NAA20_MOUSE
ID NAA20_MOUSE Reviewed; 178 AA.
AC P61600; Q14B28; Q4VAC3; Q9D7H8; Q9H0Y4; Q9NQH6; Q9Y6D2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=N-alpha-acetyltransferase 20;
DE EC=2.3.1.254 {ECO:0000250|UniProtKB:P61599};
DE AltName: Full=Methionine N-acetyltransferase;
DE AltName: Full=N-acetyltransferase 5;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20;
DE AltName: Full=N-terminal acetyltransferase B complex catalytic subunit NAT5;
DE Short=NatB complex subunit NAT5;
DE AltName: Full=NatB catalytic subunit;
GN Name=Naa20; Synonyms=Nat5;
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=Tongue;
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].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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=Brain, Heart, Kidney, Liver, Lung, 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: Catalytic subunit of the NatB complex which catalyzes
CC acetylation of the N-terminal methionine residues of peptides beginning
CC with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle
CC functions are overrepresented in the pool of NatB substrates. Required
CC for maintaining the structure and function of actomyosin fibers and for
CC proper cellular migration. {ECO:0000250|UniProtKB:P61599}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-asparaginyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:50484, Rhea:RHEA-COMP:12694, Rhea:RHEA-
CC COMP:12695, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133356, ChEBI:CHEBI:133358; EC=2.3.1.254;
CC Evidence={ECO:0000250|UniProtKB:P61599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutaminyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-
CC [protein]; Xref=Rhea:RHEA:50492, Rhea:RHEA-COMP:12698, Rhea:RHEA-
CC COMP:12699, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133361, ChEBI:CHEBI:133362; EC=2.3.1.254;
CC Evidence={ECO:0000250|UniProtKB:P61599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-aspartyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein];
CC Xref=Rhea:RHEA:50480, Rhea:RHEA-COMP:12692, Rhea:RHEA-COMP:12693,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133045, ChEBI:CHEBI:133063; EC=2.3.1.254;
CC Evidence={ECO:0000250|UniProtKB:P61599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-glutamyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein];
CC Xref=Rhea:RHEA:50488, Rhea:RHEA-COMP:12696, Rhea:RHEA-COMP:12697,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133359, ChEBI:CHEBI:133360; EC=2.3.1.254;
CC Evidence={ECO:0000250|UniProtKB:P61599};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex
CC which is composed of NAA20 and NAA25. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61599}. Nucleus
CC {ECO:0000250|UniProtKB:P61599}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK009229; BAB26152.1; -; mRNA.
DR EMBL; BC009157; AAH09157.1; -; mRNA.
DR EMBL; BC096451; AAH96451.1; -; mRNA.
DR EMBL; BC116374; AAI16375.1; -; mRNA.
DR CCDS; CCDS50735.1; -.
DR RefSeq; NP_001135437.1; NM_001141965.1.
DR RefSeq; NP_080701.1; NM_026425.3.
DR AlphaFoldDB; P61600; -.
DR SMR; P61600; -.
DR BioGRID; 212503; 6.
DR STRING; 10090.ENSMUSP00000002805; -.
DR iPTMnet; P61600; -.
DR PhosphoSitePlus; P61600; -.
DR EPD; P61600; -.
DR MaxQB; P61600; -.
DR PeptideAtlas; P61600; -.
DR PRIDE; P61600; -.
DR ProteomicsDB; 286136; -.
DR Antibodypedia; 24668; 137 antibodies from 26 providers.
DR DNASU; 67877; -.
DR Ensembl; ENSMUST00000110000; ENSMUSP00000105627; ENSMUSG00000002728.
DR GeneID; 67877; -.
DR KEGG; mmu:67877; -.
DR UCSC; uc008mry.2; mouse.
DR CTD; 51126; -.
DR MGI; MGI:1915127; Naa20.
DR VEuPathDB; HostDB:ENSMUSG00000002728; -.
DR eggNOG; KOG3234; Eukaryota.
DR GeneTree; ENSGT00550000075046; -.
DR InParanoid; P61600; -.
DR OMA; SGEIMGY; -.
DR OrthoDB; 1355894at2759; -.
DR BRENDA; 2.3.1.254; 3474.
DR BioGRID-ORCS; 67877; 30 hits in 77 CRISPR screens.
DR ChiTaRS; Naa20; mouse.
DR PRO; PR:P61600; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P61600; protein.
DR Bgee; ENSMUSG00000002728; Expressed in embryonic facial prominence and 65 other tissues.
DR ExpressionAtlas; P61600; baseline and differential.
DR Genevisible; P61600; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031416; C:NatB complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; ISO:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..178
FT /note="N-alpha-acetyltransferase 20"
FT /id="PRO_0000074535"
FT DOMAIN 2..157
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 178 AA; 20368 MW; C5CCEA50CD60E097 CRC64;
MTTLRAFTCD DLFRFNNINL DPLTETYGIP FYLQYLAHWP EYFIVAEAPG GELMGYIMGK
AEGSVAREEW HGHVTALSVA PEFRRLGLAA KLMELLEEIS ERKGGFFVDL FVRVSNQVAV
NMYKQLGYSV YRTVIEYYSA SNGEPDEDAY DMRKALSRDT EKKSIIPLPH PVRPEDIE
