NAA15_MOUSE
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 03-AUG-2022, entry version 145.
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, Pancreas,
RC 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 iPTMnet; Q80UM3; -.
DR PhosphoSitePlus; Q80UM3; -.
DR SwissPalm; Q80UM3; -.
DR EPD; Q80UM3; -.
DR MaxQB; Q80UM3; -.
DR PaxDb; Q80UM3; -.
DR PeptideAtlas; Q80UM3; -.
DR PRIDE; Q80UM3; -.
DR ProteomicsDB; 252637; -.
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:0016407; F:acetyltransferase activity; 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:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR InterPro; IPR021183; NatA_aux_su.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12569; NARP1; 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; SSF48452; 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
