NAC50_ARATH
ID NAC50_ARATH Reviewed; 447 AA.
AC Q9SQX9; F4J3S8;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=NAC domain containing protein 50 {ECO:0000303|PubMed:15029955};
DE Short=ANAC050 {ECO:0000303|PubMed:15029955};
GN Name=NAC050 {ECO:0000303|PubMed:15029955};
GN Synonyms=NAC50 {ECO:0000303|PubMed:15029955};
GN OrderedLocusNames=At3g10480 {ECO:0000312|Araport:AT3G10480};
GN ORFNames=F13M14.24 {ECO:0000312|EMBL:AAG51394.1},
GN F18K10.5 {ECO:0000312|EMBL:AAF76349.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 1).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15029955; DOI=10.1093/dnares/10.6.239;
RA Ooka H., Satoh K., Doi K., Nagata T., Otomo Y., Murakami K., Matsubara K.,
RA Osato N., Kawai J., Carninci P., Hayashizaki Y., Suzuki K., Kojima K.,
RA Takahara Y., Yamamoto K., Kikuchi S.;
RT "Comprehensive analysis of NAC family genes in Oryza sativa and Arabidopsis
RT thaliana.";
RL DNA Res. 10:239-247(2003).
RN [5]
RP FUNCTION, AND GENE FAMILY.
RX PubMed=24045019; DOI=10.1105/tpc.113.117168;
RA De Clercq I., Vermeirssen V., Van Aken O., Vandepoele K., Murcha M.W.,
RA Law S.R., Inze A., Ng S., Ivanova A., Rombaut D., van de Cotte B.,
RA Jaspers P., Van de Peer Y., Kangasjaervi J., Whelan J., Van Breusegem F.;
RT "The membrane-bound NAC transcription factor ANAC013 functions in
RT mitochondrial retrograde regulation of the oxidative stress response in
RT Arabidopsis.";
RL Plant Cell 25:3472-3490(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH JMJ14, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26617990; DOI=10.1038/celldisc.2015.3;
RA Zhang S., Zhou B., Kang Y., Cui X., Liu A., Deleris A., Greenberg M.V.C.,
RA Cui X., Qiu Q., Lu F., Wohlschlegel J.A., Jacobsen S.E., Cao X.;
RT "C-terminal domains of a histone demethylase interact with a pair of
RT transcription factors and mediate specific chromatin association.";
RL Cell Discov. 1:0-0(2015).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH JMJ14 AND NAC052, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25578968; DOI=10.1093/nar/gku1382;
RA Ning Y.-Q., Ma Z.-Y., Huang H.-W., Mo H., Zhao T.-T., Li L., Cai T.,
RA Chen S., Ma L., He X.-J.;
RT "Two novel NAC transcription factors regulate gene expression and flowering
RT time by associating with the histone demethylase JMJ14.";
RL Nucleic Acids Res. 43:1469-1484(2015).
CC -!- FUNCTION: Transcriptional repressor that binds to the motif 5'-
CC (C/T)A(C/A)G-3' in the promoter of target genes (PubMed:25578968).
CC Binds also to the 5'-CTTGNNNNNCAAG-3' consensus sequence in chromatin
CC (PubMed:26617990). Can bind to the mitochondrial dysfunction motif
CC (MDM) present in the upstream regions of mitochondrial dysfunction
CC stimulon (MDS) genes involved in mitochondrial retrograde regulation
CC (MRR) (PubMed:24045019). Together with NAC051/NAC052 and JMJ14,
CC regulates gene expression and flowering time by associating with the
CC histone demethylase JMJ14, probably by the promotion of RNA-mediated
CC gene silencing (PubMed:25578968, PubMed:26617990).
CC {ECO:0000269|PubMed:24045019, ECO:0000269|PubMed:25578968,
CC ECO:0000269|PubMed:26617990}.
CC -!- SUBUNIT: Interacts with JMJ14 and NAC052. {ECO:0000269|PubMed:25578968,
CC ECO:0000269|PubMed:26617990}.
CC -!- INTERACTION:
CC Q9SQX9; Q9SGP3: AGL58; NbExp=3; IntAct=EBI-4428214, EBI-15204316;
CC Q9SQX9; Q8LCT6: At1g24210; NbExp=3; IntAct=EBI-4428214, EBI-15203222;
CC Q9SQX9; Q9LFQ1: At5g15040; NbExp=3; IntAct=EBI-4428214, EBI-15196959;
CC Q9SQX9; Q8GUI6: JMJ14; NbExp=4; IntAct=EBI-4428214, EBI-4429826;
CC Q9SQX9; Q9SN22: SCL32; NbExp=3; IntAct=EBI-4428214, EBI-15196807;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC ECO:0000269|PubMed:26617990}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SQX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SQX9-2; Sequence=VSP_059198;
CC -!- TISSUE SPECIFICITY: Mostly expressed in floral organs, and, at low
CC levels, in other organs. {ECO:0000269|PubMed:25578968}.
CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC -!- DISRUPTION PHENOTYPE: The double mutant nac050 nac052 exhibits early
CC flowering and increased H3K4 methylation on specific genes, thus
CC leading to their derepression (PubMed:25578968). Impaired RNA-mediated
CC gene silencing (PubMed:26617990). {ECO:0000269|PubMed:25578968,
CC ECO:0000269|PubMed:26617990}.
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DR EMBL; AC011560; AAG51394.1; -; Genomic_DNA.
DR EMBL; AC013428; AAF76349.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74912.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74913.1; -; Genomic_DNA.
DR EMBL; AY059795; AAL24143.1; -; mRNA.
DR EMBL; AY091262; AAM14201.1; -; mRNA.
DR RefSeq; NP_566374.1; NM_111883.5. [Q9SQX9-1]
DR RefSeq; NP_974272.1; NM_202543.2. [Q9SQX9-2]
DR AlphaFoldDB; Q9SQX9; -.
DR SMR; Q9SQX9; -.
DR IntAct; Q9SQX9; 17.
DR iPTMnet; Q9SQX9; -.
DR PRIDE; Q9SQX9; -.
DR ProteomicsDB; 251031; -. [Q9SQX9-1]
DR EnsemblPlants; AT3G10480.1; AT3G10480.1; AT3G10480. [Q9SQX9-1]
DR EnsemblPlants; AT3G10480.2; AT3G10480.2; AT3G10480. [Q9SQX9-2]
DR GeneID; 820212; -.
DR Gramene; AT3G10480.1; AT3G10480.1; AT3G10480. [Q9SQX9-1]
DR Gramene; AT3G10480.2; AT3G10480.2; AT3G10480. [Q9SQX9-2]
DR KEGG; ath:AT3G10480; -.
DR Araport; AT3G10480; -.
DR HOGENOM; CLU_035664_13_0_1; -.
DR OMA; QYKRRRH; -.
DR PhylomeDB; Q9SQX9; -.
DR PRO; PR:Q9SQX9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQX9; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0060966; P:regulation of gene silencing by RNA; IMP:UniProtKB.
DR Gene3D; 2.170.150.80; -; 1.
DR InterPro; IPR003441; NAC-dom.
DR InterPro; IPR036093; NAC_dom_sf.
DR Pfam; PF02365; NAM; 1.
DR SUPFAM; SSF101941; SSF101941; 1.
DR PROSITE; PS51005; NAC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Flowering; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..447
FT /note="NAC domain containing protein 50"
FT /id="PRO_0000442194"
FT DOMAIN 27..178
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 126..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 392..447
FT /evidence="ECO:0000255"
FT COMPBIAS 251..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 167
FT /note="Missing (in isoform 2)"
FT /id="VSP_059198"
SQ SEQUENCE 447 AA; 50355 MW; 9D0527D228CAD3B1 CRC64;
MGRESLAVVS SPPSATAPST AVSATSLAPG FRFHPTDEEL VSYYLKRKVL GKPVRFDAIG
EVDIYKHEPW DLAVFSKLKT RDQEWYFFSA LDKKYGNGAR MNRATNKGYW KATGKDREIR
RDIQLLGMKK TLVFHSGRAP DGLRTNWVMH EYRLVEYETE TNGSLLQDAY VLCRVFHKNN
IGPPSGNRYA PFMEEEWADG GGALIPGIDV RVRVEALPQA NGNNQMDQEM HSASKDLINI
NELPRDATPM DIEPNQQNHH ESAFKPQESN NHSGYEEDED TLKREHAEED ERPPSLCILN
KEAPLPLLQY KRRRQNESNN NSSRNTQDHC SSTITTVDNT TTLISSSAAA ATNTAISALL
EFSLMGISDK KENQQKEETS PPSPIASPEE KVNDLQKEVH QMSVERETFK LEMMSAEAMI
SILQSRIDAL RQENEELKKK NASGQAS
