NAC72_ARATH
ID NAC72_ARATH Reviewed; 297 AA.
AC Q93VY3; Q8H141; Q94II4; Q9SZR8;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=NAC domain-containing protein 72 {ECO:0000303|PubMed:15029955};
DE Short=ANAC072 {ECO:0000303|PubMed:15029955};
DE AltName: Full=Protein RESPONSIVE TO DESICCATION 26 {ECO:0000303|PubMed:15319476};
GN Name=NAC072 {ECO:0000303|PubMed:15029955};
GN Synonyms=RD26 {ECO:0000303|PubMed:15319476};
GN OrderedLocusNames=At4g27410 {ECO:0000312|Araport:AT4G27410};
GN ORFNames=F27G19.10 {ECO:0000312|EMBL:CAB43873.1};
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 [MRNA] (ISOFORM 2).
RA Shinozaki K., Yamaguchi-shinozaki K., Takahashi S.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP INDUCTION BY DROUGHT.
RA Yamaguchi-Shinozaki K., Koizumi M., Urao S., Shinozaki K.;
RT "Molecular cloning and characterization of 9 cDNAs for genes that are
RT responsive to desiccation in Arabidopsis thaliana: sequence analysis of one
RT cDNA clone that encodes a putative transmembrane channel protein.";
RL Plant Cell Physiol. 33:217-224(1992).
RN [8]
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 [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15319476; DOI=10.1105/tpc.104.022699;
RA Tran L.-S.H., Nakashima K., Sakuma Y., Simpson S.D., Fujita Y.,
RA Maruyama K., Fujita M., Seki M., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Isolation and functional analysis of Arabidopsis stress-inducible NAC
RT transcription factors that bind to a drought-responsive cis-element in the
RT early responsive to dehydration stress 1 promoter.";
RL Plant Cell 16:2481-2498(2004).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16581911; DOI=10.1073/pnas.0510607103;
RA Lee J.-Y., Colinas J., Wang J.Y., Mace D., Ohler U., Benfey P.N.;
RT "Transcriptional and posttranscriptional regulation of transcription factor
RT expression in Arabidopsis roots.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6055-6060(2006).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=29659022; DOI=10.1111/nph.15127;
RA Kamranfar I., Xue G.-P., Tohge T., Sedaghatmehr M., Fernie A.R.,
RA Balazadeh S., Mueller-Roeber B.;
RT "Transcription factor RD26 is a key regulator of metabolic reprogramming
RT during dark-induced senescence.";
RL New Phytol. 218:1543-1557(2018).
CC -!- FUNCTION: Transcription factors that bind specifically to the 5'-
CC CATGTG-3' motif and with bipartite regions with 5'-CGTr-3' and 5'-YACG-
CC 3' as cores (PubMed:15319476, PubMed:29659022). Involved in the
CC regulation of metabolic reprogramming during senescence by promoting
CC the chloroplast protein degradation and the catabolism of lysine,
CC phytol and free fatty acids via the induction of CV, LKR/SDH and PES1
CC expression (PubMed:29659022). Triggers also the degradation of starch
CC and the accumulation of mono- and disaccharides during senescence by
CC enhancing the expression of AMY1, SFP1 and SWEET15 (PubMed:29659022).
CC {ECO:0000269|PubMed:15319476, ECO:0000269|PubMed:29659022}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353,
CC ECO:0000269|PubMed:16581911, ECO:0000269|PubMed:29659022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93VY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93VY3-2; Sequence=VSP_037405, VSP_037406;
CC -!- TISSUE SPECIFICITY: Expressed in leaves and in root pericycle and
CC epidermis. {ECO:0000269|PubMed:15319476, ECO:0000269|PubMed:16581911}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during senescence.
CC {ECO:0000269|PubMed:29659022}.
CC -!- INDUCTION: Strongly induced by drought, high salinity and abscisic acid
CC (ABA). Slightly up-regulated by cold treatment. Not induced by jasmonic
CC acid. {ECO:0000269|PubMed:15319476, ECO:0000269|Ref.7}.
CC -!- DOMAIN: The NAC domain includes a DNA-binding domain and a dimerization
CC domain.
CC -!- DISRUPTION PHENOTYPE: Delayed senescence (PubMed:29659022). Reduced
CC expression of genes involved in the degradation of starch and the
CC accumulation of mono- and disaccharides (e.g. AMY1, SFP1 and SWEET15)
CC as well as of genes implicated in chloroplast protein degradation and
CC in the catabolism of lysine, phytol and free fatty acids (e.g. CV,
CC LKR/SDH and PES1) (PubMed:29659022). {ECO:0000269|PubMed:29659022}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43873.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81391.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB039926; BAB63913.1; -; mRNA.
DR EMBL; AF083738; AAN60296.1; -; mRNA.
DR EMBL; AL078467; CAB43873.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161571; CAB81391.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85334.1; -; Genomic_DNA.
DR EMBL; AY057578; AAL09817.1; -; mRNA.
DR EMBL; AF428375; AAL16305.1; -; mRNA.
DR EMBL; AY091428; AAM14367.1; -; mRNA.
DR EMBL; BT000790; AAN31929.1; -; mRNA.
DR EMBL; AY087772; AAM65308.1; -; mRNA.
DR PIR; T08933; T08933.
DR RefSeq; NP_001078452.1; NM_001084983.1.
DR RefSeq; NP_567773.1; NM_118875.4. [Q93VY3-1]
DR AlphaFoldDB; Q93VY3; -.
DR SMR; Q93VY3; -.
DR BioGRID; 14136; 12.
DR IntAct; Q93VY3; 4.
DR STRING; 3702.AT4G27410.3; -.
DR PRIDE; Q93VY3; -.
DR EnsemblPlants; AT4G27410.2; AT4G27410.2; AT4G27410. [Q93VY3-1]
DR GeneID; 828849; -.
DR Gramene; AT4G27410.2; AT4G27410.2; AT4G27410. [Q93VY3-1]
DR KEGG; ath:AT4G27410; -.
DR Araport; AT4G27410; -.
DR eggNOG; ENOG502QRBC; Eukaryota.
DR HOGENOM; CLU_035664_8_4_1; -.
DR InParanoid; Q93VY3; -.
DR OrthoDB; 925823at2759; -.
DR PhylomeDB; Q93VY3; -.
DR PRO; PR:Q93VY3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93VY3; baseline and differential.
DR Genevisible; Q93VY3; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1900055; P:regulation of leaf senescence; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..297
FT /note="NAC domain-containing protein 72"
FT /id="PRO_0000376618"
FT DOMAIN 14..162
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 111..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 168..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037405"
FT VAR_SEQ 70..83
FT /note="WYFFSPRDRKYPNG -> MVFLKPKRSEISER (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037406"
FT CONFLICT 98
FT /note="T -> R (in Ref. 1; BAB63913)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="D -> G (in Ref. 5; AAN31929)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="I -> V (in Ref. 1; BAB63913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33177 MW; 7618A68331407370 CRC64;
MGVREKDPLA QLSLPPGFRF YPTDEELLVQ YLCRKVAGYH FSLQVIGDID LYKFDPWDLP
SKALFGEKEW YFFSPRDRKY PNGSRPNRVA GSGYWKATGT DKIITADGRR VGIKKALVFY
AGKAPKGTKT NWIMHEYRLI EHSRSHGSSK LDDWVLCRIY KKTSGSQRQA VTPVQACREE
HSTNGSSSSS SSQLDDVLDS FPEIKDQSFN LPRMNSLRTI LNGNFDWASL AGLNPIPELA
PTNGLPSYGG YDAFRAAEGE AESGHVNRQQ NSSGLTQSFG YSSSGFGVSG QTFEFRQ
