NAA30_MOUSE
ID NAA30_MOUSE Reviewed; 364 AA.
AC Q8CES0; B2RY23; Q7TN07;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=N-alpha-acetyltransferase 30;
DE EC=2.3.1.256 {ECO:0000250|UniProtKB:Q147X3};
DE AltName: Full=N-acetyltransferase 12;
DE AltName: Full=N-acetyltransferase MAK3 homolog;
DE AltName: Full=NatC catalytic subunit;
GN Name=Naa30; Synonyms=Mak3, Nat12;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-54, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235, 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).
CC -!- FUNCTION: Catalytic subunit of the N-terminal acetyltransferase C
CC (NatC) complex. Catalyzes acetylation of the N-terminal methionine
CC residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly.
CC Necessary for the lysosomal localization and function of ARL8B
CC sugeesting that ARL8B is a NatC substrate.
CC {ECO:0000250|UniProtKB:Q147X3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-
CC [protein]; Xref=Rhea:RHEA:50524, Rhea:RHEA-COMP:12713, Rhea:RHEA-
CC COMP:12714, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133379, ChEBI:CHEBI:133380; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-
CC [protein]; Xref=Rhea:RHEA:50560, Rhea:RHEA-COMP:12724, Rhea:RHEA-
CC COMP:12725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133386, ChEBI:CHEBI:133387; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase C (NatC)
CC complex, which is composed of NAA35, NAA38 and NAA30.
CC {ECO:0000250|UniProtKB:Q147X3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q147X3}. Nucleus
CC {ECO:0000250|UniProtKB:Q147X3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CES0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CES0-2; Sequence=VSP_031582, VSP_031583;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25468.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK015640; BAC25468.1; ALT_FRAME; mRNA.
DR EMBL; BC054060; AAH54060.1; -; mRNA.
DR EMBL; BC158065; AAI58066.1; -; mRNA.
DR CCDS; CCDS84137.1; -. [Q8CES0-1]
DR RefSeq; NP_081768.2; NM_027492.2. [Q8CES0-1]
DR AlphaFoldDB; Q8CES0; -.
DR SMR; Q8CES0; -.
DR BioGRID; 214186; 2.
DR STRING; 10090.ENSMUSP00000041450; -.
DR iPTMnet; Q8CES0; -.
DR PhosphoSitePlus; Q8CES0; -.
DR EPD; Q8CES0; -.
DR MaxQB; Q8CES0; -.
DR PaxDb; Q8CES0; -.
DR PeptideAtlas; Q8CES0; -.
DR PRIDE; Q8CES0; -.
DR ProteomicsDB; 293610; -. [Q8CES0-1]
DR ProteomicsDB; 293611; -. [Q8CES0-2]
DR Antibodypedia; 24132; 71 antibodies from 17 providers.
DR Ensembl; ENSMUST00000153488; ENSMUSP00000121679; ENSMUSG00000036282. [Q8CES0-1]
DR GeneID; 70646; -.
DR KEGG; mmu:70646; -.
DR UCSC; uc007tkc.1; mouse. [Q8CES0-1]
DR UCSC; uc007tkd.1; mouse. [Q8CES0-2]
DR CTD; 122830; -.
DR MGI; MGI:1922259; Naa30.
DR VEuPathDB; HostDB:ENSMUSG00000036282; -.
DR eggNOG; KOG3139; Eukaryota.
DR GeneTree; ENSGT00390000005665; -.
DR HOGENOM; CLU_013985_0_0_1; -.
DR InParanoid; Q8CES0; -.
DR OrthoDB; 1323575at2759; -.
DR PhylomeDB; Q8CES0; -.
DR BioGRID-ORCS; 70646; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Naa30; mouse.
DR PRO; PR:Q8CES0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8CES0; protein.
DR Bgee; ENSMUSG00000036282; Expressed in secondary oocyte and 257 other tissues.
DR ExpressionAtlas; Q8CES0; baseline and differential.
DR Genevisible; Q8CES0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031417; C:NatC complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; ISO:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR044542; NAA30-like.
DR PANTHER; PTHR45896; PTHR45896; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..364
FT /note="N-alpha-acetyltransferase 30"
FT /id="PRO_0000320033"
FT DOMAIN 216..364
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q147X3"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q147X3"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q147X3"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..229
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031582"
FT VAR_SEQ 230..259
FT /note="MRLITKDLSEPYSIYTYRYFIHNWPQLCFL -> MLPQSLLLFPLVIVQYLM
FT AMCLHNCLFIFK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031583"
FT CONFLICT 362..363
FT /note="WL -> CV (in Ref. 1; BAC25468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39433 MW; 94625FF77A700A14 CRC64;
MAEVPPGPSS LLPPPAPAAP AAAELRCPFP AGAALACCSE DEEDDEEHEG GCGSPAGGEA
ATSAKARSCL RCPQLPPEQQ QQQLNGLIGP ELRHLRAAAT LKSKVLSAAE AAAPDGASKV
TATKGAEGHP GERPPHSVPN NARTALPGRS EAAAAAAGAA SDPAAARNGL VEGTEQQEEE
EMDEQVRLLS SSLTTGCSLR SSQGREAEPG EDRTIRYVRY ESELQMPDIM RLITKDLSEP
YSIYTYRYFI HNWPQLCFLA MVGEECVGAI VCKLDMHKKM FRRGYIAMLA VDSKYRRNGI
GTNLVKKAIY AMVEGDCDEV VLETEITNKS ALKLYENLGF VRDKRLFRYY LNGVDALRLK
LWLR
