NAC69_ARATH
ID NAC69_ARATH Reviewed; 457 AA.
AC Q9M126; A8MRW7; O82590;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=NAC domain-containing protein 69 {ECO:0000303|PubMed:15029955};
DE Short=ANAC069 {ECO:0000303|PubMed:15029955};
DE AltName: Full=Protein NAC WITH TRANSMEMBRANE MOTIF 2;
DE AltName: Full=Protein NTM1-like 13 {ECO:0000303|PubMed:17158162};
GN Name=NAC69; Synonyms=NTL13 {ECO:0000303|PubMed:17158162}, NTM2;
GN OrderedLocusNames=At4g01550; ORFNames=F11O4.5;
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=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 [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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 GENE FAMILY.
RX PubMed=17098812; DOI=10.1105/tpc.106.043018;
RA Kim Y.-S., Kim S.-G., Park J.-E., Park H.-Y., Lim M.-H., Chua N.-H.,
RA Park C.-M.;
RT "A membrane-bound NAC transcription factor regulates cell division in
RT Arabidopsis.";
RL Plant Cell 18:3132-3144(2006).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21450938; DOI=10.1104/pp.111.177071;
RA Park J., Kim Y.S., Kim S.G., Jung J.H., Woo J.C., Park C.M.;
RT "Integration of auxin and salt signals by the NAC transcription factor NTM2
RT during seed germination in Arabidopsis.";
RL Plant Physiol. 156:537-549(2011).
CC -!- FUNCTION: Transcription activator activated by proteolytic cleavage
CC through regulated intramembrane proteolysis (RIP). Involved in salt
CC stress response during seed germination and seedling growth. Binds the
CC auxin-responsive IAA30 gene promoter and may serve as a molecular link
CC that interconnects a developmental feedback loop of auxin signaling
CC with a salt signal transduction pathway during seed germination
CC (PubMed:21450938). {ECO:0000269|PubMed:21450938}.
CC -!- INTERACTION:
CC Q9M126; Q9FLM0: NAC095; NbExp=3; IntAct=EBI-15191931, EBI-15191933;
CC Q9M126; Q9FI23: PDF1.2A; NbExp=3; IntAct=EBI-15191931, EBI-25516740;
CC Q9M126; Q9FPW6: POB1; NbExp=3; IntAct=EBI-15191931, EBI-15194725;
CC Q9M126; Q9LVI4: TIFY6B; NbExp=3; IntAct=EBI-15191931, EBI-1792431;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:21450938}; Single-
CC pass membrane protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00353, ECO:0000269|PubMed:21450938}. 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:0000269|PubMed:21450938}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9M126-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M126-2; Sequence=VSP_032053;
CC Name=3;
CC IsoId=Q9M126-3; Sequence=VSP_032054, VSP_032055;
CC -!- INDUCTION: By salt stress and abscisic acid (ABA) in roots.
CC {ECO:0000269|PubMed:21450938}.
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, but mutant plants mutant exhibit reduced sensitivity to
CC high salinity during seed germination and seedling development.
CC {ECO:0000269|PubMed:21450938}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62781.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF096370; AAC62781.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161492; CAB77725.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82040.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82041.1; -; Genomic_DNA.
DR EMBL; AK229312; BAF01175.1; -; mRNA.
DR PIR; B85020; B85020.
DR PIR; T01939; T01939.
DR RefSeq; NP_001078344.1; NM_001084875.1. [Q9M126-2]
DR RefSeq; NP_192064.1; NM_116385.4. [Q9M126-1]
DR AlphaFoldDB; Q9M126; -.
DR SMR; Q9M126; -.
DR BioGRID; 13433; 8.
DR IntAct; Q9M126; 7.
DR STRING; 3702.AT4G01550.1; -.
DR PaxDb; Q9M126; -.
DR PRIDE; Q9M126; -.
DR ProteomicsDB; 251283; -. [Q9M126-1]
DR EnsemblPlants; AT4G01550.1; AT4G01550.1; AT4G01550. [Q9M126-1]
DR EnsemblPlants; AT4G01550.2; AT4G01550.2; AT4G01550. [Q9M126-2]
DR GeneID; 828144; -.
DR Gramene; AT4G01550.1; AT4G01550.1; AT4G01550. [Q9M126-1]
DR Gramene; AT4G01550.2; AT4G01550.2; AT4G01550. [Q9M126-2]
DR KEGG; ath:AT4G01550; -.
DR Araport; AT4G01550; -.
DR TAIR; locus:2116982; AT4G01550.
DR eggNOG; ENOG502SPZ5; Eukaryota.
DR HOGENOM; CLU_035664_16_1_1; -.
DR InParanoid; Q9M126; -.
DR OMA; RENQSNH; -.
DR OrthoDB; 893230at2759; -.
DR PhylomeDB; Q9M126; -.
DR PRO; PR:Q9M126; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M126; baseline and differential.
DR Genevisible; Q9M126; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; 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 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; Alternative splicing; DNA-binding; Membrane; Nucleus;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..457
FT /note="NAC domain-containing protein 69"
FT /id="PRO_0000323715"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 4..153
FT /note="NAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT DNA_BIND 107..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00353"
FT REGION 158..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_032053"
FT VAR_SEQ 60
FT /note="D -> DPVWYFFCPKEYTSAKKKVKDLVGYRFYPTGEELINHYLKNKILALS
FT KIKSDD (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_032054"
FT VAR_SEQ 314..436
FT /note="SYQGTSSPGDDSVGSSNRQFLQTGGDEILSSCNDLQTYGEPSISSSTRQSQL
FT TRSIIRPKQEVKQDTSRAVDSDTSIDKESSMVKTEKKSWFITEEAMERNRNNPRYIYLM
FT RMIIGFILLLAL -> VKQITRFLYRYFCAVISILTF (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_032055"
SQ SEQUENCE 457 AA; 51816 MW; 9CBBCE615F0538B3 CRC64;
MVKDLVGYRF YPTGEELINH YLKNKILGKT WLVDEAISEI NICSYDPIYL PSLSKIKSDD
PVWYFFCPKE YTSAKKKVTK RTTSSGYWKA TGVDRKIKDK RGNRGEIGIK KTLVYYEGRV
PKGVWTPWVM HEYHITCLPQ DQRNYVICQV MYKGEDGDVP SGGNNSSEPS QSLVSDSNTV
RATSPTALEF EKPGQENFFG MSVDDLGTPK NEQEDFSLWD VLDPDMLFSD NNNPTVHPQA
PHLTPNDDEF LGGLRHVNRE QVEYLFANED FISRPTLSMT ENRNDHRPKK ALSGIIVDYS
SDSNSDAESI SATSYQGTSS PGDDSVGSSN RQFLQTGGDE ILSSCNDLQT YGEPSISSST
RQSQLTRSII RPKQEVKQDT SRAVDSDTSI DKESSMVKTE KKSWFITEEA MERNRNNPRY
IYLMRMIIGF ILLLALISNI ISVLQNLNPA MKFDRER
