NAC92_ARATH
ID NAC92_ARATH Reviewed; 285 AA.
AC Q9FKA0; Q8LFU6;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=NAC domain-containing protein 92 {ECO:0000303|PubMed:15029955};
DE Short=ANAC092 {ECO:0000303|PubMed:15029955};
DE Short=AtNAC2 {ECO:0000303|PubMed:16359384};
DE Short=AtNAC6 {ECO:0000303|PubMed:21511905};
DE AltName: Full=Protein ORESARA 1 {ECO:0000303|PubMed:9351240};
GN Name=NAC92 {ECO:0000303|PubMed:15029955};
GN Synonyms=NAC2 {ECO:0000303|PubMed:16359384},
GN NAC6 {ECO:0000303|PubMed:21511905}, ORE1 {ECO:0000303|PubMed:9351240};
GN OrderedLocusNames=At5g39610 {ECO:0000312|Araport:AT5G39610};
GN ORFNames=MIJ24.11 {ECO:0000312|EMBL:BAB08893.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY SALT STRESS; ABSCISIC ACID;
RP ETHYLENE AND AUXIN, SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE,
RP HOMODIMERIZATION, SUBUNIT, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16359384; DOI=10.1111/j.1365-313x.2005.02575.x;
RA He X.-J., Mu R.-L., Cao W.-H., Zhang Z.-G., Zhang J.-S., Chen S.-Y.;
RT "AtNAC2, a transcription factor downstream of ethylene and auxin signaling
RT pathways, is involved in salt stress response and lateral root
RT development.";
RL Plant J. 44:903-916(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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].
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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9351240; DOI=10.1111/j.0960-7412.1997.00527.x;
RA Oh S.A., Park J.-H., Lee G.I., Paek K.H., Park S.K., Nam H.G.;
RT "Identification of three genetic loci controlling leaf senescence in
RT Arabidopsis thaliana.";
RL Plant J. 12:527-535(1997).
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15295076; DOI=10.1093/pcp/pch110;
RA Woo H.R., Kim J.H., Nam H.G., Lim P.O.;
RT "The delayed leaf senescence mutants of Arabidopsis, ore1, ore3, and ore9
RT are tolerant to oxidative stress.";
RL Plant Cell Physiol. 45:923-932(2004).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY AGE-RELATED RESISTANCE.
RC STRAIN=cv. Columbia;
RX PubMed=19694953; DOI=10.1111/j.1364-3703.2009.00557.x;
RA Carviel J.L., Al-Daoud F., Neumann M., Mohammad A., Provart N.J.,
RA Moeder W., Yoshioka K., Cameron R.K.;
RT "Forward and reverse genetics to identify genes involved in the age-related
RT resistance response in Arabidopsis thaliana.";
RL Mol. Plant Pathol. 10:621-634(2009).
RN [10]
RP INDUCTION BY SALT AND ETHYLENE.
RX PubMed=19608714; DOI=10.1093/pcp/pcp107;
RA Chen T., Liu J., Lei G., Liu Y.-F., Li Z.-G., Tao J.-J., Hao Y.-J.,
RA Cao Y.-R., Lin Q., Zhang W.-K., Ma B., Chen S.-Y., Zhang J.-S.;
RT "Effects of tobacco ethylene receptor mutations on receptor kinase
RT activity, plant growth and stress responses.";
RL Plant Cell Physiol. 50:1636-1650(2009).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND INDUCTION BY
RP MIR164 AND SENESCENCE.
RX PubMed=19229035; DOI=10.1126/science.1166386;
RA Kim J.H., Woo H.R., Kim J., Lim P.O., Lee I.C., Choi S.H., Hwang D.,
RA Nam H.G.;
RT "Trifurcate feed-forward regulation of age-dependent cell death involving
RT miR164 in Arabidopsis.";
RL Science 323:1053-1057(2009).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALT STRESS AND SENESCENCE,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=20113437; DOI=10.1111/j.1365-313x.2010.04151.x;
RA Balazadeh S., Siddiqui H., Allu A.D., Matallana-Ramirez L.P., Caldana C.,
RA Mehrnia M., Zanor M.I., Koehler B., Mueller-Roeber B.;
RT "A gene regulatory network controlled by the NAC transcription factor
RT ANAC092/AtNAC2/ORE1 during salt-promoted senescence.";
RL Plant J. 62:250-264(2010).
RN [13]
RP INDUCTION BY SALT AND H2O2.
RX PubMed=20404534; DOI=10.4161/psb.5.6.11694;
RA Balazadeh S., Wu A., Mueller-Roeber B.;
RT "Salt-triggered expression of the ANAC092-dependent senescence regulon in
RT Arabidopsis thaliana.";
RL Plant Signal. Behav. 5:733-735(2010).
RN [14]
RP INDUCTION BY AUXIN AND SENESCENCE.
RX PubMed=21511905; DOI=10.1093/jxb/err094;
RA Kim J.I., Murphy A.S., Baek D., Lee S.-W., Yun D.-J., Bressan R.A.,
RA Narasimhan M.L.;
RT "YUCCA6 over-expression demonstrates auxin function in delaying leaf
RT senescence in Arabidopsis thaliana.";
RL J. Exp. Bot. 62:3981-3992(2011).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21303842; DOI=10.1093/mp/ssq080;
RA Balazadeh S., Kwasniewski M., Caldana C., Mehrnia M., Zanor M.I.,
RA Xue G.-P., Mueller-Roeber B.;
RT "ORS1, an H(2)O(2)-responsive NAC transcription factor, controls senescence
RT in Arabidopsis thaliana.";
RL Mol. Plant 4:346-360(2011).
RN [16]
RP INDUCTION BY SENESCENCE.
RX PubMed=22930749; DOI=10.1104/pp.112.203083;
RA Trivellini A., Jibran R., Watson L.M., O'Donoghue E.M., Ferrante A.,
RA Sullivan K.L., Dijkwel P.P., Hunter D.A.;
RT "Carbon deprivation-driven transcriptome reprogramming in detached
RT developmentally arresting Arabidopsis inflorescences.";
RL Plant Physiol. 160:1357-1372(2012).
RN [17]
RP FUNCTION, INTERACTION WITH GLK1 AND GLK2, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23459204; DOI=10.1038/embor.2013.24;
RA Rauf M., Arif M., Dortay H., Matallana-Ramirez L.P., Waters M.T.,
RA Gil Nam H., Lim P.-O., Mueller-Roeber B., Balazadeh S.;
RT "ORE1 balances leaf senescence against maintenance by antagonizing G2-like-
RT mediated transcription.";
RL EMBO Rep. 14:382-388(2013).
RN [18]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=23340744; DOI=10.1093/mp/sst012;
RA Matallana-Ramirez L.P., Rauf M., Farage-Barhom S., Dortay H., Xue G.-P.,
RA Droege-Laser W., Lers A., Balazadeh S., Mueller-Roeber B.;
RT "NAC transcription factor ORE1 and senescence-induced BIFUNCTIONAL
RT NUCLEASE1 (BFN1) constitute a regulatory cascade in Arabidopsis.";
RL Mol. Plant 6:1438-1452(2013).
CC -!- FUNCTION: Transcription activator that binds to DNA in promoters of
CC target genes on a specific bipartite motif 5'-[ACG][CA]GT[AG](5-
CC 6n)[CT]AC[AG]-3' (PubMed:23340744). Promotes lateral root development
CC (PubMed:16359384). Triggers the expression of senescence-associated
CC genes during age-, salt- and dark-induced senescence through a
CC regulatory network that may involve cross-talk with salt- and H(2)O(2)-
CC dependent signaling pathways (PubMed:9351240, PubMed:15295076,
CC PubMed:20113437, PubMed:21303842). Regulates also genes during seed
CC germination (PubMed:20113437). Regulates positively aging-induced cell
CC death (PubMed:19229035). Involved in age-related resistance (ARR)
CC against Pseudomonas syringae pv. tomato and Hyaloperonospora
CC arabidopsidis (PubMed:19694953). Antagonizes GLK1 and GLK2
CC transcriptional activity, shifting the balance from chloroplast
CC maintenance towards deterioration during leaf senescence
CC (PubMed:23459204). Promotes the expression of senescence-associated
CC genes, including ENDO1/BFN1, SWEET15/SAG29 and SINA1/At3g13672, during
CC senescence onset (PubMed:23340744). {ECO:0000269|PubMed:15295076,
CC ECO:0000269|PubMed:16359384, ECO:0000269|PubMed:19229035,
CC ECO:0000269|PubMed:19694953, ECO:0000269|PubMed:20113437,
CC ECO:0000269|PubMed:21303842, ECO:0000269|PubMed:23340744,
CC ECO:0000269|PubMed:23459204, ECO:0000269|PubMed:9351240}.
CC -!- SUBUNIT: Forms homodimers (PubMed:16359384). Interacts with GLK1 and
CC GLK2 (PubMed:23459204). {ECO:0000269|PubMed:16359384,
CC ECO:0000269|PubMed:23459204}.
CC -!- INTERACTION:
CC Q9FKA0; Q9FFH0: GLK2; NbExp=6; IntAct=EBI-6862413, EBI-6862475;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16359384,
CC ECO:0000269|PubMed:23459204}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and flowers, and, to a
CC lower extent, in shoots and leaves. Particularly expressed in old and
CC senescing tissues. {ECO:0000269|PubMed:16359384,
CC ECO:0000269|PubMed:20113437, ECO:0000269|PubMed:23340744}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during leaf and flower aging
CC (PubMed:20113437). Induced by EIN2 during leaf aging, but negatively
CC regulated by miR164, which expression decreases gradually with aging
CC through negative regulation by EIN2 (PubMed:19229035). In leaves,
CC accumulates at the tips and margins and in leaves undergoing
CC senescence. Present in floral organs of partly or fully opened flowers,
CC but not in young flower buds. Expressed in pollen grains of mature
CC anthers, but not in immature anthers. In petals of open flowers mostly
CC observed in the tip region. In mature siliques, accumulates at the
CC abscission zone, in the distal portion of the valve margins and the
CC tip. In roots, detected in primary and lateral roots, but not in root
CC tips. In seeds present in embryos and the micropylar endosperm
CC (PubMed:20113437, PubMed:23340744). {ECO:0000269|PubMed:19229035,
CC ECO:0000269|PubMed:20113437, ECO:0000269|PubMed:23340744}.
CC -!- INDUCTION: High levels during senescence (e.g. age-, salt- and dark-
CC related) (PubMed:19229035, PubMed:20113437, PubMed:21511905,
CC PubMed:22930749). By salt stress in an ethylene- and auxin-dependent
CC manner (PubMed:16359384, PubMed:19608714, PubMed:20113437,
CC PubMed:20404534). Induced by H(2)O(2) (PubMed:20404534). Accumulates in
CC response to abscisic acid (ABA), ethylene (ACC) and auxin (NAA)
CC (PubMed:16359384, PubMed:19608714). Repressed by high auxin (IAA)
CC levels (PubMed:21511905). Age-related resistance (ARR)-associated
CC accumulation (PubMed:19694953). Repressed by miR164 (PubMed:19229035).
CC {ECO:0000269|PubMed:16359384, ECO:0000269|PubMed:19229035,
CC ECO:0000269|PubMed:19608714, ECO:0000269|PubMed:19694953,
CC ECO:0000269|PubMed:20113437, ECO:0000269|PubMed:20404534,
CC ECO:0000269|PubMed:21511905, ECO:0000269|PubMed:22930749}.
CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization
CC domain. {ECO:0000255|PROSITE-ProRule:PRU00353}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:16359384). Delayed
CC leaf senescence and flowering (PubMed:9351240, PubMed:19229035,
CC PubMed:20113437, PubMed:21303842). Increased tolerance to various types
CC of oxidative stress including H(2)O(2), salicylhydroxamic acid (SHAM),
CC N,N-diethyldithio carbamic acid (DDC) and methyl viologen (MV)
CC (PubMed:15295076). Impaired age-related resistance (ARR) against
CC Pseudomonas syringae pv. tomato and Hyaloperonospora arabidopsidis
CC (PubMed:19694953). Increased seed germination rate under saline
CC conditions and delay of salinity-induced chlorophyll loss in leaves
CC (PubMed:20113437). {ECO:0000269|PubMed:15295076,
CC ECO:0000269|PubMed:16359384, ECO:0000269|PubMed:19229035,
CC ECO:0000269|PubMed:19694953, ECO:0000269|PubMed:20113437,
CC ECO:0000269|PubMed:21303842, ECO:0000269|PubMed:9351240}.
CC -!- MISCELLANEOUS: 'Oresara' means long-living in Korean.
CC {ECO:0000305|PubMed:9351240}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61198.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY174163; AAO41710.1; -; mRNA.
DR EMBL; AB012243; BAB08893.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94454.1; -; Genomic_DNA.
DR EMBL; AY056327; AAL07176.1; -; mRNA.
DR EMBL; AY091191; AAM14130.1; -; mRNA.
DR EMBL; AY084635; AAM61198.1; ALT_INIT; mRNA.
DR RefSeq; NP_198777.1; NM_123323.3.
DR AlphaFoldDB; Q9FKA0; -.
DR SMR; Q9FKA0; -.
DR IntAct; Q9FKA0; 3.
DR MINT; Q9FKA0; -.
DR STRING; 3702.AT5G39610.1; -.
DR PaxDb; Q9FKA0; -.
DR PRIDE; Q9FKA0; -.
DR ProteomicsDB; 250992; -.
DR DNASU; 833957; -.
DR EnsemblPlants; AT5G39610.1; AT5G39610.1; AT5G39610.
DR GeneID; 833957; -.
DR Gramene; AT5G39610.1; AT5G39610.1; AT5G39610.
DR KEGG; ath:AT5G39610; -.
DR Araport; AT5G39610; -.
DR TAIR; locus:2164895; AT5G39610.
DR eggNOG; ENOG502QR2M; Eukaryota.
DR HOGENOM; CLU_035664_5_2_1; -.
DR InParanoid; Q9FKA0; -.
DR OMA; FCATAIG; -.
DR OrthoDB; 1072945at2759; -.
DR PhylomeDB; Q9FKA0; -.
DR PRO; PR:Q9FKA0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKA0; baseline and differential.
DR Genevisible; Q9FKA0; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0080187; P:floral organ senescence; IMP:TAIR.
DR GO; GO:0048527; P:lateral root development; IMP:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:1904250; P:positive regulation of age-related resistance; IMP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:1900057; P:positive regulation of leaf senescence; IMP:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0010029; P:regulation of seed germination; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0090400; P:stress-induced premature senescence; 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 Activator; Apoptosis; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..285
FT /note="NAC domain-containing protein 92"
FT /id="PRO_0000433472"
FT DOMAIN 20..170
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 117..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
SQ SEQUENCE 285 AA; 32984 MW; 49F7141B5FB44509 CRC64;
MDYEASRIVE MVEDEEHIDL PPGFRFHPTD EELITHYLKP KVFNTFFSAT AIGEVDLNKI
EPWDLPWKAK MGEKEWYFFC VRDRKYPTGL RTNRATEAGY WKATGKDKEI FKGKSLVGMK
KTLVFYKGRA PKGVKTNWVM HEYRLEGKYC IENLPQTAKN EWVICRVFQK RADGTKVPMS
MLDPHINRME PAGLPSLMDC SQRDSFTGSS SHVTCFSDQE TEDKRLVHES KDGFGSLFYS
DPLFLQDNYS LMKLLLDGQE TQFSGKPFDG RDSSGTEELD CVWNF
