NAA20_ARATH
ID NAA20_ARATH Reviewed; 174 AA.
AC Q8LGI8; Q94EZ1; Q9SA54;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=N-terminal acetyltransferase B complex catalytic subunit NAA20 {ECO:0000303|PubMed:25966763};
DE EC=2.3.1.254 {ECO:0000269|PubMed:25966763};
DE AltName: Full=NatB N-alpha-terminal acetylation complex catalytic subunit {ECO:0000303|PubMed:24244708};
GN Name=NAA20 {ECO:0000303|PubMed:25966763};
GN Synonyms=NBC {ECO:0000303|PubMed:24244708};
GN OrderedLocusNames=At1g03150 {ECO:0000312|Araport:AT1G03150};
GN ORFNames=F10O3.2 {ECO:0000312|EMBL:AAD25793.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=24244708; DOI=10.1371/journal.pone.0080697;
RA Ferrandez-Ayela A., Micol-Ponce R., Sanchez-Garcia A.B., Alonso-Peral M.M.,
RA Micol J.L., Ponce M.R.;
RT "Mutation of an Arabidopsis NatB N-alpha-terminal acetylation complex
RT component causes pleiotropic developmental defects.";
RL PLoS ONE 8:E80697-E80697(2013).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25966763; DOI=10.1105/tpc.15.00173;
RA Xu F., Huang Y., Li L., Gannon P., Linster E., Huber M., Kapos P.,
RA Bienvenut W., Polevoda B., Meinnel T., Hell R., Giglione C., Zhang Y.,
RA Wirtz M., Chen S., Li X.;
RT "Two N-terminal acetyltransferases antagonistically regulate the stability
RT of a nod-like receptor in Arabidopsis.";
RL Plant Cell 27:1547-1562(2015).
CC -!- FUNCTION: Catalytic subunit of the NatB N-alpha-acetyltransferase
CC complex. Involved in plant immunity through the regulation of SNC1
CC stability (PubMed:25966763). {ECO:0000269|PubMed:25966763}.
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:0000269|PubMed:25966763};
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:0000269|PubMed:25966763};
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:0000269|PubMed:25966763};
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:0000269|PubMed:25966763};
CC -!- DISRUPTION PHENOTYPE: Reticulated leaves, early flowering and aborted
CC or unfertilized ovules in siliques. {ECO:0000269|PubMed:24244708}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25793.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006550; AAD25793.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27536.1; -; Genomic_DNA.
DR EMBL; AF387013; AAK62458.1; -; mRNA.
DR EMBL; AY081466; AAM10028.1; -; mRNA.
DR EMBL; AY084247; AAM60842.1; -; mRNA.
DR PIR; F86162; F86162.
DR RefSeq; NP_563677.1; NM_100197.3.
DR AlphaFoldDB; Q8LGI8; -.
DR SMR; Q8LGI8; -.
DR IntAct; Q8LGI8; 2.
DR STRING; 3702.AT1G03150.1; -.
DR iPTMnet; Q8LGI8; -.
DR PaxDb; Q8LGI8; -.
DR PRIDE; Q8LGI8; -.
DR ProteomicsDB; 251343; -.
DR EnsemblPlants; AT1G03150.1; AT1G03150.1; AT1G03150.
DR GeneID; 839562; -.
DR Gramene; AT1G03150.1; AT1G03150.1; AT1G03150.
DR KEGG; ath:AT1G03150; -.
DR Araport; AT1G03150; -.
DR TAIR; locus:2007584; AT1G03150.
DR eggNOG; KOG3234; Eukaryota.
DR HOGENOM; CLU_013985_7_1_1; -.
DR InParanoid; Q8LGI8; -.
DR OMA; TILDYYA; -.
DR OrthoDB; 1355894at2759; -.
DR PhylomeDB; Q8LGI8; -.
DR PRO; PR:Q8LGI8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LGI8; baseline and differential.
DR GO; GO:0031416; C:NatB complex; IBA:GO_Central.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..174
FT /note="N-terminal acetyltransferase B complex catalytic
FT subunit NAA20"
FT /id="PRO_0000439081"
FT DOMAIN 2..151
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT CONFLICT 153
FT /note="D -> N (in Ref. 3; AAK62458/AAM10028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 20395 MW; 2489531C2BB45D49 CRC64;
MTTIRRFSCN DLLRFTSVNL DHLTETFNMS FYMTYLARWP DYFHVAEGPG NRVMGYIMGK
VEGQGESWHG HVTAVTVSPE YRRQQLAKKL MNLLEDISDK IDKAYFVDLF VRASNTPAIK
MYEKLGYIIY RRVLRYYSGE EDGLDMRKAL SRDVEKKSVI PLKRPITPDE LEYD
