NAA10_ARATH
ID NAA10_ARATH Reviewed; 192 AA.
AC Q9FKI4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=N-terminal acetyltransferase A complex catalytic subunit NAA10 {ECO:0000303|PubMed:25966763};
DE Short=AtNAA10 {ECO:0000303|PubMed:25966763};
DE EC=2.3.1.255 {ECO:0000269|PubMed:25966763};
GN Name=NAA10 {ECO:0000303|PubMed:25966763};
GN OrderedLocusNames=At5g13780 {ECO:0000312|Araport:AT5G13780};
GN ORFNames=MXE10.5 {ECO:0000312|EMBL:AAK96745.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH NAA15, DISRUPTION PHENOTYPE,
RP AND INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=26184543; DOI=10.1038/ncomms8640;
RA Linster E., Stephan I., Bienvenut W.V., Maple-Groedem J., Myklebust L.M.,
RA Huber M., Reichelt M., Sticht C., Moeller S.G., Meinnel T., Arnesen T.,
RA Giglione C., Hell R., Wirtz M.;
RT "Downregulation of N-terminal acetylation triggers ABA-mediated drought
RT responses in Arabidopsis.";
RL Nat. Commun. 6:7640-7640(2015).
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).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH NAA15.
RC STRAIN=cv. Columbia;
RX PubMed=27385766; DOI=10.1093/jxb/erw257;
RA Feng J., Li R., Yu J., Ma S., Wu C., Li Y., Cao Y., Ma L.;
RT "Protein N-terminal acetylation is required for embryogenesis in
RT Arabidopsis.";
RL J. Exp. Bot. 67:4779-4789(2016).
RN [8]
RP FUNCTION.
RX PubMed=27610925; DOI=10.1080/15592324.2016.1231293;
RA Feng J., Ma L.;
RT "NatA is required for suspensor development in Arabidopsis.";
RL Plant Signal. Behav. 11:E1231293-E1231293(2016).
CC -!- FUNCTION: Catalytic subunit of the NatA N-alpha-acetyltransferase
CC complex (PubMed:26184543, PubMed:25966763). Required for male
CC gametocyte development, embryogenesis, suspensor development and the
CC formation of the quiescent center (QC) in the root meristem
CC (PubMed:27385766, PubMed:27610925). Involved in plant immunity through
CC the regulation of SNC1 and RPM1 stability (PubMed:25966763).
CC {ECO:0000269|PubMed:25966763, ECO:0000269|PubMed:26184543,
CC ECO:0000269|PubMed:27385766, ECO:0000269|PubMed:27610925}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133369; EC=2.3.1.255;
CC Evidence={ECO:0000269|PubMed:25966763};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000269|PubMed:25966763};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000269|PubMed:25966763};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC ChEBI:CHEBI:133371; EC=2.3.1.255;
CC Evidence={ECO:0000269|PubMed:25966763};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC Evidence={ECO:0000269|PubMed:25966763};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC ChEBI:CHEBI:133375; EC=2.3.1.255;
CC Evidence={ECO:0000269|PubMed:25966763};
CC -!- SUBUNIT: Part of the NatA complex. Interacts with NAA15.
CC {ECO:0000269|PubMed:26184543, ECO:0000269|PubMed:27385766}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, shoots and flowers.
CC {ECO:0000269|PubMed:26184543}.
CC -!- INDUCTION: Down-regulated upon abscisic acid treatment.
CC {ECO:0000269|PubMed:26184543}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal when homozygous.
CC {ECO:0000269|PubMed:26184543, ECO:0000269|PubMed:27385766}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB011484; BAB10599.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91940.1; -; Genomic_DNA.
DR EMBL; AY054554; AAK96745.1; -; mRNA.
DR EMBL; AY064689; AAL47392.1; -; mRNA.
DR EMBL; AY087018; AAM64579.1; -; mRNA.
DR RefSeq; NP_196882.1; NM_121381.4.
DR AlphaFoldDB; Q9FKI4; -.
DR SMR; Q9FKI4; -.
DR IntAct; Q9FKI4; 10.
DR STRING; 3702.AT5G13780.1; -.
DR PaxDb; Q9FKI4; -.
DR PRIDE; Q9FKI4; -.
DR ProteomicsDB; 251359; -.
DR EnsemblPlants; AT5G13780.1; AT5G13780.1; AT5G13780.
DR GeneID; 831223; -.
DR Gramene; AT5G13780.1; AT5G13780.1; AT5G13780.
DR KEGG; ath:AT5G13780; -.
DR Araport; AT5G13780; -.
DR TAIR; locus:2177120; AT5G13780.
DR eggNOG; KOG3235; Eukaryota.
DR HOGENOM; CLU_013985_7_2_1; -.
DR InParanoid; Q9FKI4; -.
DR OMA; MSMQNAN; -.
DR OrthoDB; 1489230at2759; -.
DR PhylomeDB; Q9FKI4; -.
DR BRENDA; 2.3.1.255; 399.
DR PRO; PR:Q9FKI4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKI4; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0031415; C:NatA complex; IPI:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:TAIR.
DR GO; GO:1990190; F:peptide-glutamate-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:InterPro.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 1.
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..192
FT /note="N-terminal acetyltransferase A complex catalytic
FT subunit NAA10"
FT /id="PRO_0000439078"
FT DOMAIN 2..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 192 AA; 21715 MW; A1B0153B5623027A CRC64;
MVCIRRATVD DLLAMQACNL MCLPENYQMK YYLYHILSWP QLLYVAEDYN GRIVGYVLAK
MEEESNECHG HITSLAVLRT HRKLGLATKL MTAAQAAMEQ VYEAEYVSLH VRRSNRAAFN
LYTETLGYKI NDVEAKYYAD GEDAYDMRKN LKGKQNHHHA HGHHHHHGGG CCSGDAKVVE
TAQAVDGKAV SK
