NAC78_ARATH
ID NAC78_ARATH Reviewed; 567 AA.
AC Q84K00; Q84UG1; Q9LZ84; Q9SNW1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=NAC domain-containing protein 78 {ECO:0000303|PubMed:15029955};
DE Short=ANAC078 {ECO:0000303|PubMed:15029955};
DE AltName: Full=Protein NTM1-like 11 {ECO:0000303|PubMed:17158162};
GN Name=NAC078;
GN Synonyms=NAC2 {ECO:0000312|EMBL:AED90739.1},
GN NTL11 {ECO:0000303|PubMed:17158162}; OrderedLocusNames=At5g04410;
GN ORFNames=T32M21.10;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RA Colgan D.F., Xi Q., Chua N.-H.;
RT "NAC2 is highly expressed in root meristem.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 [GENOMIC DNA] OF 178-535, AND VARIANT ASP-393.
RC STRAIN=cv. Bla-1, cv. Bretagny, cv. Bs-1, cv. Bu-0, cv. Chi-1, cv. Hau-0,
RC cv. Jl-1, cv. Kent, and cv. Lisse;
RX PubMed=12618409; DOI=10.1093/genetics/163.2.723;
RA Barrier M., Bustamante C.D., Yu J., Purugganan M.D.;
RT "Selection on rapidly evolving proteins in the Arabidopsis genome.";
RL Genetics 163:723-733(2003).
RN [6]
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 [7]
RP GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17158162; DOI=10.1093/nar/gkl1068;
RA Kim S.Y., Kim S.G., Kim Y.S., Seo P.J., Bae M., Yoon H.K., Park C.M.;
RT "Exploring membrane-associated NAC transcription factors in Arabidopsis:
RT implications for membrane biology in genome regulation.";
RL Nucleic Acids Res. 35:203-213(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HIGH LIGHT, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19887540; DOI=10.1093/pcp/pcp159;
RA Morishita T., Kojima Y., Maruta T., Nishizawa-Yokoi A., Yabuta Y.,
RA Shigeoka S.;
RT "Arabidopsis NAC transcription factor, ANAC078, regulates flavonoid
RT biosynthesis under high-light.";
RL Plant Cell Physiol. 50:2210-2222(2009).
RN [9]
RP FUNCTION.
RX PubMed=21889048; DOI=10.1016/j.plantsci.2011.07.001;
RA Yabuta Y., Osada R., Morishita T., Nishizawa-Yokoi A., Tamoi M., Maruta T.,
RA Shigeoka S.;
RT "Involvement of Arabidopsis NAC transcription factor in the regulation of
RT 20S and 26S proteasomes.";
RL Plant Sci. 181:421-427(2011).
CC -!- FUNCTION: Transcriptional activator activated by proteolytic cleavage
CC through regulated intramembrane proteolysis (RIP) (By similarity).
CC Transcripition activator associated with the induction of genes related
CC to flavonoid biosynthesis and required for the accumulation of
CC anthocyanins in response to high light stress (PubMed:19887540). Plays
CC a role in the regulation of 20S and 26S proteasomes in response to high
CC light stress (PubMed:21889048). {ECO:0000250|UniProtKB:Q949N0,
CC ECO:0000269|PubMed:19887540, ECO:0000269|PubMed:21889048}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q949N0}; Single-
CC pass membrane protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00353, ECO:0000269|PubMed:19887540}. Note=Localized
CC primarily in plasma membrane or endoplasmic reticulum membrane as
CC dormant form and, upon specific stress or signal, is processed into a
CC transcriptionally active and nuclear form after a proteolytic cleavage
CC through regulated intramembrane proteolysis (RIP).
CC {ECO:0000250|UniProtKB:Q949N0}.
CC -!- TISSUE SPECIFICITY: Expressed in root meristem (Ref.1). Expressed in
CC roots, rosette leaves, cauline leaves, shoot apex, stems and flowers
CC (PubMed:17158162). {ECO:0000269|PubMed:17158162, ECO:0000269|Ref.1}.
CC -!- INDUCTION: By exposure to high light (PubMed:19887540). Induced by heat
CC and methyl methanesulfonate (MMS) treatment (PubMed:17158162).
CC {ECO:0000269|PubMed:17158162, ECO:0000269|PubMed:19887540}.
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 under normal growth
CC conditions. {ECO:0000269|PubMed:19887540}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF09254.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF201456; AAF09254.1; ALT_FRAME; mRNA.
DR EMBL; AL162875; CAB85547.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90739.1; -; Genomic_DNA.
DR EMBL; AY099609; AAM20460.1; -; mRNA.
DR EMBL; AY128859; AAM91259.1; -; mRNA.
DR EMBL; AY140474; AAN46238.1; -; Genomic_DNA.
DR EMBL; AY140475; AAN46239.1; -; Genomic_DNA.
DR EMBL; AY140476; AAN46240.1; -; Genomic_DNA.
DR EMBL; AY140477; AAN46241.1; -; Genomic_DNA.
DR EMBL; AY140478; AAN46242.1; -; Genomic_DNA.
DR EMBL; AY140479; AAN46243.1; -; Genomic_DNA.
DR EMBL; AY140480; AAN46244.1; -; Genomic_DNA.
DR EMBL; AY140481; AAN46245.1; -; Genomic_DNA.
DR EMBL; AY140482; AAN46246.1; -; Genomic_DNA.
DR PIR; T48437; T48437.
DR RefSeq; NP_196061.1; NM_120523.4.
DR AlphaFoldDB; Q84K00; -.
DR SMR; Q84K00; -.
DR BioGRID; 15599; 1.
DR STRING; 3702.AT5G04410.1; -.
DR PaxDb; Q84K00; -.
DR PRIDE; Q84K00; -.
DR ProteomicsDB; 251228; -.
DR EnsemblPlants; AT5G04410.1; AT5G04410.1; AT5G04410.
DR GeneID; 830320; -.
DR Gramene; AT5G04410.1; AT5G04410.1; AT5G04410.
DR KEGG; ath:AT5G04410; -.
DR Araport; AT5G04410; -.
DR TAIR; locus:2184342; AT5G04410.
DR eggNOG; ENOG502QTKI; Eukaryota.
DR HOGENOM; CLU_032008_1_0_1; -.
DR InParanoid; Q84K00; -.
DR OMA; QIGCGVQ; -.
DR OrthoDB; 416063at2759; -.
DR PhylomeDB; Q84K00; -.
DR PRO; PR:Q84K00; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84K00; baseline and differential.
DR Genevisible; Q84K00; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009962; P:regulation of flavonoid biosynthetic process; IMP:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
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 Activator; DNA-binding; Membrane; Nucleus; Reference proteome;
KW Stress response; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..567
FT /note="NAC domain-containing protein 78"
FT /id="PRO_0000132314"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 9..159
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 108..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 393..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 393
FT /note="N -> D"
FT /evidence="ECO:0000269|PubMed:12618409"
FT CONFLICT 7
FT /note="T -> A (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..108
FT /note="VV -> IL (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="R -> K (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="H -> Q (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="G -> V (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="D -> E (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..398
FT /note="QEALD -> PETLE (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="L -> M (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="G -> R (in Ref. 1; AAF09254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 567 AA; 63511 MW; 05EB16AB22AEDFDE CRC64;
MGRGSVTSLA PGFRFHPTDE ELVRYYLKRK VCNKPFKFDA ISVTDIYKSE PWDLPDKSKL
KSRDLEWYFF SMLDKKYSNG SKTNRATEKG YWKTTGKDRE IRNGSRVVGM KKTLVYHKGR
APRGERTNWV MHEYRLSDED LKKAGVPQEA YVLCRIFQKS GTGPKNGEQY GAPYLEEEWE
EDGMTYVPAQ DAFSEGLALN DDVYVDIDDI DEKPENLVVY DAVPILPNYC HGESSNNVES
GNYSDSGNYI QPGNNVVDSG GYFEQPIETF EEDRKPIIRE GSIQPCSLFP EEQIGCGVQD
ENVVNLESSN NNVFVADTCY SDIPIDHNYL PDEPFMDPNN NLPLNDGLYL ETNDLSCAQQ
DDFNFEDYLS FFDDEGLTFD DSLLMGPEDF LPNQEALDQK PAPKELEKEV AGGKEAVEEK
ESGEGSSSKQ DTDFKDFDSA PKYPFLKKTS HMLGAIPTPS SFASQFQTKD AMRLHAAQSS
GSVHVTAGMM RISNMTLAAD SGMGWSYDKN GNLNVVLSFG VVQQDDAMTA SGSKTGITAT
RAMLVFMCLW VLLLSVSFKI VTMVSAR
