   [6]
RP   FUNCTION.
RX   PubMed=15452080; DOI=10.1167/iovs.03-1410;
RA   Wall D.S., Gendron R.L., Good W.V., Miskiewicz E., Woodland M., Leblanc K.,
RA   Paradis H.;
RT   "Conditional knockdown of tubedown-1 in endothelial cells leads to
RT   neovascular retinopathy.";
RL   Invest. Ophthalmol. Vis. Sci. 45:3704-3712(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854 AND SER-855, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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: Auxillary subunit of N-terminal acetyltransferase complexes
CC       which display alpha (N-terminal) acetyltransferase (NAT) activity. The
CC       NAT activity may be important for vascular, hematopoietic and neuronal
CC       growth and development. Required to control retinal neovascularization
CC       in adult ocular endothelial cells. In complex with XRCC6 and XRCC5
CC       (Ku80), up-regulates transcription from the osteocalcin promoter.
CC       {ECO:0000269|PubMed:10842358, ECO:0000269|PubMed:12145306,
CC       ECO:0000269|PubMed:12888564, ECO:0000269|PubMed:15452080}.
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase A complex (also
CC       called the NatA complex) composed of NAA10 and NAA15 (PubMed:12888564).
CC       Within the complex interacts with NAA10 (PubMed:12888564). Component of
CC       the N-terminal acetyltransferase A (NatA)/HYPK complex at least
CC       composed of NAA10, NAA15 and HYPK, which has N-terminal
CC       acetyltransferase activity (By similarity). In complex with NAA10,
CC       interacts with HYPK (By similarity). Component of the N-terminal
CC       acetyltransferase E (NatE) complex at least composed of NAA10, NAA15
CC       and NAA50 (By similarity). Within the complex interacts with NAA10; the
CC       interaction is required for binding to NAA50 (By similarity). Interacts
CC       with NAAT50 (By similarity). The interaction of the NatA complex with
CC       NAA50 reduces the acetylation activity of the NatA complex (By
CC       similarity). Component of the N-terminal acetyltransferase E
CC       (NatE)/HYPK complex at least composed of NAA10, NAA15, NAA50 and HYPK
CC       (By similarity). In complex with NAA10 interacts with HYPK; the
CC       interaction with HYPK reduces the capacity of the NatA complex to
CC       interact with NAA50 (By similarity). Interacts with NAA11 (By
CC       similarity). Interacts with XRCC6 and XRCC5 (PubMed:12145306).
CC       {ECO:0000250|UniProtKB:Q9BXJ9, ECO:0000269|PubMed:12145306,
CC       ECO:0000269|PubMed:12888564}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cytoplasm, perinuclear region {ECO:0000250}. Note=Mainly cytoplasmic,
CC       nuclear in some cases. Present in the free cytosolic and cytoskeleton-
CC       bound polysomes, but not in the membrane-bound polysomes.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Endothelial cells, osteoblasts and myeloid cells of
CC       the hematopoietic tissue. Present in adult ovary, bone marrow, brain,
CC       heart, kidney, testis and osteoblasts. {ECO:0000269|PubMed:11297529,
CC       ECO:0000269|PubMed:12145306, ECO:0000269|PubMed:12888564}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in endothelial cells during
CC       embryonic vasculogenesis, and then down-regulated and restricted to
CC       specific endothelial cells. In the brain, expression is highest in
CC       regions that contain dividing and proliferating cells. As brain
CC       development progresses, expression restricts to the hippocampus and
CC       cerebellar cortex. {ECO:0000269|PubMed:11297529}.
CC   -!- INDUCTION: Regulated by NMDA receptor. {ECO:0000269|PubMed:11297529}.
CC   -!- PTM: Acetylated. {ECO:0000269|PubMed:10842358}.
CC   -!- PTM: Cleaved by caspases during apoptosis. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF73953.2; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAF73953.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF510858; AAO33713.1; -; mRNA.
DR   EMBL; BC050017; AAH50017.1; -; mRNA.
DR   EMBL; AF237622; AAF73953.2; ALT_SEQ; mRNA.
DR   CCDS; CCDS17340.1; -.
DR   AlphaFoldDB; Q80UM3; -.
DR   SMR; Q80UM3; -.
DR   IntAct; Q80UM3; 6.
DR   MINT; Q80UM3; -.
DR   STRING; 10090.ENSMUSP00000029303; -.
DR   GlyGen; Q80UM3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q80UM3; -.
DR   PhosphoSitePlus; Q80UM3; -.
DR   SwissPalm; Q80UM3; -.
DR   EPD; Q80UM3; -.
DR   MaxQB; Q80UM3; -.
DR   PaxDb; 10090-ENSMUSP00000029303; -.
DR   PeptideAtlas; Q80UM3; -.
DR   ProteomicsDB; 252637; -.
DR   Pumba; Q80UM3; -.
DR   AGR; MGI:1922088; -.
DR   MGI; MGI:1922088; Naa15.
DR   eggNOG; KOG1156; Eukaryota.
DR   InParanoid; Q80UM3; -.
DR   PhylomeDB; Q80UM3; -.
DR   ChiTaRS; Naa15; mouse.
DR   PRO; PR:Q80UM3; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q80UM3; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0031415; C:NatA complex; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IDA:MGI.
DR   GO; GO:0043022; F:ribosome binding; ISO:MGI.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   Gene3D; 1.25.40.1010; -; 1.
DR   Gene3D; 1.25.40.1040; -; 1.
DR   InterPro; IPR021183; NatA_aux_su.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR22767:SF6; N-ALPHA-ACETYLTRANSFERASE 15, NATA AUXILIARY SUBUNIT; 1.
DR   PANTHER; PTHR22767; N-TERMINAL ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF12569; NatA_aux_su; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   PIRSF; PIRSF000422; N-terminal-AcTrfase-A_aux_su; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Angiogenesis; Cytoplasm; Developmental protein;
KW   Differentiation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   TPR repeat; Transcription; Transcription regulation.
FT   CHAIN           1..865
FT                   /note="N-alpha-acetyltransferase 15, NatA auxiliary
FT                   subunit"
FT                   /id="PRO_0000106295"
FT   REPEAT          46..79
FT                   /note="TPR 1"
FT   REPEAT          80..113
FT                   /note="TPR 2"
FT   REPEAT          148..184
FT                   /note="TPR 3"
FT   REPEAT          224..257
FT                   /note="TPR 4"
FT   REPEAT          374..407
FT                   /note="TPR 5"
FT   REPEAT          409..441
FT                   /note="TPR 6"
FT   REPEAT          485..518
FT                   /note="TPR 7"
FT   REPEAT          672..705
FT                   /note="TPR 8"
FT   REPEAT          799..834
FT                   /note="TPR 9"
FT   REGION          500..865
FT                   /note="Interaction with HYPK"
FT                   /evidence="ECO:0000250"
FT   REGION          575..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           612..629
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         262
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT   MOD_RES         588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT   MOD_RES         734
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT   MOD_RES         755
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXJ9"
FT   MOD_RES         854
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         855
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   CONFLICT        256
FT                   /note="G -> E (in Ref. 2 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="R -> K (in Ref. 2 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        452
FT                   /note="V -> M (in Ref. 2 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        620
FT                   /note="Q -> P (in Ref. 4; AAF73953)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="Q -> P (in Ref. 4; AAF73953)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        704
FT                   /note="G -> S (in Ref. 2 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        814
FT                   /note="G -> R (in Ref. 4; AAF73953)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   865 AA;  100961 MW;  230C5B6EE8697440 CRC64;
     MPAVSLPPKE NALFKRILRC YEHKQYRNGL KFCKQILSNP KFAEHGETLA MKGLTLNCLG
     KKEEAYELVR RGLRNDLKSH VCWHVYGLLQ RSDKKYDEAI KCYRNALKWD KDNLQILRDL
     SLLQIQMRDL EGYRETRYQL LQLRPAQRAS WIGYAIAYHL LEDYEMAAKI LEEFRKTQQT
     SPDKVDYEYS ELLLYQNQVL REAGLYREAL EHLCTYEKQI CDKLAVEETK GELLLQLCRL
     EDAADVYRGL QERNPGNWAY YKGLEKALKP ANMLERLKIY EEAWTKYPRG LVPRRLPLNF
     LSGEKFKECL DRFLRMNFSK GCPPVFNTLR SLYRDKEKVA IVEELVVGYE TSLKSCRLFN
     PNDDGKEEPP TTLLWVQYYL AQHYDKIGQP SIALEYINTA IESTPTLIEL FLVKAKIYKH
     AGNIKEAARW MDEAQALDTA DRFINSKCAK YVLKANLIKE AEEMCSKFTR EGTSAVENLN
     EMQCMWFQTE CAQAYKAMNK FGEALKKCHE IERHFIEITD DQFDFHTYCM RKITLRSYVD
     LLKLEDVLRQ HPFYFKAARI AIEIYLKLHD NPLTDENKEH EADTANMSDK ELKKLRNKQR
     RAQKKAQIEE EKKNAEKEKQ QRNQKKKKDD DDEEIGGPKE ELIPEKLAKV ETPLEEAIKF
     LTPLKNLVKN KIETHLFAFE IYFRKEKFLL MLQSVKRAFA IDSGHPWLHE CMIRLFHSVC
     ESKDLPETVR TVLKQEMNRL FGATNPKNFN ETFLKRNSDS LPHRLSAAKM VYYLDSSSQK
     RAIELATTLD GSLTNRNLQT CMEVLEALCD GSLGDCKEAA EAYRASCHKL FPYALAFMPP
     GYEEDMKITV NGDSSAETEE LANEI
//