NSI_ARATH
ID NSI_ARATH Reviewed; 258 AA.
AC Q7X9V3; A8MRN8; Q8LD61; Q9C6X3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Acetyltransferase NSI;
DE EC=2.3.1.-;
DE AltName: Full=Nuclear shuttle protein-interacting protein;
GN Name=NSI; OrderedLocusNames=At1g32070; ORFNames=T12O21.3;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, ACETYLATION, AND INTERACTION WITH CABBAGE LEAF CURL
RP VIRUS NSP.
RX PubMed=12837950; DOI=10.1105/tpc.012120;
RA McGarry R.C., Barron Y.D., Carvalho M.F., Hill J.E., Gold D., Cheung E.,
RA Kraus W.L., Lazarowitz S.G.;
RT "A novel Arabidopsis acetyltransferase interacts with the geminivirus
RT movement protein NSP.";
RL Plant Cell 15:1605-1618(2003).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-258 (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH BEGOMOVIRUSES NSP.
RX PubMed=15452236; DOI=10.1128/jvi.78.20.11161-11171.2004;
RA Carvalho M.F., Lazarowitz S.G.;
RT "Interaction of the movement protein NSP and the Arabidopsis
RT acetyltransferase AtNSI is necessary for Cabbage leaf curl geminivirus
RT infection and pathogenicity.";
RL J. Virol. 78:11161-11171(2004).
RN [8]
RP FUNCTION, MUTAGENESIS OF ILE-107; LYS-136 AND ASP-194, DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16461385; DOI=10.1104/pp.105.075556;
RA Carvalho M.F., Turgeon R., Lazarowitz S.G.;
RT "The geminivirus nuclear shuttle protein NSP inhibits the activity of
RT AtNSI, a vascular-expressed Arabidopsis acetyltransferase regulated with
RT the sink-to-source transition.";
RL Plant Physiol. 140:1317-1330(2006).
CC -!- FUNCTION: Acetyltransferase that acetylates in vitro histones H2A and
CC H3. Does not act as a transcriptional activator but might be involved
CC in the sink-source transition. In case of begomoviruses infection,
CC acetylates the capsid protein (CP), but not the nuclear shuttle protein
CC (NSP). Required for begomovirus infection and systemic spread.
CC {ECO:0000269|PubMed:12837950, ECO:0000269|PubMed:15452236,
CC ECO:0000269|PubMed:16461385}.
CC -!- ACTIVITY REGULATION: Inhibited by the viral nuclear shuttle protein
CC (NSP) that binds to the region required for oligomerization.
CC {ECO:0000269|PubMed:16461385}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.39 uM for acetate {ECO:0000269|PubMed:16461385};
CC Note=Vmax:15.1 fmol/min/pmol enzyme.;
CC -!- SUBUNIT: Oligomer. Interacts with begomoviruses NSP but not with CP.
CC This interaction may allow NSP to recruit NSI monomers to acetylate
CC viral genome-bound CP and thus regulate nuclear export of viral genome
CC by NSP. {ECO:0000269|PubMed:12837950, ECO:0000269|PubMed:15452236}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12837950}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7X9V3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7X9V3-2; Sequence=VSP_033513;
CC Name=3;
CC IsoId=Q7X9V3-3; Sequence=VSP_033514;
CC -!- TISSUE SPECIFICITY: Highly expressed in cauline leaves, at lower levels
CC in stems, siliques, inflorescences and rosettes leaves and at very low
CC levels in roots. Expressed in the xylem parenchyma and phloem of the
CC leaves and root, and in guard cells of young leaves.
CC {ECO:0000269|PubMed:12837950, ECO:0000269|PubMed:16461385}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the apical meristem, root vasculature
CC and all veins in the cotyledons of young developing seedlings. Loss of
CC expression in the older maturing tissues.
CC {ECO:0000269|PubMed:16461385}.
CC -!- PTM: Autoacetylated.
CC -!- MISCELLANEOUS: Lacks the bromodomain involved in binding of other
CC acetyltransferases to histones.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY281105; AAP22085.1; -; mRNA.
DR EMBL; AC074309; AAG50796.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31431.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31432.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31433.1; -; Genomic_DNA.
DR EMBL; AY086183; AAM64262.1; -; mRNA.
DR EMBL; BT024481; ABD19662.1; -; mRNA.
DR EMBL; BX818104; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A86445; A86445.
DR RefSeq; NP_001077641.1; NM_001084172.1. [Q7X9V3-3]
DR RefSeq; NP_564387.1; NM_102941.3. [Q7X9V3-2]
DR RefSeq; NP_973950.1; NM_202221.2. [Q7X9V3-1]
DR AlphaFoldDB; Q7X9V3; -.
DR SMR; Q7X9V3; -.
DR BioGRID; 25333; 5.
DR IntAct; Q7X9V3; 5.
DR STRING; 3702.AT1G32070.2; -.
DR iPTMnet; Q7X9V3; -.
DR PaxDb; Q7X9V3; -.
DR PRIDE; Q7X9V3; -.
DR ProteomicsDB; 250484; -. [Q7X9V3-1]
DR EnsemblPlants; AT1G32070.1; AT1G32070.1; AT1G32070. [Q7X9V3-2]
DR EnsemblPlants; AT1G32070.2; AT1G32070.2; AT1G32070. [Q7X9V3-1]
DR EnsemblPlants; AT1G32070.3; AT1G32070.3; AT1G32070. [Q7X9V3-3]
DR GeneID; 840099; -.
DR Gramene; AT1G32070.1; AT1G32070.1; AT1G32070. [Q7X9V3-2]
DR Gramene; AT1G32070.2; AT1G32070.2; AT1G32070. [Q7X9V3-1]
DR Gramene; AT1G32070.3; AT1G32070.3; AT1G32070. [Q7X9V3-3]
DR KEGG; ath:AT1G32070; -.
DR Araport; AT1G32070; -.
DR TAIR; locus:2195361; AT1G32070.
DR eggNOG; ENOG502QSCQ; Eukaryota.
DR InParanoid; Q7X9V3; -.
DR OMA; VPFHANY; -.
DR OrthoDB; 1429454at2759; -.
DR PhylomeDB; Q7X9V3; -.
DR PRO; PR:Q7X9V3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7X9V3; baseline and differential.
DR Genevisible; Q7X9V3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IDA:TAIR.
DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IDA:TAIR.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:TAIR.
DR GO; GO:0030187; P:melatonin biosynthetic process; IDA:TAIR.
DR GO; GO:0062055; P:photosynthetic state transition; IDA:TAIR.
DR GO; GO:0046739; P:transport of virus in multicellular host; IMP:TAIR.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR045039; NSI-like.
DR PANTHER; PTHR43626; PTHR43626; 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; Alternative splicing; Host-virus interaction; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..258
FT /note="Acetyltransferase NSI"
FT /id="PRO_0000333286"
FT DOMAIN 107..258
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 107..194
FT /note="Interaction with begomoviruses NSP protein"
FT VAR_SEQ 15
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_033513"
FT VAR_SEQ 164
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_033514"
FT MUTAGEN 107
FT /note="I->T: Complete loss of interaction with CaLCuV NSP
FT protein."
FT /evidence="ECO:0000269|PubMed:16461385"
FT MUTAGEN 136
FT /note="K->E: Complete loss of interaction with CaLCuV NSP
FT protein."
FT /evidence="ECO:0000269|PubMed:16461385"
FT MUTAGEN 194
FT /note="D->G: Complete loss of interaction with CaLCuV NSP
FT protein."
FT /evidence="ECO:0000269|PubMed:16461385"
SQ SEQUENCE 258 AA; 28649 MW; B71F5A70BA7BF912 CRC64;
MLLIPISSSS SSSISPPPNS YPSNHHSLFF SNLTFPIQHG SRKLKTLRLR ANFWESIRSG
FVKNNNSTQL VEPPSIVNDE EEETEPLLPV EFTLVERNLE DGLVEEIIFS SGGEIDVYDL
QGLCDKVGWP RRPLVKLAAA LKNSYMVATL HSVMKSSSDS DSSEGGDGEK QQEKKLIGMA
RATSDHAFNA TIWDVLVDPE YQGQGLGKAL VEKLVRALLQ RDIGNISLFA DSQVVDFYQN
LGFEADPEGI KGMFWYPK
